DE69133326T2 - Verbesserte humanähnlich gemachte immunglobuline - Google Patents

Verbesserte humanähnlich gemachte immunglobuline Download PDF

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DE69133326T2
DE69133326T2 DE69133326T DE69133326T DE69133326T2 DE 69133326 T2 DE69133326 T2 DE 69133326T2 DE 69133326 T DE69133326 T DE 69133326T DE 69133326 T DE69133326 T DE 69133326T DE 69133326 T2 DE69133326 T2 DE 69133326T2
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antibody
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immunoglobulin
antibodies
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L. Cary QUEEN
Sung Man CO
P. William SCHNEIDER
F. Nicholas LANDOLFI
L. Kathleen COELINGH
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AbbVie Biotherapeutics Inc
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Protein Design Labs Inc
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    • C07K16/464—Igs containing CDR-residues from one specie grafted between FR-residues from another
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Description

  • Erfindungsgebiet
  • Die vorliegende Erfindung bezieht sich im Allgemeinen auf die Kombination von Technologien rekombinanter DNA und monoklonaler Antikörper zur Entwicklung neuer therapeutischer Mittel und, insbesondere, auf die Herstellung nicht immunogener Antikörper mit einer starken Affinität für ein bestimmtes Antigen.
  • Hintergrund der Erfindung
  • Der Anfang der Technologie monoklonaler Antikörper Mitte der 1970-iger hat eine neue Ära in der Medizin eingeläutet. Zum erstenmal hatten Forscher und Kliniker Zugang zu im Wesentlichen unbegrenzten Mengen an einheitlichen Antikörpern, die in der Lage sind, an eine bestimmte Antigenstelle zu binden und die verschiedene immunologische Effektorfunktionen besitzen. Von diesen Proteinen, die als "monoklonale Antikörper" bekannt sind, wurde gelehrt, dass sie z. B. vielversprechend sind, um schädliche Zellen in vivo zu entfernen. Tatsächlich schien der klinische Wert monoklonaler Antikörper für diesen Zweck alleine grenzenlos zu sein.
  • Leider war die Entwicklung geeigneter therapeutischer Produkte basierend auf diesen Proteinen durch eine Anzahl von Nachteilen, die mit der Produktion monoklonaler Antikörper verbunden sind, stark erschwert. Z. B. sind die meisten monoklonalen Antikörper von der Maus abgeleitet und fixieren das humane Komplement nicht gut. Auch fehlen ihnen andere wichtige funktionelle Immunoglobulin-Charakteristika, wenn sie in Menschen verwendet werden.
  • Vielleicht ist es am wichtigsten, dass nicht humane monoklonale Antikörper wesentliche Aminosäure-Sequenz-Stücke enthalten, welche immunogen sind, wenn sie in einen Menschen injiziert werden. Zahlreiche Studien haben gezeigt, dass die Immunantwort, die nach der Injektion eines fremden Antikörpers in einem Patienten hervorgerufen wird, ziemlich stark sein kann, was die therapeutische Nützlichkeit des Antikörpers nach einer anfänglichen Behandlung im Wesentlichen beseitigt. Da erwartet werden kann, dass eine zunehmende Anzahl an verschiedenen Maus- oder anderen (gegenüber Menschen) antigenen monoklonalen Antikörpern zur Behandlung verschiedener Krankheiten entwickelt werden, können nach einer oder mehreren Behandlungen mit nicht humanen Antikörpern darüber hinaus darauffolgende Behandlungen, selbst für nicht damit im Zusammenhang stehende Therapien, aufgrund einer Kreuzreaktivität unwirksam oder sogar selbst gefährlich sein.
  • Während die Produktion sogenannter "chimärer Antikörper" (z. B. variable Regionen der Maus, die mit humanen konstanten Regionen verbunden sind) sich als teilweise erfolgreich erwiesen haben, verbleibt ein beträchtliches Problem hinsichtlich der Immunogenität. Darüber hinaus blieben Bemühungen, humane B-Zellen zu immortalisieren oder humane Hybridomen zu erzeugen, die in der Lage sind, humane Immunoglobuline gegen ein gewünschtes Antigen zu produzieren insbesondere bei vielen wichtigen humanen Antigenen im Allgemeinen erfolglos. Kürzlich wurde die rekombinante DNA-Technologie verwendet, um Immunoglobuline zu erzeugen, welche humane Framework-Regionen, kombiniert mit hypervariablen Regionen (complementarity determining regions = CDRs) von einem Donor-Maus- oder Ratten-Immunoglobulin aufweisen (siehe z. B. EPO-Veröffentlichung Nr. 0 239 400). Diese neuen Proteine werden "reshaped" oder "humanisierte" Immunoglobuline genannt, und das Verfahren, durch welches das Donor-Immunoglobulin in ein human-ähnliches Immunoglobulin umgewandelt wird, indem seine CDRs mit einem humanen Framework kombiniert werden, wird "Humanisierung" genannt. Humanisierte Antikörper sind wichtig, da sie an das gleiche Antigen binden, wie die ursprünglichen Antikörper, aber weniger immunogen sind, wenn sie in Menschen injiziert werden.
  • Jedoch bestand bei den Vorgehensweisen der Humanisierung ein Hauptproblem im Verlust der Affinität für das Antigen (Jones et al., Nature, 321, 522–525 (1986)), in manchen Fällen um das Zehnfache oder mehr, insbesondere wenn das Antigen ein Protein ist (Verhoeyen et al., Science, 239, 1534–1536 (1988)). Der Verlust jeglicher Affinität ist natürlich höchst unerwünscht. Es bedeutet zumindest, dass mehr von dem humanisierten Antikörper in den Patienten injiziert werden muss, was mit höheren Kosten und einem größeren Risiko für Nebenwirkungen verbunden ist. Noch kritischer ist, dass ein Antikörper mit verringerter Affinität schwächere biologische Funktionen wie Komplement-Lyse, Antikörper-abhängige zelluläre Cytotoxizität oder Virus-Neutralisation, besitzen kann. Z. B. kann der Verlust der Affinität in dem teilweise humanisierten Antikörper HuVHCAMP dazu geführt haben, dass er seine gesamte Fähigkeit zur Vermittlung der Komplement-Lyse verloren hat (siehe Riechmann et al., Nature, 332, 323–327 (1988); Tabelle 1).
  • Somit besteht ein Bedürfnis für humanisierte Antikörper, die insbesondere mit starker Affinität für bestimmte Antigene reaktiv sind. Diese humanisierten Immunoglobuline sollten im Wesentlichen nicht immunogen in Menschen bleiben, trotzdem leicht und ökonomisch auf ein solche einfache Weise hergestellt werden, die für eine therapeutische Formulierung und andere Verwendungen geeignet ist. Die vorliegende Erfindung erfüllt diese und andere Bedürfnisse.
  • Zusammenfassung der Erfindung
  • Die vorliegende Erfindung stellt ein humanisiertes Immunoglobulin bereit, worin die humanisierte variable Leichtketten-Region eine Sequenz umfasst, die in 1A (unten) gezeigt ist, und die humanisierte variable Schwerketten-Region eine Sequenz umfasst, die in 1B (unten) gezeigt ist. Das humanisierte Immunoglobulin ist z. B. bei der Behandlung von mit myeloider Leukämie verbundenen humanen Erkrankungen nützlich, wobei die humanisierten Immunoglobuline insbesondere in der Lage sind, an ein CD33-Antigen zu binden. Die Immunoglobuline können zwei Paare an Leichtketten/Schwerketten-Komplexen besitzen, wobei mindestens eine Kette die hypervariablen Regionen (complementarity determining regions) der Maus, welche mit Segmenten der humanen Framework-Region funktionell verbunden sind, umfasst. Z. B. können die hypervariablen Regionen (complementarity determining regions) von der Maus, mit oder ohne zusätzliche natürlich assoziierten Maus-Aminosäureresten, in humane Framework-Regionen eingeführt werden, um humanisierte Immunoglobuline zu erzeugen, die in der Lage sind, mit Affinitätsgraden an das CD33-Antigen zu binden, die stärker sind als ungefähr 107 M–1. Diese humanisierten Immunoglobuline werden auch in der Lage sein, das Binden des CDR-gebenden Maus-monoklonalen Antikörpers an CD33 zu blockieren. Diese humanisierten Immunoglobuline können alleine in im Wesentlichen reiner Form oder zusammen mit einem chemotherapeutischen Mittel wie Cytosinarabinosid oder Daunorubicin, welche gegen Leukämiezellen wirksam sind, oder komplexiert mit einem Radionuklid wie Iod-131, verwendet werden. Alle diese Verbindungen werden insbesondere nützlich sein, um Leukämie und Krankheiten zu behandeln, die durch Knochenmarkszellen vermittelt sind.
  • Die vorliegende Erfindung stellt auch die Verwendung des humanisierten Immunoglobulins bei der Herstellung eines Medikaments zur Behandlung myeloider Leukämie in einem Menschen bereit.
  • KURZE BESCHREIBUNG DER FIGUREN
  • 1. Aminosäure-Sequenzen (1-Buchstaben-Code) der variablen Regionen der leichten Kette (A) und schweren Kette (B) des Maus-M195-Antikörpers (obere Zeilen), verglichen mit dem humanisierten Antikörper (untere Zeilen), wobei die Signalsequenzen nicht enthalten sind. Die drei CDRs in jeder Kette sind unterstrichen. Die Reste in dem humanisierten Antikörper-Framework, die durch Maus-Aminosäuren oder typische humane Aminosäuren ersetzt sind, sind zweifach unterstrichen. Die Nummer an der ersten Position in jeder Zeile ist links angegeben.
  • 2. Schema für verankerte Polymerasekettenreaktion (PCR)-Klonierung der cDNAs für variable Domänen der schweren und leichten Kette. Die RNA wurde von ungefähr 107 Hybridoma-Zellen unter Verwendung des Heißphenolextraktionsverfahrens hergestellt. Kurz gesagt, wurden die Zellen resuspendiert und in 1 ml RNA-Extraktionspuffer (50 mM Natriumacetat pH 5,2/1% SDS) gemischt, mit 0,5 ml Phenol pH 5,2 bei 65°C für 15 min extrahiert, gefolgt von weiteren 15 min auf Eis. Die wässrige Phase wurde gewonnen und zweimal mit Ethanol präzipitiert. Die cDNA wurde aus 10 μg der gesamten RNA unter Verwendung von reverser Transkriptase (BRL, Betheseda, MD) und Oligo-dT12-18 (Pharmacia, Piscatway, New Jersey) als Primer synthetisiert. Ein Poly(dG)-Schwanz wurde unter Verwendung von terminaler Deoxynukleotidtransferase (BRL) an das 3'-Ende der cDNA angebracht (E. Y. Loh et al., Science 243, 217 (1989)), die Gene der variablen Domäne (V) wurden unter Verwendung von AmpIiTaq (Perkin Elmer-Cetus) mit dem Primer mc045 (TAATCTAGAATTCCCCCCCCCCCCCCCCC), welcher an die Poly(dG)-Schwänze hybridisiert, und Primern, die an die Gene der konstanten Region hybridisieren (C), amplifiziert. Der für die leichte Kette verwendete Primer war mc045 (TATAGAGCTCAAGCTTGGATGGTGGGAAGATGGATACAGTTGGTGC). Für die schwere Kette war der verwendete Primer mc047 (TATAGAGCTCAAGCTTCCAGTGGATAGAC(CAT)GATGGGG(GC)TGT(TC)G TTTTGGC).
  • Die Sequenz in Klammern zeigt eine Basendegeneration auf. Die Degeneration wurde so eingeführt, dass der Primer in der Lage sein würde, an die meisten Gamma-Ketten zu hybridisieren. Die amplifizierten Fragmente wurden dann mit EcoRI und Hind III verdaut und zur Sequenzierung in den pUC18-Vektor kloniert.
  • 3. Sequenzen der cDNA und translatierte Aminosäure-Sequenzen der variablen Regionen der leichten Kette (A) und schweren Kette (B) des Antikörpers M195. Die CDR-Sequenzen sind unterstrichen. Das reife Leichketten-Protein beginnt mit Aminosäure 21D und das reife Schwerketten-Protein mit Aminosäure 20E, gefolgt von den jeweiligen Signalsequenzen.
  • 4. Schematisches Diagramm der Plasmide pVgl-dhfr (A) und pVk (B). Das Plasmid pVgl-dhfr enthält die folgenden Teile: ein BamHI-EcoRI-Fragment mit ungefähr 4200 Basenpaaren, enthaltend die amp- und dhfr-Gene; ein 630-bp-Fragment enthaltend den humanen Cytomegalovirus IE1-Genpromotor und Enhancer (Boshart et al., Cell 41, 521 (1985)), an den 5'- und 3'-Enden durch EcoRI bzw. Xbal-Linker flankiert; und ein 2800 bp Xbal-BamHI-Fragment, enthaltend das Gen der humanen Gamma-1 konstanten Region mit 215 bp des darauffolgenden Introns und des Poly(A)-Signals. Das Plasmid pVk wurde ähnlich konstruiert, wobei ein Gen mit 1530 Basenpaaren die humane Kappakonstante Region das gamma-1-Gen und das gpt-Gen das dhfr-Gen ersetzt. Die Plasmide wurden aus den angegebenen Teilen unter Verwendung von im Fachgebiet wohlbekannten Verfahren konstruiert (s. Maniatis et al., Molecular Cloning: A Laboratory Manual, 2. Ausgabe, Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y. (1989), und PCT/89/01578, eingereicht am 13. April 1989. Z. B. wurde pVg1-dhfr aus dem Plasmid pVg1 durch Ersetzen des Hind III-Bgl II-Fragments, enthaltend das hyg-Gen, durch ein 660 bp-Fragment, enthaltend das dhfr-Gen und Verlängern an eine Bgl II-Stelle konstruiert (Simonsen et al., Proc. Natl. Acad. Sci. USA 80, 2495, 1983)).
  • 5. Fluorocytometrie von U937-Zellen, die mit (. .) keinem Antikörper, (...) humanisiertem M195-Antikörper, (---) chimärem M195-Antikörper angefärbt sind. Die Zellen wurden in FACS-Puffer (PBS + 2% FCS + 0,1% Azid) mit ungefähr 5 × 106/ml suspendiert. 100 μl der Zellsuspension wurden in ein Polystyrolröhrchen transferiert und mit 50 ng aufgereinigtem Antikörper auf Eis für 30 min inkubiert. Die Zellen wurden mit FACS-Puffer gewaschen und mit FITC-markiertem Ziegen-anti-humanem Ig-Antikörper auf Eis für weitere 30 min inkubiert. Die Zellen wurden wieder gewaschen und schließlich in PBS + 1 Paraformaldehyd resuspendiert. Die Zellen wurden auf einem FACSmate (Becton Dickinson) analysiert.
  • 6. Aminosäure-Sequenzen der leichten Kette (A) und der schweren Kette (B) des humanisierten M195-Antikörpers (untere Zeilen) und humanen Eu-Antikörpers (obere Zeilen), wobei die Signalsequenzen nicht enthalten sind. Die drei CDRs in jeder Kette sind unterstrichen. Die Reste in dem Framework, die in dem humanisierten Antikörper durch Maus-Aminosäuren ersetzt wurden, sind doppelt unterstrichen.
  • 7. Oligonukleotide, die bei der Konstruktion der schweren Kette des humanisierten M195 (A; ma1–4) und der leichten Kette (B; ma5–8) verwendet wurden. Die folgenden Paare an Oligonukleotiden wurden gemischt, mit Klenow-Polymerase verlängert und mit den angegebenen Enzymen vor der Ligation in pUC18 geschnitten: ma1 und ma2 mit Xba I und Kpn I, ma3 und ma4 mit Xba I und Kpn I, ma5 und ma6 mit Xba I und Hind III, ma7 und ma8 mit Xba I und Hind III. Dann wurden die ma1-ma2- und ma3-ma4-Fragmente mit Xba I und Kpn I von pUC18 ausgeschnitten und zusammen in die Xba I-Stelle von pVg1-dhfr ligiert; und die ma5-ma6- und ma7-ma8-Fragmente wurden mit Xba I und Hind III ausgeschnitten und in die Xba-I-Stelle von pVk zusammen ligiert.
  • 8. Kompetitives Binden von markiertem M195-Tracer an U937-Zellen. Ungefähr 4 × 105 U937-Zellen wurden mit 4,5 ng radio-iodiertem Maus-M195-Antikörper (6 μci/μg) und variierenden Mengen von entweder unmarkiertem Maus-M195-Antikörper (·) oder humanisiertem M195-Antikörper (°) in 200 μl Bindepuffer (PBS + 2% fötales Kälberserum + 0,1% Natriumazid) inkubiert. Nach Inkubation für 2 h bei 0°C wurden die Zellen zweimal mit Bindepuffer gewaschen und durch Zentrifugation gesammelt. Die an die Zellen gebundene Radioaktivität wurde gemessen und ist als Verhältnis von gebunden/frei cpm ausgedrückt.
  • DETAILLIERTE BESCHREIBUNG DER ERFINDUNG
  • Gemäß der vorliegenden Erfindung werden neue humanisierte Immunoglobuline bereitgestellt, die in der Lage sind, mit starker Affinität spezifisch an bestimmte CD33-Antigene zu binden. Diese Immunoglobuline sind in Menschen im Wesentlichen nicht immunogen, weisen aber Bindeaffinitäten von mindestens ungefähr 108 M–1, vorzugsweise 109 M–1 bis 1010 M–1 oder stärker auf. Die humanisierten Immunoglobuline besitzen ein humanes Framework und weisen hypervariable Regionen (complementarity determining regions = CDRs) und eine begrenzte Anzahl weiterer Aminosäuren von einem Donor-Immunoglobulin auf, welches spezifisch gegenüber dem Antigen reaktiv ist. Die Immunoglobuline können ökonomisch in großen Mengen hergestellt werden und finden z. B. bei der Behandlung von verschiedenen humanen Erkrankungen mittels einer Vielzahl von Techniken Anwendung.
  • Damit die Erfindung vollständiger verstanden wird, werden mehrere Definitionen dargelegt. Wie es hierin verwendet wird, bezieht sich der Ausdruck "Immunoglobulin" auf ein Protein, das aus einem oder mehreren Polypeptiden besteht, die im Wesentlichen durch Immunoglobulin-Gene kodiert werden. Die erkannten Immunoglobulin-Gene schließen die Gene der Kappa-, Lambda-, Alpha-, Gamma-(IgG1, IgG2, IgG3, IgG4), Delta-, Epsilon- und mu-konstanten Regionen sowie die unzähligen Gene von Immunoglobulin-variablen Regionen ein. "Leichte Ketten" von Immunoglobulinen voller Länge (ungefähr 25 Kd oder 214 Aminosäuren) werden durch ein Gen der variablen Region am NH2-Terminus (ungefähr 110 Aminosäuren) und durch ein Gen der Kappa- oder Lambda-konstanten Region an dem COOH-Terminus kodiert. "Schwere Ketten" von Immunoglobulin voller Länge (ungefähr 50 Kd oder 446 Aminosäuren) werden entsprechend durch ein Gen der variablen Region kodiert (ungefähr 116 Aminosäuren) und durch eines der anderen zuvor erwähnten Gene der konstanten Region, z. B. Gamma (kodiert ungefähr 330 Aminosäuren) kodiert.
  • Eine Form von Immunoglobulin stellt die Basisstruktureinheit eines Antikörpers dar. Diese Form ist ein Tetramer und besteht aus zwei identischen Paaren an Immunoglobulin-Ketten, wobei jedes Paar eine leichte und eine schwere Kette besitzt. In jedem Paar sind die variablen Regionen der leichten und schweren Kette zusammen verantwortlich für die Bindung an ein Antigen, und die konstanten Regionen sind verantwortlich für die Antikörper-Effektorfunktionen. Zusätzlich zu Antikörpern können Immunoglobuline in einer Vielzahl von anderen Formen. einschließlich z. B. Fv, Fab und (Fab')2 sowie als bifunktionelle Hybridantikörper (z. B. Lanzavecchia et al., Eur. J. Immunol. 17, 105 (1987)) und in Einzelketten (z. B. Huston et al., Proc. Natl. Acad. Sci. USA 85, 5879–5883 (1988) und Bird et al., Science 242, 423–426 (1988)) existieren. (Siehe, im Allgemeinen, Hood et al., "Immunology", Benjamin, N.Y., 2. Ausgabe (1984) und Hunkapiller und Hood, Nature 223, 15–16 (1986)).
  • Eine variable Region einer leichten oder schweren Immunoglobulin-Kette besteht aus einer "Framework"-Region, die von drei hypervariablen Regionen, die auch CDRs genannt werden, unterbrochen ist. Die Ausdehnung der Framework-Region und der CDRs wurde genau definiert (siehe "Sequences of Proteins of Immunological Interest", E. Kabat et al., US Department of Health and Human Services, (1983)). Die Sequenzen der Framework-Regionen verschiedener leichter oder schwerer Ketten sind innerhalb einer Spezies relativ konserviert. Wie es hierin verwendet wird, ist eine "humane Framework-Region" eine Framework-Region, die im Wesentlichen identisch (ungefähr 85% oder mehr, gewöhnlich 90–95% oder mehr) ist zu der Framework-Region eines natürlich vorkommenden humanen Immunoglobulins. Die Framework-Region eines Antikörpers, also die kombinierten Framework-Regionen der Bestandteile der leichten und schweren Ketten, dient dazu, die CDRs zu positionieren und auszurichten. Die CDRs sind vorwiegend verantwortlich für die Bindung an ein Epitop eines Antigens.
  • Chimäre Antikörper sind Antikörper, deren Gene für die leichte und schwere Kette typischerweise durch Genmanipulation aus Genen der variablen und konstanten Region eines Immunoglobulins konstruiert wurden, die zu verschiedenen Spezies gehören. Z. B. können die variablen Segmente der Gene von einem monoklonalen Maus-Antikörper an humane konstante Segmente gebunden werden, wie Gamma 1 und Gamma 3. Ein typischer therapeutischer chimärer Antikörper ist somit ein Hybridprotein, das aus der variablen oder Antigen-bindenden Domäne von einem Maus-Antikörper und der konstanten oder Effektordomäne von einem humanen Antikörper zusammengesetzt ist (z. B. A.T.C.C. Accession Nr. CRL 9688 sekretiert einen Anti-Tac chimären Antikörper), obwohl andere Säugerspezies verwendet werden können.
  • Wie es hierin verwendet wird, bezieht sich der Ausdruck "humanisiertes" Immunoglobulin auf ein Immunoglobulin, das eine humane Framework-Region und eine oder mehrere CDRs von einem nicht humanen (im Allgemeinen einem Maus- oder Ratten-) Immunoglobulin umfasst. Das nicht humane Immunoglobulin, das die CDRs bereitstellt, wird "Donor" genannt und das humane Immunoglobulin, das das Framework bereitstellt, wird "Akzeptor" genannt. Konstante Regionen müssen nicht vorhanden sein, doch wenn sie vorhanden sind, dann müssen sie im Wesentlichen identisch zu konstanten Regionen von humanem Immunoglobulin sein, d. h. mindestens ungefähr 85– 90%, vorzugsweise ungefähr 95% oder mehr identisch. Daher sind alle Teile eines humanisierten Immunoglobulins, mit Ausnahme von möglicherweise den CDRs, im Wesentlichen identisch mit entsprechenden Teilen der natürlichen humanen Immunoglobulin-Sequenzen. Ein "humanisierter Antikörper" ist ein Antikörper, der ein humanisiertes Leichtketten- und ein humanisiertes Schwerketten-Immunoglobulin umfasst. Z. B. würde ein humanisierter Antikörper keinen typischen chimären Antikörper, wie er oben definiert ist, umfassen, z. B., da die gesamte variable Region eines chimären Antikörpers nicht human ist. Man sagt, dass der Donor-Antikörper durch das Verfahren der "Humanisierung" "humanisiert" wurde, da man annimmt, dass der resultierende humanisierte Antikörper an das gleiche Antigen bindet, wie der Donor-Antikörper, welcher die CDRs bereitstellt.
  • Es ist klar, dass die durch das Verfahren der vorliegenden Erfindung gestalteten humanisierten Antikörper zusätzlich konservative Aminosäure-Substitutionen aufweisen können, die im Wesentlichen keine Auswirkung auf die Antigen-Bindung oder andere Immunoglobulin-Funktionen besitzen. Durch konservative Substitutionen sind Kombinationen wie gly, ala; val, ile, leu; asp, glu; asn, gln; ser, thr; lys, arg; und phe, tyr beabsichtigt.
  • Humanisierte Immunoglobuline, einschließlich humanisierte Antikörper, wurden mittels Genmanipulation konstruiert. Die meisten humanisierten Immunoglobuline, die zuvor beschrieben wurden (Jones et al., op. cit.; Verhoeyen et al., op. cit; Riechmann et al., op. cit.) umfassten ein Framework, welches identisch ist mit dem Framework einer speziellen humanen Immunoglobulin-Kette, dem Akzeptor und drei CDRs von einer nicht humanen Donor-Immunoglobulin-Kette. In einem Fall (Riechmann et al., op. cit.) wurden zwei zusätzliche Aminosäuren im Framework verändert, damit sie die gleichen sind, wie die Aminosäuren in anderen humanen Framework-Regionen. Die vorliegende Erfindung schließt Kriterien ein, durch welche eine limitierte Anzahl an Aminosäuren in dem Framework einer humanisierten Immunoglobulin-Kette dahingehend ausgewählt wird, dass sie gleich sind wie die Aminosäuren an solchen Positionen in dem Donor und nicht in dem Akzeptor, um die Affinität eines Antikörpers, der die humanisierte Immunoglobulin-Kette umfasst, zu erhöhen.
  • Die vorliegende Erfindung basiert zum Teil auf dem Modell, dass zwei Gründe, die zu dem Verlust an Affinität bei vorherigen Mitteln zur Herstellung humanisierter Antikörper (unter Verwendung von zum Beispiel Maus-Antikörpern als Quelle für die CDRs) beitragen, sind:
    • (1) Wenn die Maus-CDRs mit dem humanen Framework kombiniert werden, werden die Aminosäuren in dem Framework nahe der CDRs human anstelle von murin. Ohne dass man auf die Theorie festgelegt werden möchte, wird angenommen, dass diese veränderten Aminosäuren die CDRs leicht stören können, da sie andere elektrostatische oder hydrophobe Kräfte erzeugen als in dem Donor-Maus-Antikörper, und die gestörten CDRs können mit dem Antigen einen nicht so wirksamen Kontakt eingehen, wie die CDRs in dem Donor-Antikörper;
    • (2) Auch Aminosäuren in dem ursprünglichen Maus-Antikörper, welche in der Nähe von, aber nicht Teil der CDRs sind (d. h. noch Teil des Frameworks sind), können mit dem Antigen in Kontakt treten, was zur Affinität beiträgt. Diese Aminosäuren gehen verloren, wenn der Antikörper humanisiert wird, da alle Framework-Aminosäuren human gemacht werden.
    • (3) Es wurde berichtet, dass injizierte Maus-Antikörper eine viel kürzere Halbwertszeit im humanen Kreislauf besitzen, als die Halbwertszeit von normalen Antikörpern ist (D. Shaw et al., J. Immunol. 138, 4534–4538 (1987)). Vermutlich weisen injizierte humanisierte Antikörper eine Halbwertszeit auf, die ähnlicher ist zu natürlich auftretenden humanen Antikörpern, was erlaubt, kleinere und weniger häufige Dosen zu verabreichen.
  • Um diese Probleme zu vermeiden, und um humanisierte Antikörper zu erzeugen, die eine sehr starke Affinität für ein gewünschtes Antigen besitzen, verwendet die vorliegende Erfindung zur Gestaltung humanisierter Immunoglobuline ein oder mehrere der folgenden Prinzipien. Die Kriterien können auch einzeln oder, wenn erforderlich, in Kombination verwendet werden, um die gewünschte Affinität oder andere Charakteristika zu erreichen.
  • Ein Prinzip ist, dass als Akzeptor ein Framework von einem speziellen humanen Immunoglobulin verwendet wird, welches ungewöhnlich homolog ist zu dem zu humanisierenden Donor-Immunoglobulin, oder es wird ein Konsensus-Framework von vielen humanen Antikörpern verwendet. Z. B. zeigt der Vergleich der Sequenz einer variablen Region der schweren (oder leichten) Kette von der Maus zu humanen schweren (oder leichten) variablen Regionen in einer Datenbank (z. B. der National Biomedical Research Foundation Protein Identification Resource), dass das Ausmaß an Homologie gegenüber verschiedenen humanen Regionen in weiten Grenzen variiert, typischennreise von ungefähr 40% bis ungefähr 60–70%. Indem als Akzeptor-Immunoglobulin eine der humanen variablen Regionen der schweren (bzw. leichten) Kette ausgewählt wird, die am meisten homolog sind zu der variablen Region der schweren (bzw. leichten) Kette des Donor-Immunoglobulins, werden weniger Aminosäuren verändert werden, wenn aus dem Donor-Immunoglobulin das humanisierte Immunoglobulin gemacht wird. Somit und wieder ohne, dass man auf die Theorie festgelegt werden möchte, wird angenommen, dass es weniger wahrscheinlich ist, dass eine Aminosäure in Nähe der CDRs verändert wird, welche ihre Konformation stört. Darüber hinaus kann die genaue Gesamtgestalt eines humanisierten Antikörpers, der die humanisierte Immunoglobulin-Kette umfasst, der Gestalt des Donor-Antikörpers stärker ähneln, wodurch auch die Wahrscheinlichkeit der Störung der CDRs verringert wird.
  • Typischerweise wird als Akzeptor eine der 3–5 homologsten Sequenzen der variablen Region der schweren Kette in einer repräsentativen Sammlung von mindestens ungefähr 10 bis 20 verschiedenen humanen schweren Ketten ausgewählt werden, um das Framework der schweren Kette bereitzustellen, und genauso für die leichte Kette. Vorzugsweise wird eine der 1–3 homologsten variablen Regionen verwendet werden. Die ausgewählte Akzeptor-Immunoglobulin-Kette wird in der Framework-Region am meisten bevorzugt mindestens ungefähr 65% Homologie zu dem Donor-Immunoglobulin aufweisen.
  • In vielen Fällen kann es bevorzugt sein, leichte und schwere Ketten von dem gleichen humanen Antikörper als Akzeptor-Sequenzen zu verwenden, um sicherzugehen, dass die humanisierten leichten und schweren Ketten einen vorteilhaften Kontakt miteinander eingehen. In diesem Fall werden die leichten und schweren Ketten des Donors nur mit Ketten von humanen Antikörpern verglichen werden, deren vollständige Sequenz bekannt ist, z. B. von Eu, Lay, Pom, Wol, Sie, Gal, Ou und WEA-Antikörpern (Kabat et al., op. cit.; gelegentlich sind die letzten paar Aminosäuren einer humanen Kette nicht bekannt und müssen durch Homologie zu anderen humanen Antikörpern abgeleitet werden). Der humane Antikörper wird so gewählt werden, dass darin die Sequenzen der variablen Regionen der leichten und schweren Kette zusammengenommen insgesamt am meisten homolog sind zu den Sequenzen der variablen Region der leichten und schweren Kette des Donors. Manchmal wird der Sequenz der schweren Kette ein größeres Gewicht gegeben. Der ausgewählte humane Antikörper wird dann sowohl Akzeptor-Sequenzen der leichten als auch der schweren Kette bereitstellen. In der Praxis wird oft gefunden, dass der humane Eu-Antikörper diese Rolle einnimmt. Ungeachtet der Weise, wie das Akzeptor-Immunoglobulin gewählt wird, kann eine höhere Affinität erreicht werden, indem eine kleine Zahl an Aminosäuren in dem Framework der humanisierten Immunoglobulin-Kette so gewählt wird, dass sie die gleichen sind, wie die Aminosäuren an solchen Positionen in dem Donor und nicht wie in dem Akzeptor. Ein zweites Prinzip ist, dass die folgenden Kategorien definieren, welche Aminosäuren von dem Donor ausgewählt werden können. Tatsächlich wird die Donor-Aminosäure an vielen oder an allen Aminosäure-Positionen in einer dieser Kategorien ausgewählt werden.
  • Kategorie 1: Die Aminosäureposition ist in einer CDR, wie von Kabat et al., op. cit. definiert.
  • Kategorie 2: Wenn eine Aminosäure in dem Framework des humanen Akzeptor-Immunoglobulins ungewöhnlich ist (d. h. "rar", was, wie es hierin verwendet wird, angibt, dass eine Aminosäure an dieser Position in weniger als ungefähr 20%, aber gewöhnlich weniger als ungefähr 10% der Sequenzen der Region der humanen schweren (bzw. leichten) Kette V in einer repräsentativen Datenbank auftritt), und wenn die Donor-Aminosäure an dieser Position typisch ist für humane Sequenzen (d. h. "gewöhnlich", was, wie es hierin verwendet wird, angibt, dass eine Aminosäure in mehr als ungefähr 25%, aber gewöhnlich mehr als ungefähr 50% der Sequenzen in einer repräsentativen Datenbank auftritt), dann kann eher die Donor-Aminosäure anstele der Akzeptor ausgewählt werden. Dieses Kriterium hilft, sicherzugehen, dass eine atypische Aminosäure in dem humanen Framework die Antikörperstruktur nicht zerstört. Darüber hinaus kann der humanisierte Antikörper weniger immunogen gemacht werden, indem eine ungewöhnliche Aminosäure gegen eine Aminosäure von dem Donor-Antikörper, welche typisch ist für humane Antikörper, ersetzt wird.
  • Alle Sequenzen von variablen Regionen der humanen leichten und schweren Kette werden jeweils in "Untergruppen" von Sequenzen unterteilt, welche besonders homolog zueinander sind und die gleichen Aminosäuren an bestimmten kritischen Positionen besitzen (Kabat et al., op. cit.). Wenn entschieden wird, ob eine Aminosäure in einer humanen Akzeptor-Sequenz "rar" oder "gewöhnlich" unter humanen Sequenzen ist, wird es oft bevorzugt sein, nur solche humanen Sequenzen, die in der gleichen Untergruppe wie die der Akzeptor-Sequenz sind, zu betrachten.
  • Kategorie 3: In den Positionen direkt neben einer oder mehreren der drei CDRs in der Primärsequenz der humanisierten Immunogloublin-Kette können eher die Donor-Aminosäure(n) anstelle der die Akzeptor-Aminosäure ausgewählt werden. Diese Aminosäuren treten insbesondere vermutlich mit den Aminosäuren in den CDRs in Wechselwirkung und es ist, wenn sie von dem Akzeptor ausgewählt werden, wahrscheinlich, dass sie die Donor-CDRs stören und die Affinität verringern. Darüber hinaus können die angrenzenden Aminosäuren direkt mit dem Antigen wechselwirken (Amit et al., Science, 233, 747–753 (1986)), und das Auswählen dieser Aminosäuren von dem Donor kann erwünscht sein, um alle Antigen-Kontakte beizubehalten, die eine Affinität in dem ursprünglichen Antikörper bereitstellen.
  • Kategorie 4: Ein dreidimensionales Modell, typischerweise des ursprünglichen Donor-Antikörpers, zeigt, dass bestimmte Aminosäuren außerhalb der CDRs in Nähe der CDRs sind und eine gute Wahrscheinlichkeit besteht, dass sie durch Wasserstoffbindungen, Van der Waals-Kräfte, hydrophobe Wechselwirkungen etc. mit Aminosäuren in den CDRs wechselwirken. An solchen Aminosäurepositionen kann die Donor-Immunoglobulin-Aminosäure eher als die Akzeptor-Immunoglobulin-Aminosäure ausgewählt werden. Aminosäuren gemäß diesem Kriterium werden im Allgemeinen ein Seitenkettenatom innerhalb von ungefähr 3 Å-Einheiten von manchem Atom in den CDRs besitzen und müssen ein Atom enthalten, das mit den CDR-Atomen gemäß etablierter chemischer Kräfte wechselwirken könnte, wie solchen, wie sie oben angegeben sind.
  • Im Fall von Atomen, die eine Wasserstoffbindung bilden können, werden die 3 Å zwischen ihren Kernen gemessen, aber für Atome, die keine Bindung bilden, werden die 3 Å zwischen ihren Van der Waals-Flächen gemessen. Daher müssen in dem letzteren Fall die Kerne bei Atomen, von welchen angenommen wird, dass sie wechselwirken, innerhalb von ungefähr 6 Å liegen (3 + Summe der Van der Waals-Radien). In vielen Fällen werden die Kerne von 4 oder 5 bis 6 Å voneinander entfernt sein. Bei der Bestimmung, ob eine Aminosäure mit den CDRs wechselwirken kann, ist es bevorzugt, die letzten 8 Aminosäuren der CDR 2 der schweren Kette als Teil der CDRs nicht zu betrachten, da sich diese 8 Aminosäuren vom Standpunkt der Struktur aus gesehen mehr als Teil des Frameworks verhalten.
  • Aminosäuren in dem Framework, die in der Lage sind, mit Aminosäuren in den CDRs in Wechselwirkung zu treten, und welche daher zur Kategorie 4 gehören, können auf andere Weise unterschieden werden. Der Lösungsmittelzugängliche Oberflächenbereich jeder Framework-Aminosäure wird auf zwei Arten berechnet: (1) in dem intakten Antikörper und (2) in einem hypothetischen Molekül, das aus dem Antikörper besteht, von welchem die CDRs entfernt wurden. Eine beträchtliche Differenz zwischen diesen Zahlen von ungefähr 10 Å2 oder mehr zeigt, dass die Zugänglichkeit der Framework-Aminosäure gegenüber Lösungsmittel zumindest teilweise durch die CDRs blockiert wird, und dass die Aminosäure daher mit den CDRs in Kontakt tritt. Der Lösungsmittel-zugängliche Oberflächenbereich einer Aminosäure kann basierend auf einem dreidimensionalen Modell eines Antikörpers unter Verwendung von im Fachgebiet bekannten Algorithmen berechnet werden (z. B. Connolly, J. Appl. Cryst. 16, 548 (1983) und Lee und Richards, J. Mol. Biol. 55, 379 (1971)). Framework-Aminosäuren können gelegentlich auch indirekt mit den CDRs wechselwirken, indem die Konformation einer anderen Framework-Aminosäure beeinflusst wird, welche wiederum die CDRs kontaktiert.
  • Die Aminosäuren an mehreren Positionen in dem Framework sind dafür bekannt, dass sie in der Lage sind, mit den CDRs in vielen Antikörpern in Wechselwirkung zu treten (Chothia und Lesk, J. Mol. Biol. 196, 901 (1987), Chothia et al., Nature 342, 877 (1989) und Tramontano et al., J. Mol. Biol. 215, 175 (1990)), insbesondere an den Positionen 2, 48, 64 und 71 der leichten Kette und 26–30, 71 und 94 der schweren Kette (Nummerierung gemäß Kabat, op. cit.), und diese Aminosäuren werden daher im Allgemeinen in Kategorie 4 sein. Typischerweise werden humanisierte Immunoglobuline zusätzlich zu diesen Donor-Aminosäuren (wenn sie verschieden sind) aus Kategorie 4 enthalten. Es ist auch wahrscheinlich, dass die Aminosäuren an den Positionen 35 in der leichten Kette und 93 und 103 in der schweren Kette mit den CDRs wechselwirken. An all diesen nummerierten Positionen ist es bevorzugt, dass die Donor-Aminosäure anstelle der Akzeptor-Aminosäure (wenn sie sich voneinander unterscheiden) ausgewählt wird, damit sie in dem humanisierten Immunoglobulin auftritt. Andererseits können bestimmte Positionen, die in Kategorie 4 sein können, wie die ersten 5 Aminosäuren der leichten Kette, manchmal von dem Akzeptor-Immunoglobulin ausgewählt werden, ohne dass in dem humanisierten Immunoglobulin ein Verlust der Affinität erhalten wird.
  • Chothia und Lesk (op. cit.) definieren die CDRs unterschiedlich als Kabat et al. (op. cit.). Insbesondere ist CDR1 so definiert, dass die Reste 26–32 eingeschlossen sind. Demgemäß wählen Riechmann et al. (op. cit.) diese Aminosäuren von den Donor-Immunoglobulinen aus.
  • Computerprogramme zur Bildung von Modellen von Proteinen wie Antikörpern sind allgemein erhältlich und dem Fachmann wohlbekannt (siehe Levy et al., Biochemistry 28, 7168–7175 (1989); Bruccoleri et al., Nature 335, 564–568 (1988); Chothia et al., Science 233, 755–758 (1986)). Diese sind nicht Teil der Erfindung. Tatsächlich können die bekannten Antikörperstrukturen, welche von der Brookhaven Protein Datenbank erhältlich sind, als Rohmodelle anderer Antikörper, wenn erforderlich, verwendet werden, da alle Antikörper ähnliche Strukturen besitzen. Kommerziell erhältliche Computerprogramme können verwendet werden, um diese Modelle auf einem Computermonitor darzustellen, um die Distanz zwischen Atomen zu berechnen, und um die Wahrscheinlichkeit von verschiedenen wechselwirkenden Aminosäuren abzuschätzen (siehe Ferrin et al., J. Mol. Graphics 6, 13–27 (1988)).
  • Zusätzlich zu den obigen Kategorien, welche beschreiben, wann eine Aminosäure in dem humanisierten Immunoglobulin von dem Donor genommen werden kann, können bestimmte Aminosäuren in dem humanisierten Immunoglobulin weder von dem Donor noch dem Akzeptor genommen werden, wenn sie in die Kategorie fallen:
  • Kategorie 5: Wenn die Aminosäure an einer gegebenen Position in dem Donor-Immunoglobulin "rar" für humane Sequenzen ist, und die Aminosäure an der Position in dem Akzeptor-Immunoglobulin auch "rar" für humane Sequenzen ist, wie es oben definiert ist, dann kann die Aminosäure an der Position in dem humanisierten Immunoglobulin so ausgewählt werden, dass sie eine Aminosäure ist, die "typisch" für humane Sequenzen ist. Eine bevorzugte Wahl ist die Aminosäure, die am häufigsten an der Position in den bekannten humanen Sequenzen auftritt, welche zu der gleichen Untergruppe wie die Akzeptor-Sequenz gehören.
  • Humanisierte Antikörper weisen im Allgemeinen mindestens 3 potenzielle Vorteile gegenüber Maus- oder in manchen Fällen chimären Antikörpern zur Verwendung in der Humantherapie auf:
    • 1) Da der Effektorteil human ist, kann er besser mit anderen Teilen des humanen Immunsystems wechselwirken (z. B. die Targetzellen wirksamer durch Komplement-abhängige Cytotoxizität (CDC) oder Antikörper-abhängige zelluläre Cytotoxizität (ADCC) zerstören).
    • 2) Das humane Immunsystem sollte das Framework oder die konstante Region des humanisierten Antikörpers nicht als fremd erkennen, und die Antikörperreaktion gegen einen solchen injizierten Antikörper sollte geringer sein als gegen einen vollständig fremden Maus-Antikörper oder einen teilweise fremden chimären Antikörper.
  • In einem Aspekt ist die vorliegende Erfindung auf die Gestaltung humanisierter-Immunoglobuline gerichtet, die hergestellt werden, indem rekombinante DNA-Segmente, die für die CDRs der schweren und leichten Kette von einem Donor-Immunoglobulin, das in der Lage ist, das gewünschte Antigen CD33 zu binden, kodieren, welche an DNA-Segmente gebunden sind, die für humane Akzeptor-Framework-Regionen kodieren. Beispielhafte DNA-Sequenzen, die gemäß der vorliegenden Erfindung gestaltet sind, kodieren für die Polypeptid-Ketten, umfassend CDRs schwerer und leichter Kette mit im Wesentlichen humanen Framework-Regionen, wie es in 1 gezeigt ist. Aufgrund der Codondegeneration und nicht kritischer Aminosäure-Substitutionen können andere DNA-Sequenzen leicht gegen solche Sequenzen ausgetauscht werden, wie es unten detailliert beschrieben ist. Im Allgemeinen finden die Kriterien der vorliegenden Erfindung Anwendung zur Gestaltung im Wesentlichen für jedes humanisierte Immunoglobulin.
  • Die DNA-Segmente werden typischerweise ferner eine Expressionskontroll-DNA-Sequenz einschließen, die mit den Kodierungssequenzen des humanisierten Immunoglobulins verbunden sind, einschließlich natürlichassoziierter oder heterologer Promotorregionen. Vorzugsweise werden die Expressionskontrollsequenzen eukaryontische Promotorsysteme in Vektoren sein, die in der Lage sind, eukaryontische Wirtszellen zu transformieren oder transfizieren, es können aber auch Kontrollsequenzen für prokaryontische Wirte verwendet werden. Nachdem der Vektor in den geeigneten Wirt inkorporiert wurde, wird der Wirt unter Bedingungen gehalten, die geeignet sind für ein hohes Level an Expression der Nukleotidsequenzen und, wenn erwünscht, kann darauf das Gewinnen und Aufreinigen der humanisierten leichten Ketten, schweren Ketten, der Dimere der leichten/schweren Kette oder von intakten Antikörpern, Bindefragmenten oder anderen Immunoglobulin-Formen folgen (siehe S. Beychok, Cells of Immunoglobulin Synthesis, Academic Press, N.Y., (1979)).
  • DNA-Sequenzen humaner konstanter Regionen können gemäß wohlbekannter Vorgehensweisen von einer Vielzahl von humanen Zellen, aber vorzugsweise immortalisierten B-Zellen isoliert werden (siehe Kabat op. cit. und WP 87/02671). Die CDRs zur Herstellung der Immunoglobuline der vorliegenden Erfindung werden entsprechend von monoklonalen Antikörpern abgeleitet werden, die in der Lage sind, an das bestimmte Antigen, wie den humanen IL-2-Rezeptor, zu binden, und in jeder zweckmäßigen Säuger-Quelle einschließlich Mäusen, Ratten, Kaninchen oder anderen Wirbeltieren, die in der Lage sind, Antikörper zu produzieren, durch wohlbekannte Verfahren produziert zu werden. Geeignete Quell-Zellen für die konstante Region und die Framework-DNA-Sequenzen und Wirtszellen für die Immunoglobulin-Expression und Sekretion können von einer Anzahl von Quellen wie der American Type Culture Collection erhalten werden ("Catalogue of Cell Lines and Hybridomas", 6. Ausgabe (1988) Rockville, Maryland, USA).
  • Alternativ können Polypeptid-Fragmente, die nur einen Teil der primären Antikörper-Struktur umfassen, hergestellt werden, wobei die Fragmente eine oder mehrere Immunoglobulin-Aktivitäten besitzen (z. B. Komplement-Fixierungsaktivität). Diese Polypeptid-Fragmente können durch proteolytische Spaltung von intakten Antikörpern mittels Verfahren, die im Fachgebiet wohlbekannt sind, hergestellt werden, oder durch Insertion von Stoppcodons an den gewünschten Stellen unter Verwendung von ortsgerichteter Mutagenese, wie nach CH1, um Fab-Fragmente zu erzeugen oder nach der Gelenkregion, um (Fab')2-Fragmente herzustellen. Einzelketten-Antikörper können hergestellt werden, indem VL und VH mit einem DNA-Linker verbunden werden (siehe Huston et al., op. cit., und Bird et al., op. cit.). Da die Immunoglobulinverwandten Gene wie viele Gene separate funktionelle Regionen enthalten, wobei jede eine oder mehrere unterschiedliche biologische Aktivitäten besitzet. können die Gene auch mit funktionellen Regionen von anderen Genen verbunden werden (z. B. Enzymen, siehe allgemein übertragene U.S.S.N. 132,387, angemeldet am 15. Dezember 1987), um Fusionsproteine zu erzeugen (z. B. Immunotoxine), die neue Eigenschaften besitzen. Die Nukleinsäure-Sequenzen der vorliegenden Erfindung, die in der Lage sind, um schließlich die gewünschten humanisierten Antikörper zu exprimieren, können aus einer Vielzahl von verschiedenen Polynukleotiden (genomischer oder cDNA, RNA, synthetischen Oligonukleotiden, etc.) und Komponenten (z. B. V-, J-, D- und C-Regionen) sowie durch eine Vielzahl verschiedener Techniken erzeugt werden. Gegenwärtig ist die Verbindung geeigneter synthetischer und genomischer Sequenzen das übliche Verfahren zur Herstellung, es können aber auch cDNA-Sequenzen verwendet werden (siehe europäische Patentveröffentlichung Nr. 0239400 und L. Riechmann et al., Nature 332, 323–327 (1988)).
  • Wie zuvor erwähnt, werden die DNA-Sequenzen in Wirten exprimiert werden, nachdem die Sequenzen funktionsfähig (d. h. so positioniert sind, um sicherzugehen, dass sie funktionieren) an Expressionskontrollsequenzen gebunden wurden. Diese Expressionsvektoren sind typischennreise in den Wirtsorganismen entweder als Episome oder als ein wesentlicher Teil der chromosomalen DNA des Wirts replizierbar. Gewöhnlich werden Expressionsvektoren Selektionsmarker, z. B. Tetracyclin oder Neomycin, enthalten, um die Detektion solcher Zellen zu erlauben, die mit den gewünschten DNA-Sequenzen transformiert sind (siehe z. B. US-Patent 4,704,362).
  • E. coli ist ein prokaryontischer Wirt, der insbesondere zur Klonierung der DNA-Sequenzen der vorliegenden Erfindung nützlich ist. Andere mikrobielle Wirte, die zur Verwendung geeignet sind, schließen Bazillen, wie Bacillus subtilis, und andere Enterobacteriaceae wie Salmonella, Serratia und verschiedene Pseudomonas-Spezies ein. In diesen prokaryontischen Wirten kann man auch Expressionsvektoren erzeugen, welche typischerweise Expressionskontrollsequenzen enthalten werden, die mit der Wirtszelle kompatibel sind (z. B. ein Replikationsursprung). Zusätzlich wird jede beliebige Anzahl aus einer Vielzahl von Promotoren vorhanden sein, wie das Lactose-Promotorsystem, ein Tryptophan (TRP)-Promotorsystem, ein Beta-Lactamase-Promotorsystem oder ein Promotorsystem von dem Phagen Lambda. Die Promotoren werden typischerweise die Expression kontrollieren, ggf. mit einer Operatorsequenz, und sie weisen Ribosom-Bindestellen-Sequenzen und dgl. auf, um die Transkription und Translation zu initiieren und durchzuführen.
  • Es können auch andere Mikroben, wie Hefe, für die Expression verwendet werden. Saccharomyces ist ein bevorzugter Wirt, mit geeigneten Vektoren mit Expressionskontrollsequenzen wie Promotoren, einschließlich 3-Phosphoglyceratkinase oder anderen glykolytischen Enzymen und einem Replikationsursprung, Terminationssequenzen und dgl., wie gewünscht.
  • Zusätzlich zu Mikroorganismen kann auch eine Säugergewebezellkultur verwendet werden, um die Polypeptide der vorliegenden Erfindung zu exprimieren und zu erzeugen (siehe Winnacker, "From Genes to Clones", VCH Publishers, N.Y., N.Y. (1987)). Gegenwärtig sind eukaryontische Zellen bevorzugt, da eine Anzahl von geeigneten Wirtszelllinien, die in der Lage sind, intakte Immunoglobuline zu sekretieren, im Fachgebiet entwickelt wurden, und schließen die CHO-Zelllinien, verschiedene COS-Zelllinien, HeLa-Zellen, vorzugsweise Myelom-Zelllinien etc. und transformierte B-Zellen oder Hybridome ein. Expressionsvektoren für diese Zellen können Expressionskontrollsequenzen wie einen Replikationsursprung, einen Promotor, einen Enhancer (Queen et al, Immunol. Rev., 89, 49–68 (1986)) und notwendige Prozessierungsinformationsstellen wie Ribosom-Bindestellen, RNA-Splicestellen, Polyadenylierungsstellen und transkriptionale Terminatorsequenzen enthalten. Bevorzugte Expressionskontrollsequenzen sind Promotoren, die von Immunoglobulingenen, SV40, Adenovirus, Cytomegalovirus, bovinem Papillomavirus und dgl. abgeleitet sind.
  • Die Vektoren, die die DNA-Segmente von Interesse (z. B. die für die schwere und leichte Kette kodierenden Sequenzen und Expressionkontrollsequenzen) enthalten, können durch wohlbekannte Verfahren, die abhängig von der Art des zellulären Wirts variieren, in die Wirtszelle transferiert werden. Z. B. wird die Calciumchlorid-Transfektion gewöhnlich für prokaryontische Zellen verwendet, wohingegen die Calciumphosphat-Behandlung oder Elektroporation für andere zelluläre Wirte verwendet werden kann. (Siehe im Allgemeinen Maniatis et al., Molecular Cloning: A Laborator Manual, Cold Spring Harbor Press, (1982)).
  • Wenn sie exprimiert wurden, können die ganzen Antikörper, ihre Dimere, einzelne leichte und schwere Ketten oder andere Immunoglobulin-Formen der vorliegenden Erfindung gemäß Standardverfahren des Fachgebiets einschließlich der Ammoniumsulfatpräzipitation, Affinitätssäulen, Säulenchromatographie, Gelektrophorese und dgl. aufgereinigt werden (siehe im Allgemeinen R. Scopes, "Protein Purification", Springer-Verlag, N.Y. (1982)). Im Wesentlichen reine Immunoglobuline mit mindestens ungefähr 90–95% Homogenität sind bevorzugt, und 98–99% oder mehr Homogenität sind für pharmazeutische Verwendungen am meisten bevorzugt. Wenn sie teilweise oder zu der gewünschten Homogenität aufgereinigt sind, können die Polypeptide dann therapeutisch (einschließlich extrakorporal) oder bei der Entwicklung und Durchführung von Assay-Verfahren, Immunofluoreszenz-Anfärbungen und dgl. verwendet werden. Siehe im Allgemeinen Immunological Methods, Vols. I und II, Lefkovits und Pernis, Hrsg., Academic Press, New York, N.Y. (1979 und 1981)).
  • Eine bevorzugte pharmazeutische Zusammensetzung der vorliegenden Erfindung umfasst die Verwendung von einem oder mehreren der vorliegenden Antikörper in Immunotoxinen. Immunotoxine sind durch zwei Komponenten gekennzeichnet und sind insbesondere nützlich zur in vitro oder in vivo Abtötung von ausgewählten Zellen. Eine Komponente ist ein cytotoxisches Mittel, welches gewöhnlich tödlich ist für eine Zelle, wenn es angebunden oder absorbiert ist. Die zweite Komponente, die als das "Verabreichungsvehikel" bezeichnet wird, stellt ein Mittel zur Verabreichung des toxischen Mittels an einen bestimmten Zelltyp, wie Zellen, die ein Karzinom umfassen, bereit. Die zwei Komponenten sind gewöhnlich durch eine Vielzahl von wohlbekannten chemischen Verfahren chemisch miteinander verbunden. Z. B. kann die Verbindung, wenn das cytotoxische Mittel ein Protein und die zweite Komponente ein intaktes Immunoglobulin ist, mittels heterobifunktioneller Crosslinker, z. B. SPDP, Carbodiimid, Glutaraldehyd oder dgl. durchgeführt werden. Die Herstellung verschiedener Immunotoxine ist im Fachgebiet wohlbekannt und kann z. B. in "Monoclonal Antibody-Toxin Conjugates: Aiming the Magic Bullet," Thorpe et al., Monoclonal Antibodies in Clinical Medicine, Academic Press, S. 168–190 (1982) gefunden werden. Die Komponenten können auch genetisch verbunden werden (siehe Chaudhary et al., Nature 339, 394 (1989)).
  • Zur Verwendung in Immunotoxinen sind eine Vielzahl von cytotoxischen Mitteln geeignet. Cytotoxische Mittel können Radionuklide, wie Iod-131 oder andere Isotope von Iod, Yttrium-90, Rhenium-188 und Wismut-212 oder andere Alpha-Strahler; eine Anzahl von chemotherapeutischen Wirkstoffen wie Vindesin, Methotrexat, Adriamycin, und Cisplatin; und cytotoxische Proteine wie ribosomale Inhibierungsproteine wie antivirales Pokeweed Protein, Pseudomonas Exotoxin A, Ricin, Diphtherie-Toxin, Ricin A-Kette etc. oder ein Mittel einschließen, welches an der Zelloberfläche wirksam ist, wie die Phospholipaseenzyme (z. B. Phospholipase C). (Siehe im Allgemeinen WO 90/07861, veröffentlicht am 26. Juli 1990; "Chimeric Toxins", Olsnes und Phil, Pharmac. Ther. 25, 355–381 (1982); und "Monoclonal Antibodies for Cancer Detection and Therapy", Hrsg. Baldwin und Byers, S. 159–179, 224–266, Academic Press (1985)).
  • Die Verabreichungskomponente des Immunotoxins wird die humanisierten Immunoglobuline der vorliegenden Erfindung einschließen. Es werden vorzugsweise intakte Immunoglobuline und ihre Bindefragmente wie Fab verwendet. Typischerweise werden die Antikörper in den Immunotoxinen des humanen IgM- oder IgG-Isotyps sein, wenn erwünscht können aber andere konstante Regionen vom Säuger verwendet werden.
  • Die humanisierten Antikörper und pharmazeutischen Zusammensetzungen davon sind insbesondere nützlich für die parenterale Verabreichung, i. e. subkutan, intramuskulär oder intravenös. Die Zusammensetzungen für eine parenterale Verabreichung werden gewöhnlich eine Lösung des Immunoglobulins oder eines Cocktails davon, gelöst in einem annehmbaren Träger, vorzugsweise einem wässrigen Träger, umfassen. Es kann eine Vielzahl von wässrigen Trägern verwendet werden, z. B. Wasser, gepuffertes Wasser, 0,4% Salzlösung, 0,3% Glycin und dgl. Diese Lösungen sind steril und im Allgemeinen frei von partikulären Stoffen. Diese Zusammensetzungen können durch konventionelle wohlbekannte Sterilisationstechniken sterilisiert werden. Die Zusammensetzungen können pharmazeutisch annehmbare Hilfssubstanzen enthalten, wenn es erforderlich ist, den physiologischen Bedingungen nahezukommen, wie pH-regulierende und Puffermittel, Toxizitätsregulierende Mittel und dgl. z. B. Natriumacetat, Natriumchlorid, Kaliumchlorid, Calciumchlorid, Natriumlactat, humanes Albumin etc. Die Konzentration von Antikörpern in diesen Formulierungen kann in weiten Grenzen variieren, d. h. von weniger als ungefähr 0,5 Gew.-%, gewöhnlich soviel wie oder mindestens ungefähr 1% soviel wie 15 oder 20 Gew.-%, und wird vor allem basierend auf den Fluidvolumina, Viskositäten etc. gemäß der speziellen Verabreichungsweise ausgewählt werden.
  • Somit könnte eine typische pharmazeutische Zusammensetzung für die Injektion so hergestellt sein, dass sie bis zu 1 ml steriles gepuffertes Wasser und 1–10 mg Immunoglobulin enthält. Eine typische Zusammensetzung für die intravenöse Infusion könnte so hergestellt sein, dass sie bis zu 250 ml sterile Ringer-Lösung und 150 mg Antikörper enthält. Gegenwärtige Verfahren zur Herstellung parenteral verabreichbarer Zusammensetzungen werden dem Fachmann bekannt oder offensichtlich sein und sind detaillierter in z. B. Remington's Pharmaceutical Science 15. Ausgabe, Mack Publishing Company, Easton, Pennsylvania (1980) beschrieben, welche hierin durch Bezugnahme darauf enthalten ist.
  • Die Antikörper dieser Erfindung können zur Aufbewahrung gefroren oder lyophilisiert werden und vor der Verwendung in einem geeigneten Träger rekonstituiert werden. Es wurde gezeigt, dass diese Technik effektiv ist bei konventionellen Immunoglobulinen, und es können im Fachgebiet bekannte Lyophilisations- und Rekonstitutions-Techniken verwendet werden. Der Fachmann wird verstehen, dass Lyophilisation und Rekonstitution zu variierenden Graden an Verlust der Antikörperaktivität führen können (z. B. bei konventionellen Immunoglobulinen neigen IgM-Antikörper dazu, einen größeren Aktivitätsverlust zu unterlaufen als IgG-Antikörper), und dass die Mengen der Verwendung so eingestellt werden müssen, um dies zu kompensieren.
  • Die Zusammensetzungen, die die vorliegenden humanisierten Antikörper oder einen Cocktail davon enthalten, können für prophylaktische und/oder therapeutische Behandlungen verabreicht werden. In der therapeutischen Anwendung werden die Zusammensetzungen einem Patienten in einer Menge verabreicht, die ausreicht, um die Krankheit und ihre Komplikationen zu heilen oder zumindest teilweise zum Stillstand zu bringen. Eine Menge, die ausreicht, um dies zu erreichen, ist als "therapeutisch wirksame Dosis" definiert. Die Mengen, die für diese Verwendung wirksam sind, werden von der Schwere der Infektion und dem allgemeinen Zustand des Immunsystems des Patienten abhängen, sie werden aber im Allgemeinen im Bereich von ungefähr 1 bis ungefähr 200 mg Antikörper pro Dosis liegen, wobei üblicherweise Dosierungen von 5 bis 25 mg verwendet werden. Es muss daran gedacht werden, dass die Materialien dieser Erfindung im Allgemeinen bei ernsten Krankheitszuständen verwendet werden können, d. h. in lebensbedrohlichen oder potenziell lebensbedrohlichen Situationen. In solchen Fällen ist es im Hinblick auf die Minimierung von körperfremden Substanzen und die geringere Wahrscheinlichkeit von "Fremdsubstanz"-Abweisungen, welche durch die vorliegenden humanisierten Immunoglobuline dieser Erfindung erreicht wird, möglich und kann von dem behandelnden Arzt als erwünscht angesehen werden, wesentliche Überschüsse dieser Antikörper zu verabreichen.
  • In prophylaktischen Anwendungen werden Zusammensetzungen, die die vorliegenden Immunoglobuline oder einen Cocktail davon enthalten, an einen Patienten verabreicht, der sich noch nicht in einem Krankheitszustand befindet, um die Resistenz des Patienten zu verbessern. Eine solche Menge ist als "prophylaktisch wirksame Dosis" definiert. Bei dieser Verwendung hängen die genauen Mengen von dem Gesundheitszustand des Patienten und dem allgemeinen Level an Immunität ab, reichen im Allgemeinen aber von 0,1 bis 25 mg pro Dosis.
  • Es können einzelne oder mehrere Verabreichungen der Zusammensetzungen durchgeführt werden, wobei die Dosislevel und die Dosismuster von dem behandelnden Arzt ausgewählt werden. In jedem Fall sollten die pharmazeutischen Formulierungen eine Menge des/der Antikörper/s dieser Erfindung bereitstellen, die ausreichend ist, um den Patienten effektiv zu behandeln.
  • Für diagnostische Zwecke können die Antikörper entweder markiert oder unmarkiert sein. Unmarkierte Antikörper können in Kombination mit anderen markierten Antikörpern (sekundären Antikörpern) verwendet werden, die mit dem humanisierten Antikörper reagieren, wie Antikörper, die spezifisch sind für humane konstante Regionen von Immunoglobulinen. Alternativ können die Antikörper direkt markiert werden. Es können eine weitreichende Vielzahl von Markierungen verwendet werden, wie Radionuklide, fluoreszierende Mittel, Enzyme, Enzymsubstrate, Enzym-Cofaktoren, Enzyminhibitoren, Liganden (insbesondere Haptene) etc. Es sind eine Vielzahl von Arten von Immunoassays erhältlich und dem Fachmann wohlbekannt.
  • Die folgenden Beispiele werden zur Veranschaulichung und nicht zur Beschränkung angegeben.
  • Die Herstellung von humanisiertem M195-Antikörper (Tanimoto et al., Leukemia 3, 339 (1989)), welcher an das CD33-Antigen bindet, ist unten beschrieben.
  • cDNAs für die Gene für die variable Domäne der schweren Kette und leichten Kette des Antikörpers wurden im Wesentlichen unter Verwendung von verankerten Polymerasekettenreaktionen kloniert (Loh et al., Science 243, 219 (1989)), wobei 3'-Primer, die an die konstanten Regionen hybridisieren und Hind III-Stellen enthielten, und 5'-Primer verwendet wurden, die an die dG-Schwänze hybridisieren und EcoRI-Stellen enthielten (das Schema ist in 2 gezeigt). Die PCR-amplifizierten Fragmente wurden mit EcoRI und Hind III verdaut und zur Sequenzierung in den pUC18-Vektor kloniert. Es wurden mindestens zwei schwere Ketten und zwei Kappa-Klone sequenziert und es wurde gefunden, dass sie die gleiche Sequenz aufweisen. Die abgeleiteten Aminosäure-Sequenzen der reifen variablen Regionen der leichten und schweren Kette sind in 1, obere Zeilen, gezeigt.
  • Um die hohe Bindungsaffinität des humanisierten Antikörpers beizubehalten, wurden bei der Gestaltung des Antikörpers die Prinzipien und Kategorien, die oben beschrieben sind, angewandt. Basierend auf einer hohen Sequenzhomologie wurde der humane Eu-Antikörper ausgewählt, um sowohl die leichte als auch schwere Kette des humanen Akzeptor-Frameworks für den Maus-Antikörper bereitzustellen.
  • Es wurden die Computerprogramme ABMOD und ENCAD (Levitt, J. Mol. Biol. 168, 595 (1983) und Zilber et al., Biochemistry 29, 10032 (1990)) verwendet, um ein Modell der variablen Region des Maus-Antikörpers zu konstruieren. Das Modell wurde verwendet, um die Aminosäuren in jedem Framework zu bestimmen, welche nahe genug zu den CDRs waren, um potenziell mit ihnen wechselzuwirken (Kategorie 4 oben). Die Positionen, von denen gefunden wurde, dass sie in die Kategorien (1)–(5) fallen, wie oben definiert, sind in Tabelle 1 angegeben, nummeriert wie in 1.
  • TABELLE 1 M195-Antikörper
    Figure 00300001
  • Bei der Gestaltung des humanisierten Antikörpers wurde die Aminosäure an jeder Position so ausgewählt, dass sie gleich ist wie in der humanen Akzeptor-Sequenz, es sei denn, die Position fiel in die Kategorien (1)–(4), wobei dann die Aminosäure von der Maus-Donor-Sequenz verwendet wurde, oder sie fiel in Kategorie (5), wobei dann eine Aminosäure verwendet wurde, die typisch ist für humane Sequenzen an dieser Position.
  • Für die Konstruktion von Genen für die humanisierten Antikörper wurden Nukleotidsequenzen ausgewählt, die für die Proteinsequenzen der humanisierten schweren und leichten Ketten kodieren, einschließlich Signalpeptiden, typischerweise von den Maus-Antikörper-Ketten, im Allgemeinen unter Verwendung von Codons, die in der Maussequenz gefunden werden. Es wurden mehrere degenerierte Codons verändert, um Restriktionsstellen zu bilden, oder um unerwünschte zu entfernen. Die Nukleotidsequenzen enthielten auch Splice-Donor-Signale, die typisch sind für Immunoglobulin-Gene, und eine Xbal-Stelle an jedem Ende. Jedes Gen wurde aus vier überlappenden synthetischen Oligonukleotiden konstruiert. Für jedes Gen einer variablen Domäne wurden zwei Paare an überlappenden Oligonukleotiden an alternierenden Strängen synthetisiert, welche die gesamten Kodierungssequenzen sowie das Signalpeptid und das Splice-Donor-Signal umfassten. Die Oligonukleotide wurden auf einem Applied Biosystems 380B DNA-Synthetisierer synthetisiert. Jedes Oligo wies eine Länge von ungefähr 110–140 Basen mit einer 15–20 Basenüberlappung auf. Doppelsträngige DNA-Fragmente wurden mit Klenow- oder Taq-Polymerase oder Sequenase aus jedem Paar an Oligonukleotiden synthetisiert, mit Restriktionsenzymen verdaut, an den pUC18-Vektor ligiert und sequenziert. Zwei Fragmente mit den entsprechenden korrekten Halbsequenzen wurden dann in die Xbal-Stellen von pVg1-dhfr (schwere Kette)- oder pVk (leichte Kette)-Expressionsvektoren in den geeigneten Orientierungen ligiert, um die kompletten Gene der schweren und leichten Kette zu erzeugen. Die Reaktionen wurden unter Bedingungen durchgeführt, die im Fachgebiet wohlbekannt sind (Maniatis et al., op. cit.).
  • Die Plasmide der schweren Kette und leichten Kette wurden durch Elektroporation in Sp2/0-Maus-Myelomazellen transfiziert, und die Zellen wurden auf die gpt-Expression hin selektiert. Die Klone wurden durch Untersuchung der Produktion von humanem Antikörper in dem Kulturüberstand mittels ELISA gescreent, und von am besten produzierenden Klonen wurde ein Antikörper aufgereinigt. Der Antikörper wurde aufgereinigt, indem Gewebekulturüberstand über eine Säule von Staphylokokken-Protein-Sepharose CL-4B (Pharmacia) geleitet wurde. Die gebundenen Antikörper wurden mit 0,2 M Glycin-HCl, pH 3,0 eluiert und mit 1 M Tris, pH 8,0 neutralisiert. Der Puffer wurde in PBS ausgetauscht, indem er über eine PD10-Säule (Pharmacia) geleitet wurde.
  • Die Bindung des humanisierten Antikörpers an Zelltypen, die das entsprechende Antigen exprimieren, wurde in U937-Zellen getestet. Wie es durch Fluorozytometrie bestimmt wurde, bindet der humanisierte Antikörper ungefähr genauso gut wie der ursprüngliche Maus-Antikörper und die entsprechenden chimären Antikörper. Darüber hinaus konkurriert der humanisierte Antikörper ungefähr genauso gut wie der entsprechende Maus-Antikörper mit dem radiomarkierten Maus-Antikörper hinsichtlich der Bindung an die Zellen, so dass der humanisierte Antikörper ungefähr die gleiche Bindungsaffinität aufweist wie der Maus-Antikörper, typischerweise im Bereich von zweifach oder besser.
  • Von den vorangehenden Ausführungen wird verstanden werden, dass die humanisierten Immunoglobuline der vorliegenden Erfindung zahlreiche Vorteile gegenüber anderen Antikörpern bieten. Im Vergleich zu anderen monoklonalen Antikörpern kann das vorliegende humanisierte Immunoglobulin ökonomischer produziert werden und im Wesentlichen weniger fremde Aminosäuren enthalten. Diese verringerte Wahrscheinlichkeit der Antigenizität nach der Injektion in einen Menschen stellt eine beträchtliche therapeutische Verbesserung dar.
  • Es folgt eine detaillierte Beschreibung des humanisierten Immunoglobulins.
  • EXPERIMENTE
  • Beispiel
  • Humanisierte Immunoglobuline zu dem CD33-Antigen
  • Pro Jahr treten in den USA ungefähr 10000 bis 15000 neue Fälle von myeloider (auch nicht lymphozytische oder granulozytische Leukämie genannt) Leukämie auf (Cancer Facts & Figures, American Cancer Society, 1987). Es gibt zwei Hauptformen myeloider Leukämie: akute myeloide Leukämie (AML) und chronische myeloide Leukämie (CML). Trotz der Behandlung mit Chemotherapie beträgt die Langzeitüberlebensrate in Patienten mit AML weniger als 10–20% (Clarkson et al., CRC Critical Review in Oncology/Hematology 4, 221 (1986)), und das Überleben mit CML und verwandten Krankheiten wie chronischer myelomonozytärer Leukämie (CMML), chronischer Monozyten-Leukämie (CMMOL) und dem myelodysplastischen Syndrom (MDS) ist sogar noch geringer.
  • Das p67-Protein oder CD33-Antigen wird auf der Oberfläche von Vorläufern der Knochenmarkszellen und der leukämischen Zellen der meisten Fälle von AML, aber nicht auf lymphoiden Zellen oder nicht hämopoetischen Zellen gefunden (siehe Leucocyte Typing III, hrsg. von A. J. McMichael, Oxford University Press, S. 622–629 (1987)). Antikörper, von welchen bekannt ist, dass sie an das CD33-Antigen binden, schließen L4B3, L1 B2 und MY9 ein (Andrews et al., Blood 62, 124 (1983) und Griffin et al., Leukemia Research 8, 521 (1984)).
  • Ein anderer Antikörper, der an CD33 bindet, ist M195 (Tanimoto et al., Leukemia 3, 339 (1989) und Scheinberg et al., Leukemia 3, 440 (1989)). Es wurde die Reaktivität von M195 mit einer breiten Vielzahl von Zellen und Geweben getestet. Bei normalen Zellen wurde von M195 berichtet, dass er nur an manche Monozyten und Knochenmarksvorläuferzellen bindet. In der Forschung wurde auch berichtet, dass er nicht an andere hämopoetische Zellen oder an nicht hämopoetische Gewebe bindet. M195 hat an Zellen der meisten Fälle von AML und in allen Fällen von CML in der Myeloblastenphase gebunden.
  • Es wurde ein klinischer Versuch der Phase I von M195 bei AML durchgeführt (Scheinberg et al., Proc. ASCO 9, 207 (1990)). Es wurde gefunden, dass M195, der mit Iod-131 radiomarkiert war, schnell und spezifisch Leukämiezellen sowohl im Blut als auch in dem Knochenmark ansteuert.
  • Gemäß der vorliegenden Erfindung werden humanisierte Immunoglobuline bereitgestellt, die spezifisch mit CD33-verwandten Epitopen reaktiv sind. Diese Immunoglobuline, welche Bindeaffinitäten für CD33 von mindestens ungefähr 107 M–1 und vorzugsweise 108 M–1 bis 1010 M–1 oder stärker besitzen, sind z. B. in der Lage, Leukämiezellen zu zerstören. Die humanisierten Immunoglobuline weisen ein humanes Framework auf und haben hypervariable Regionen (complementarity determining regions = CDRs) des M195-Maus-Immunoglobulins, das spezifisch reaktiv ist gegenüber dem CD33-Antigen.
  • Es ist wichtig, dass M195 nicht an die ultimativen hämopoetischen Stammzellen bindet, so dass M195, das in der Therapie verwendet wird, minimal damit wechselwirken wird und minimal solche Zellen zerstören wird, welche kritisch sind für die Bildung aller Blutzellen. Somit finden die CD33-spezifischen Immunoglobuline der vorliegenden Erfindung, welche ökonomisch in großen Mengen produziert werden können, z. B. Anwendung bei der Behandlung von Knochenmarkszell-vermittelten Erkrankungen in Menschen mittels einer Vielzahl von Techniken.
  • In einem Aspekt ist die vorliegende Erfindung auf rekombinante DNA-Segmente gerichtet, die für die CDRs der schweren und/oder leichten Kette des monoklonalen Antikörpers M195 kodieren. Die DNA-Segmente, die für diese Regionen kodieren, werden typischerweise an DNA-Segmente gebunden, die für die geeigneten humanen Framework-Regionen kodieren. Beispielhafte DNA-Sequenzen, welche durch Expression für die Polypeptidketten, umfassend die CDRs der schweren und leichten Kette des monoklonalen Antikörpers M195, kodieren, sind in 3 enthalten. Aufgrund der Codondegeneration und nicht kritischen Aminosäure-Substitutionen können leicht andere DNA-Sequenzen gegen diese Sequenzen substituiert werden, wie es unten detailliert beschrieben ist.
  • Die Antikörper der vorliegenden Erfindung werden typischerweise jeweils Anwendung bei der Behandlung von hämatologischen Malignitäten finden. Z. B. schließen typische Krankheitszustände, die behandelt werden können, AML, CML, CMML, CMMOL und MDS ein (siehe im Allgemeinen Hoffbrand & Pettit, Essential Haematology, Blackwell Scientific Publications, Oxford (1980)). Die Antikörper können auch für eine Knochenmarksablation vor der Knochenmarkstransplantation verwendet werden.
  • Alle humanisierten Immunoglobuline der vorliegenden Erfindung können auch in Kombination mit anderen Antikörpern, insbesondere humanisierten Antikörpern, die gegenüber verschiedenen myeloiden Antigenen reaktiv sind, verwendet werden. Z. B. schließen geeignete Antigene, mit welchen ein Cocktail humanisierter Immunoglobuline reagieren kann, CD13, CD14, CD15, CD16 und CD34 ein (siehe Leukocyte Typing III, op. cit., S. 576–732).
  • Die Antikörper können auch als separat verabreichte Zusammensetzungen, die zusammen mit chemotherapeutischen Mitteln verabreicht werden, verwendet werden. Typischerweise können die Mittel Cytosinarabinosid und Daunorubicin einschließen, aber es können auch zahlreiche zusätzliche Mittel (z. B. 6-Thioguanin), die dem Fachmann der Leukämiebehandlung wohlbekannt sind, verwendet werden (siehe Hoffbrand & Pettit, op. cit.). Eine bevorzugte pharmazeutische Zusammensetzung der vorliegenden Erfindung umfasst die Verwendung der vorliegenden Immunoglobuline in Immunotoxinen, um Leukämiezellen abzutöten.
  • Die humanisierten Antikörper der vorliegenden Erfindung können ferner eine weitreichende Vielzahl von Zweckmäßigkeiten in vivo ausüben. Als Beispiel können die Antikörper zur Detektion von CD33-Antigenen, zur Isolierung spezifischer Knochenmarkszellen oder dgl., verwendet werden.
  • EXPERIMENTE
  • Klonierung von Schwerketten- und Leichtketten-cDNA
  • cDNAs für die Gene der variablen Domäne der schweren Kette und leichten Kette wurden unter Verwendung von verankerten Polymerasekettenreaktionen (E. Y. Loh et al., Science 243, (1989)) unter Verwendung von 3'-Primern, die an die konstanten Regionen hybridisieren und Hind III-Stellen enthielten, und 5'-Primern, die an die dG-Schwänze hybridisieren und EcoRI-Stellen enthielten (das Schema ist in 2 gezeigt) kloniert. Die PCR-amplifizierten Fragmente wurden mit EcoRI und Hind III verdaut und zur Sequenzierung in den pUC18-Vektor kloniert. Für M195 wurden zwei Gamma-2a-spezifische und zwei Kappaspezifische Klone sequenziert. Die zwei Gamma-2a-Klone bzw. die zwei Kappa-Klone sind in der Sequenz identisch. Die cDNA-Sequenzen der variablen Domäne und die abgeleiteten Aminosäure-Sequenzen sind in 3 gezeigt.
  • Konstruktion und Expression eines chimären Antikörpers
  • Zur Konstruktion und Expression der Gene der chimären Antikörper wurden zwei Plasmidvektoren hergestellt. Das Plasmid pVg1-dhfr (4A) enthält einen Cytomegalovirus IE1-Promotor und Enhancer (M. Boshart et al., Cell 41, 521 (1985)), das humane genomische Cγ1-Segment, das einen Teil des darauffolgenden Introns enthält, und ein Dihydrofolatreduktase (dhfr)-Gen (Simonsen et al., Proc. Natl. Acad. Sci. USA 80, 2495 (1984)) zur Selektion. Das Plasmid pVk (4B) ist ähnlich zu dem pVg1-dhfr, enthält aber das humane genomische Cκ-Segment und das gpt-Gen. Derivate der variablen Regionen der M195 schweren und leichten Kette wurden von den cDNAs durch Polymerasekettenreaktion hergestellt. Die 5'-Primer hybridisierten an die V-Regionen, beginnend an den ATG-Codons, und enthielten Xbal-Stellen; die 3'-Primer hybridisierten an die letzten 15 Nukleotide der J-Regionen und enthielten Splice-Donor-Signale und Xbal-Stellen (siehe Queen et al., Proc. Natl. Acad. Sci. USA 86, 10029 (1989)). Die modifizierten V-Regionen wurden in die Xbal-Stellen der entsprechenden Plasmidvektoren zwischen dem CMV-Promotor und den Teilintrons der konstanten Regionen kloniert.
  • Für die Expression der chimären Antikörper wurden die Plasmide der schweren Kette und der Kappa-Kette in Sp2/0-Maus-Myelomazellen durch Elektroporation transfiziert und die Zellen wurden hinsichtlich der gpt-Expression selektiert. Die Klone, die eine maximale Menge an vollständigem Antikörper sekretierten, wurden durch ELISA detektiert. Durch Flusszytometrie wurde gezeigt, dass der aufgereinigte chimäre M195-Antikörper an U937-Zellen bindet, welche das CD33-Antigen exprimieren (5).
  • Computer-Modelling von humanisierten Antikörpern
  • Um die hohe Bindungsaffinität in den humanisierten Antikörpern beizubehalten, wurde den allgemeinen Verfahren von Queen et al. gefolgt (siehe Queen et al., Proc. Natl. Acad. Sci. USA 86, 10029 (1989) und WO 90/07861). Je homologer ein humaner Antikörper zu dem ursprünglichen murinen Antikörper ist, desto geringer ist die Wahrscheinlichkeit, dass durch die Kombination der murinen CDRs mit dem humanen Framework Störungen in den CDRs eingeführt werden, die die Affinität verringern könnten. Normalerweise werden zur Bereitstellung der Framework-Sequenzen die schwere Kette und die leichte Kette von dem gleichen humanen Antikörper ausgewählt, um die Möglichkeit der Inkompatibilität beim Zusammenführen der zwei Ketten zu verringern. Basierend auf der Sequenzhomologie-Suche gegen dir NBRF-Proteinsequenz-Datenbank (durchgeführt mit der MicroGenie Sequence Analysis Software (Beckman)), wurde der Antikörper Eu ausgewählt, um die Framework-Sequenzen zur Humanisierung von M195 bereitzustellen.
  • Das Computerprogramm ENCAD (M. Levitt, J. Mol. Biol. 168, 595 (1983)) wurde verwendet, um ein Modell der M195 variablen Region zu konstruieren. Das Modell wurde verwendet, um die Aminosäuren in dem M195-Framework zu bestimmen, die nahe genug zu den CDRs sind, um potenziell mit ihnen wechselzuwirken (Kategorie 4 unten). Um die humanisierten M195 variablen Regionen der leichten und schweren Kette zu gestalten, wurde die Aminosäure an jeder Position so ausgewählt, dass sie die gleiche ist wie in dem Eu-Antikörper, es sei denn, dass die Position in eine oder mehrere der 4 Kategorien fiel:
    • (1) Die Position fiel in eine CDR,
    • (2) Die Eu-Aminosäure war ungewöhnlich für humane Antikörper an dieser Position, wohingegen die M195-Aminosäure typisch war für humane Antikörper an dieser Position,
    • (3) Die Position war unmittelbar neben einer CDR,
    • (4) Das oben beschriebene Modell legte nahe, dass die Aminosäure physikalisch nahe der Antigenbinderegion (CDRs) sein könnte.
  • In Kategorie (2) wird "ungewöhnlich" so interpretiert, dass Aminosäuren eingeschlossen sind, die in weniger als ungefähr 20% der humanen Sequenzen in den gleichen Untergruppen (wie von Kabat et al., op. cit. definiert) wie die leichten und schweren Ketten von Eu auftreten, und "typisch" wird so interpretiert, dass Aminosäuren eingeschlossen sind, die in mehr als ungefähr 25%, aber im Allgemeinen mehr als 50% der humanen Sequenzen in solchen Untergruppen auftreten. Für Positionen in diesen Kategorien wurde die Aminosäure des Maus-M195-Antikörpers verwendet: Die Aminosäuren jeder Kategorie sind in Tabelle 8 gezeigt. Manche Aminosäuren können in mehr als eine Kategorie fallen. Die Endsequenzen der variablen Domänen der leichten und schweren Kette von humanisiertem M195 sind, verglichen mit den Eu-Sequenzen, in 6 gezeigt,
  • TABELLE 8
    Figure 00390001
  • Für die Konstruktion von Genen für die humanisierten Antikörper wurden Nukleotidsequenzen ausgewählt, die für die Proteinsequenzen der humanisierten schweren und leichten Ketten kodieren, einschließlich der gleichen Signalpeptide wie in den Maus-M195-Ketten (3), im Allgemeinen unter Verwendung von Codons, die in der Maussequenz gefunden werden. Es wurden mehrere degenerierte Codons verändert, um Restriktionsstellen zu bilden, oder um unerwünschte zu entfernen. Die Nukleotidsequenzen enthielten auch die gleichen Splice-Donor-Signale, wie sie in den chimären Genen verwendet werden, und eine Xbal-Stelle an jedem Ende. Jedes Gen wurde aus vier überlappenden synthetischen Oligonukleotiden konstruiert. Für jedes Gen einer variablen Domäne wurden zwei Paare an überlappenden Oligonukleotiden an alternierenden Strängen synthetisiert, welche die gesamten Kodierungssequenzen sowie das Signalpeptid und das Splice-Donor-Signal (7) umfassten. Die Oligonukleotide wurden auf einem Applied Biosystems 380B DNA-Synthetisierer synthetisiert. Jedes Oligo wies eine Länge von ungefähr 110–140 Basen mit einer ungefähren Basenüberlappung von 15 auf. Doppelsträngige DNA-Fragmente wurden mit Klenow-Polymerase aus jedem Paar an Oligonukleotiden synthetisiert, mit Restriktionsenzymen verdaut, an den pUC18-Vektor ligiert und sequenziert. Zwei Fragmente mit den entsprechenden korrekten Halbsequenzen wurden dann in Xbal-Stellen der pVg1-dhfr- oder pVk-Expressionsvektoren in den geeigneten Orientierungen ligiert, um die kompletten Gene der schweren und leichten Kette zu erzeugen. Die Reaktionen wurden unter Bedingungen, die im Fachgebiet wohlbekannt sind, durchgeführt (Maniatis, et al., op. cit.).
  • Die Plasmide der schweren Kette und leichten Kette wurden durch Elektroporation in Sp2/0-Maus-Myelomazellen transfiziert und die Zellen wurden auf die gpt-Expression hin selektiert. Die Klone wurden durch Untersuchung der Produktion von humanem Antikörper in dem Kulturüberstand mittels ELISA gescreent, und von am besten produzierenden Klonen wurde Antikörper aufgereinigt. Der Antikörper wurde aufgereinigt, indem Gewebekulturüberstand über eine Säule von Staphylokokken-Protein-Sepharose CL-4B (Pharmacia) geleitet wurde. Der gebundene Antikörper wurde mit 0,2 M Glycin-HCl, pH 3,0 eluiert und mit 1 M Tris, pH 8,0 neutralisiert. Der Puffer wurde in PBS ausgetauscht, indem er über eine PD10-Säule (Pharmacia) geleitet wurde.
  • Eigenschaften von humanisierten Antikörpern
  • Der humanisierte M195-Antikörper wurde im Vergleich zu den murinen und chimären Antikörpern charakterisiert. Der humanisierte Antikörper hat an U937-Zellen in einer fluorozytometrischen Analyse auf eine Weise gebunden, die ähnlich ist wie die des chimären Antikörpers (5), was zeigt, dass er das gleiche CD33-Antigen erkennt.
  • Die Affinität des humanisierten Antikörpers wurde durch Konkurrieren mit dem radioiodierten Maus-M195-Antikörper bestimmt (8). Die Bindeaffinitäten wurden gemäß den Verfahren von Berzofsky (J. A. Berzofsky und I. Berkower, in Fundamental Immunology (Hrsg. W. E. Paul), Raven Press (New York), 595 (1984)) bestimmt. Der Maus-M195 wies eine Affinität auf, die vergleichbar war mit dem veröffentlichten Wert (Tanimoto et al., op. cit.), und der humanisierte M195-Antikörper wies eine Affinität auf, die innerhalb des experimentellen Fehlers gleich war wie die des Maus-M195.
  • Der humanisierte M195 ist nützlich, um eine Antikörper-abhängige Cytotoxizität zu vermitteln, wenn humane Effektorzellen und humane CD33-exprimierende Zellen verwendet werden. Dies ist analog zu anderen humanisierten Antikörpern, wie von Junghans et al., Cancer Research 50, 1495 (1990) berichtet wurde.
  • Leider weist die Verwendung von nicht humanen monoklonalen Antikörpern wie M195 bestimmte Nachteile bei der Behandlung von Menschen auf, insbesondere bei wiederholten therapeutischen Anwendungen.

Claims (5)

  1. Humanisiertes Immunoglobulin, wobei die humanisierte variable Leichtketten-Region eine Sequenz umfasst, die in 1A (unten) gezeigt ist, und die humanisierte variable Schwerketten-Region eine Sequenz umfasst, die in 1B (unten) gezeigt ist.
  2. Humanisiertes Immunoglobulin nach Anspruch 1 in aufgereinigter Form.
  3. Humanisiertes Immunoglobulin nach Anspruch 1 oder Anspruch 2, welches in Gegenwart von humanen Ziel- und Effektorzellen eine Antikörper-abhängige zelluläre Cytotoxizität vermitteln kann.
  4. Verwendung eines humanisierten Immunoglobulins, wie es in Anspruch 1 definiert ist, wobei das Immunoglobulin gegebenenfalls an ein cytotoxisches Mittel konjugiert ist, bei der Herstellung eines Medikamentes zur Behandlung myeloider Leukämie in einem Menschen.
  5. Humanisiertes Immunoglobulin, wie es in Anspruch 1 definiert ist, konjugiert an ein cytotoxisches Mittel, zur Verwendung als Pharmazeutikum.
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CA2098404C (en) 2002-08-20
US6180370B1 (en) 2001-01-30
DE69133326D1 (de) 2003-11-13
US5693761A (en) 1997-12-02
CA2098404A1 (en) 1992-06-20
KR100231090B1 (ko) 1999-11-15
US5530101A (en) 1996-06-25
JPH06503963A (ja) 1994-05-12
EP0566647A1 (de) 1993-10-27
ATE251639T1 (de) 2003-10-15
AU9172691A (en) 1992-07-22
EP0566647B1 (de) 2003-10-08
EP1386932A1 (de) 2004-02-04
JP3276369B2 (ja) 2002-04-22
US5693762A (en) 1997-12-02
EP0566647A4 (de) 1995-06-14
WO1992011018A1 (en) 1992-07-09
US5585089A (en) 1996-12-17
AU7548196A (en) 1997-02-20
AU671949B2 (en) 1996-09-19

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