JP2005000169A - 免疫グロブリン変異体 - Google Patents
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Abstract
【解決手段】a.少なくとも一部の移入可変ドメイン及びヒト重鎖免疫グロブリンサブグループの共通ヒト可変ドメインのアミノ酸配列を得、b.この移入及びヒトアミノ可変ドメイン配列中の相補性決定領域(CDR)アミノ酸配列を同定し、c.ヒトCDRアミノ酸配列を対応する移入CDRアミノ酸に置き換え;d.移入抗体の枠組み構造領域(FR)及び対応する共通抗体のFRのアミノ酸配列を並べ;e.対応する共通抗体残基に非相同である並べたFR配列中の移入抗体FR残基を同定し、f.非同種移入抗体アミノ酸残基について、共通抗体FR配列中の対応するアミノ酸残基を該残基に置き換えることでヒト化抗体を製造する。
【選択図】 なし
Description
本発明の目的は、輸入(移入)非ヒト抗体およびヒト抗体のアミノ酸配列からなるヒト化抗体を作成するための以下の工程からなる方法により達成される:
a.少なくとも一部の輸入抗体可変ドメインおよび共通(コンセンサス)可変ドメインのアミノ酸配列を得;
b.この輸入およびヒト可変ドメイン配列中の相補性決定領域(CDR)のアミノ酸配列を同定し;
c.対応するヒトCDRアミノ酸配列に代えて輸入CDRアミノ酸配列を置換し;
d.輸入抗体の枠組み構造領域(FR)および対応する共通抗体のFRのアミノ酸配列を整列させ;
e.対応する共通抗体残基とは非相同な整列させたFR配列中の輸入抗体FR残基を同定し;
f.非相同な輸入アミノ酸残基が、少なくとも次の効果:
1.抗原と直接非共有結合する;
2.CDRと相互作用する;または
3.VL−VH界面に関係する;
のうちの1つを有すると合理的に予想されるか否かを決定し、そして
g.これらの効果のうち少なくとも1つを有すると合理的に予想されるいずれかの非相同な輸入抗体アミノ酸残基について、その残基を共通抗体FR配列中の対応するアミノ酸残基に代えて置換する。
b.(重鎖の可変ドメインのFR中)2H、4H、24H、36H、37H、39H、43H、45H、49H、58H、60H、67H、68H、69H、70H、73H、74H、75H、76H、78H、91H、92H、93H、および103H。
好ましい態様において、共通FR部位で置換される非CDR残基は、非ヒト抗体の対応する位置に見られる残基である。
DIQMTQSPSSLSASVGDRVTITCRASQDVNTAV
AWYQQKPGKAPKLLIYSASFLESGVPSRFSGSR
SGTDFTLTISSLQPEDFATYYCQQHYTTPPTFG
QGTKVEIKRT
2.配列番号2、これはmuMAb4D5のヒト化変異体の重鎖可変ドメインである:
EVQLVESGGGLVQPGGSLRLSCAASGFNIKDTY
IHWVRQAPGKGLEWVARIYPTNGYTRYADSVKG
RFTISADTSKNTAYLQMNSLRAEDTAVYYCSRW
GGDGFYAMDVWGQGTLVTVSS
別の態様において、本発明はヒト化抗体の製造において使用するための共通抗体可変ドメインアミノ酸配列、そのような共通配列のコンピューター表示を得て、使用し、保存するための方法、そしてそのような配列の配列データを含むコンピューターを提供する。1つの態様において、次の共通抗体可変ドメインアミノ酸配列を提供する:
配列番号3(軽鎖):
DIQMTQSPSSLSASVGDRVTITCRASQDVSSYL
AWYQQKPGKAPKLLIYAASSLESGVPSRFSGSG
SGTDFTLTISSLQPEDFATYYCQQYNSLPYTFG
QGTKVEIKRT、および
配列番号4(重鎖):
EVQLVESGGGLVQPGGSLRLSCAASGFTFSDYA
MSWVRQAPGKGLEWVAVISENGGYTRYADSVKG
RFTISADTSKNTAYLQMNSLRAEDTAVYYCSRW
GGDGFYAMDVWGQGTLVTVSS。
通常、以下の用語または語句は、説明、実施例および請求の範囲において用いられた場合には以下に示す定義を有する。
DIQMTQSPSSLSASVGDRVTITCRASQDVSSYL
AWYQQKPGKAPKLLIYAASSLESGVPSRFSGSG
SGTDFTLTISSLQPEDFATYYCQQYNSLPYTFG
QGTKVEIKRT(配列番号3);
VH共通ドメインは次のアミノ酸配列を有している:
EVQLVESGGGLVQPGGSLRLSCAASGFTFSDYA
MSWVRQAPGKGLEWVAVISENGGYTRYADSVKG
RFTISADTSKNTAYLQMNSLRAEDTAVYYCSRW
GGDGFYAMDVWGQGTLVTVSS(配列番号4)。
これらの配列は共通CDRならびに共通FR残基を含む(例えば図1を参照)。
DIQMTQSPSSLSASVGDRVTITCRASQDVNTAV
AWYQQKPGKAPKLLIYSASFLESGVPSRFSGSR
SGTDFTLTISSLQPEDFATYYCQQHYTTPPTFG
QGTKVEIKRT
(配列番号1、これはhuMAb4D5の軽鎖可変ドメインである);または
EVQLVESGGGLVQPGGSLRLSCAASGFNIKDTY
IHWVRQAPGKGLEWVARIYPTNGYTRYADSVKG
RFTISADTSKNTAYLQMNSLRAEDTAVYYCSRW
GGDGFYAMDVWGQGTLVTVSS
(配列番号2、これはhuMAb4D5の重鎖可変ドメインである)
を含むポリペプチドの生物学的性質を有する任意のポリペプチド配列と定義される。
「制御配列」の用語は、特定の宿主生物における機能的に結合されたコード化配列の発現に必要なDNA配列を意味する。原核生物に適当な制御配列には、例えばプロモーター、所望によりオペレーター配列、リボソーム結合部位、そして可能ならば未だ不完全にしか理解されていない他の配列が含まれる。真核細胞は、プロモーター、ポリアデニル化シグナル、およびエンハンサーを使用することが知られている。
抗体のヒト化のための本発明者らのアプローチにおける不可欠な工程は、輸入およびヒト化抗体のコンピューターグラフィックスモデルの構築である。これらのモデルを用いて、6つの相補性決定領域(CDR)が輸入枠組み構造からヒト枠組み構造へうまく移植し得るか否かを決定し、CDRコンホメーションを維持するために輸入抗体由来のどの枠組み構造をヒト化抗体に組み込むことが必要であるかを決定する。さらに、輸入およびヒト化抗体の配列分析および該モデルの参照は、どの枠組み構造残基が普通でなくてそれゆえに抗原結合または適当な抗体構造の維持に関与することがあり得るかを識別するための助けとなりうる。
本発明の実施において、輸入抗体のヒト化における最初の工程は、その中に輸入配列を組み込むための共通アミノ酸配列を得ることである。次に上述の方法を用いてこれらの配列のためのモデルを得る。本発明の特定の態様において、共通ヒト配列はKabatら[Kabat,E.A.ら, 「免疫学的な興味のあるタンパク質の配列」(National Institutes of Health, Bethesda, MD (1987)]の配列編集物における最も豊富なサブクラス、すなわちVLκサブグループIおよびVHグループIII由来であり、上の定義に示される配列を有する。
a.少なくとも一部の輸入抗体可変ドメインおよび共通可変ドメインのアミノ酸配列を得;
b.輸入およびヒト可変ドメイン配列中の相補性決定領域(CDR)のアミノ酸配列を同定し;
c.対応するヒトCDRアミノ酸配列に代えて輸入CDRアミノ酸配列を置換し;
d.輸入抗体の枠組み構造領域(FR)および対応する共通抗体のFRのアミノ酸配列を整列させ;
e.対応する共通抗体残基とは非相同な整列されたFR配列中の輸入抗体FR残基を同定し;
f.非相同な輸入アミノ酸残基が少なくとも次の効果:
1.抗原と直接非共有結合する;
2.CDRと相互作用するか;または
3.VL−VH界面に関与する;
のうちの1つを有すると合理的に予想されるか否かを決定し、そして
g.これらの効果のうち少なくとも1つを有すると合理的に予想されるいずれかの非相同な輸入抗体アミノ酸残基について、その残基を共通抗体FR配列中の対応するアミノ酸残基の代わりに置換する。
a.(軽鎖の可変ドメインのFR中)4L、35L、36L、38L、43L、44L、46L、58L、62L、63L、64L、65L、66L、67L、68L、69L、70L、71L、73L、85L、87L、98L、または
b.(重鎖の可変ドメインのFR中)2H、4H、24H、36H、37H、39H、43H、45H、49H、58H、60H、67H、68H、69H、70H、73H、74H、75H、76H、78H、91H、92H、93H、および103H。
好ましくは、共通FR部位で置換される非CDR残基は、非ヒト抗体の対応する位置に見られる残基である。所望により、特定のアミノ酸残基が所望でない効果を有することが合理的に予想され得るか否かを決定し、それらの効果を矯正するために上述の他の方法工程を使用することができる。
本発明の特定の態様は天然の抗体およびモノクローナル抗体に関する[これらを以下の実施例中、ATCCに寄託された抗体ハイブリドーマ(以下に開示する)により示す]。従って、本明細書中のモノクローナル抗体の使用についての言及は、天然または本来の抗体ならびにヒト化およびキメラ抗体の使用を含むことを意図している。本明細書中で用いる「抗体」の用語は、特に除外しない限り抗体可変ドメインおよび他の分離可能な抗体ドメインを含む。
本発明の抗体およびポリペプチドのアミノ酸配列変異体(本明細書中、標的ポリペプチドと称する)は、適当なヌクレオチド変化を標的ポリペプチドをコードしているDNAに導入することにより、または所望の標的ポリペプチドのインビトロ合成により製造する。このような変異体には、例えば非ヒト抗体のヒト化変異体、ならびに特定のアミノ酸配列内の残基からの欠失体、または該残基の挿入体または置換体が含まれる。最終の構築物が所望の特徴を有しているならば、欠失、挿入、および置換の任意の組み合わせを行って最終の構築物に到達することができる。さらにアミノ酸の変化により、例えばグリコシル化部位の数または位置の変化、任意の膜アンカー特性の改変、および/または標的ポリペプチドの細胞内位置の改変(天然の標的ポリペプチドの任意のリーダー配列を挿入、欠失もしくはその他の様式でそれに影響を与えることによる)などの標的ポリペプチドの翻訳後プロセシングの改変が可能である。
(1)疎水性:ノルロイシン、met、ala、val、leu、ile;
(2)中性の親水性:cys、ser、thr;
(3)酸性:asp、glu;
(4)塩基性:asn、gln、his、lys、arg;
(5)鎖の配向に影響を与える残基:gly、pro;および
(6)芳香族性:trp、tyr、phe。
標的ポリペプチドをコードしているcDNAまたはゲノムDNAを、さらにクローニング(DNAの増幅)または発現を行うために複製可能なベクターに挿入する。多くのベクターが利用可能であり、適当なベクターの選択は、1)DNA増幅に用いるのかまたは発現のために用いるのか、2)ベクターに挿入すべきDNAのサイズ、3)ベクターにより形質転換すべき宿主細胞に依存するであろう。各々のベクターは、その機能(DNAの増幅またはDNAの発現)および適合性である宿主細胞に依存する様々な成分を含む。通常のベクター成分には、以下に示す1またはそれ以上の成分が含まれるがそれらに限定はされない:シグナル配列、複製起点、1またはそれ以上のマーカー遺伝子、エンハンサー成分、プロモーターおよび転写終結配列。
通常、シグナル配列はベクターの成分であってもよいし、また、ベクター中に挿入される標的ポリペプチドDNAの一部であってもよい。
発現およびクローニングベクターの両方は、1またはそれ以上の選択された宿主細胞中でのベクターの複製を可能にする核酸配列を含む。通常、クローニングベクターにおいて、この配列は宿主染色体DNAとは独立したベクターの複製を可能にする配列であり、複製起点または自立的に複製する配列を含む。このような配列は、様々な細菌、酵母およびウイルスについて周知である。プラスミドpBR322由来の複製起点は、大部分のグラム陰性細菌のために適当であり、2μプラスミド起点は酵母のために適当であり、様々なウイルス起点(SV40、ポリオーマ、アデノウイルス、VSVまたはBPV)は哺乳動物細胞におけるクローニングベクターのために有用である。通常、複製起点成分は哺乳動物発現ベクターのためには必要ではない(通常、SV40起点はそれが初期プロモーターを含むという理由だけで使用することがある)。
発現およびクローニングベクターは選択遺伝子(選択可能なマーカーとも称される)を含むべきである。この遺伝子は、選択的培養培地中で増殖される形質転換された宿主細胞の生存または増殖のために必要なタンパク質をコードする。選択遺伝子を含んでいるベクターで形質転換されていない宿主細胞は、該培養培地中で生存しないであろう。通常の選択遺伝子は、(a)抗生物質または他の毒素、例えばアンピシリン、ネオマイシン、メトトレキセート、またはテトラサイクリンに対する耐性を与えるタンパク質、(b)栄養要求性欠失を補足するタンパク質、または(c)複合培地から得られない重要な栄養素を供給するタンパク質、例えばBacilliに対するD−アラニンラセマーゼをコードしている遺伝子を供給するタンパク質をコードする。
発現およびクローニングベクターは、通常、宿主生物により認識され、かつ標的ポリペプチド核酸に機能的に結合されるプロモーターを含有する。プロモーターは、それらが機能的に結合している例えば標的ポリペプチドをコードしている特定の核酸配列の転写および翻訳を制御する構造遺伝子の出発コドンの上流(5')(通常約100〜1000bp以内)に位置する非翻訳配列である。このようなプロモーターは、通常2つのクラス、誘導性プロモーターおよび構成性プロモーターに分類される。誘導性プロモーターとは、培養条件における若干の変化、例えば栄養素の存在もしくは不在または温度の変化に応じて、それらの制御下にDNAからの増大レベルの転写を開始させるプロモーターである。現在、様々な可能性ある宿主細胞により認識される多数のプロモーターが周知である。これらのプロモーターは、制限酵素消化によりDNA源からプロモーターを取り単離されたプロモーター配列をベクターに挿入することにより、標的ポリペプチドをコードしているDNAに機能的に結合される。天然の標的ポリペプチドプロモーター配列および多くの異種プロモーターの両方を用いて、標的ポリペプチドDNAの増幅および/または発現を指令することができる。しかし、異種プロモーターは通常、天然の標的ポリペプチドプロモーターに比べて、より大きな転写および発現される標的ポリペプチドのより高い収量を可能にするので好ましい。
本発明の標的ポリペプチドをコードしているDNAの高等真核生物による転写は、エンハンサー配列をベクター中に挿入することにより増大することが多い。エンハンサーはDNAのcis作用成分であり、通常約10〜300bpであり、プロモーターに対してその転写を増大させるように作用する。エンハンサーは比較的、配向および位置に無関係であり、転写単位に対して5'[Laminsら, Proc.Natl.Acad.Sci.USA, 78:993 (1981)]および3'[Luskyら, Mol.Cell Biol., 3:1108 (1983)]で見いだされており、イントロン内[Banerjiら, Cell, 33:729 (1983)]ならびにコード化配列自体の中[Osborneら, Mol.Cell Biol., 4:1293 (1984)]に見いだされている。哺乳動物遺伝子(グロビン、エラスターゼ、アルブミン、αフェトプロテインおよびインスリン)由来の多くのエンハンサー配列が現在知られている。しかし、通常は真核細胞ウイルス由来のエンハンサーが使用されるであろう。その例には、複製起点の後期側のSV40エンハンサー(bp100〜270)、サイトメガロウイルス初期プロモーターエンハンサー、複製起点の後期側のポリオーマエンハンサー、そしてアデノウイルスエンハンサーが含まれる。また真核性プロモーターの活性化のためのエンハンサー成分についてはYaniv, Nature, 297:17-18 (1982)を参照。該エンハンサーは、標的ポリペプチドDNAに対して5'または3'の位置でベクター中にスプライスし得るが、プロモーターから5'の部位に位置させるのが好ましい。
真核宿主細胞(酵母、菌、昆虫、植物、動物、ヒト、または他の多細胞性生物由来の有核細胞)において用いられる発現ベクターもまた転写の終結のためおよびmRNAを安定化するために必要な配列を含有するであろう。このような配列は、通常、真核性またはウイルス性DNAまたはcDNAの5'および時には3'非翻訳領域から入手可能である。これらの領域は、標的ポリペプチドをコードしているmRNAの非翻訳部分においてポリアデニル化フラグメントとして転写されるヌクレオチドセグメントを含む。さらに3'非翻訳領域は、転写終結部位を含む。
本明細書中のベクターのクローニングまたは発現のために適当な宿主細胞は、原核生物、酵母、または上記の高等真核細胞である。適当な原核生物には、ユーバクテリア、例えばグラム陰性またはグラム陽性生物、例えばE.coli(大腸菌)、B.subtilisなどのBacilli、P.aeruginosaなどのPseudomonas種、Salmonella typhimuriumuまたはSerratia marcescansが含まれる。1つの好ましいE.coliクローニング宿主はE.coli 294(ATCC 31,446)であるが、他の株、例えばE.coli B、E.coliX1776(ATCC 31,537)、およびE.coli W3110(ATCC 27,325)も適している。これらの例は説明のための例であって限定するものではない。宿主細胞が極小量のタンパク質分解酵素を分泌するのが好ましい。別法では、インビトロクローニング法、例えばPCRまたは他の核酸ポリメラーゼ反応が適している。
本発明の標的ポリペプチドを産生させるために用いる原核細胞は、Sambrookら(上記)により一般的に開示されている適当な培地中で培養する。
遺伝子の増幅および/または発現は、例えばmRNAの転写の定量のための通常のサザンブロット法、ノーザンブロット法[Thomas, Proc.Natl.Acad.Sci.USA, 77:5201-5205 (1980)]、ドットブロット法(DNA分析)またはin situハイブリッド形成法により、本明細書中で提供される配列に基づいた適当なラべル化プローブを用いて、サンプル中で直接測定することができる。様々なラベルを用いることができるが、最も一般的には放射性同位元素、特に32Pを用いる。しかし、例えばポリヌクレオチド中への導入のためにビオチン−修飾化ヌクレオチドを用いる他の方法もまた用いることができる。次いで、ビオチンはアビジンまたは抗体への結合のための部位として適しており、広範な種類のラベル、例えば放射性核種、蛍光物質、酵素などを用いてラベル化することができる。別法では、DNA二本鎖、RNA二本鎖、およびDNA−RNA雑種二本鎖またはDNA−タンパク質二本鎖を含む特異的な二本鎖を認識し得る抗体を用いることができる。次いで抗体をラベル化し、表面上に二本鎖を形成した上で二本鎖に結合された抗体の存在を検出することができるように二本鎖が該表面に結合している場所でアッセイを行うことができる。
標的ポリペプチドは、好ましくは培養培地から分泌されるポリペプチドとして回収するが、分泌シグナルを有さずに直接発現されたときには宿主細胞溶解物から回収することもできる。
標的ポリペプチドの共有結合修飾は、本発明の範囲内に含まれる。本発明の範囲内に含まれる共有結合修飾の1つの型は、標的ポリペプチドのフラグメントである。約40アミノ酸残基までを有している標的ポリペプチドフラグメントは、化学合成により、または完全長の標的ポリペプチドまたは変異体標的ポリペプチドの酵素的または化学的切断により好都合に調製することができる。標的ポリペプチドまたはそのフラグメントの他の型の共有結合修飾は、標的ポリペプチドまたはそのフラグメントの特定のアミノ酸残基を、選択された側鎖またはNまたはC末端残基と反応し得る有機誘導化物質と反応させることにより該分子中に誘導される。
可能性あるグリコシル化部位のグリコシル化は、Duskinら[J.Biol.Chem. 257, 3105 (1982)]により開示されているように化合物ツニカマイシンの使用により妨げることができる。ツニカマイシンは、タンパク質−N−グリコシド結合の形成をブロックする。
標的ポリペプチドの共有結合修飾の別の型は、標的ポリペプチドを様々な非タンパク質性ポリマー、例えばポリエチレングリコール、ポリプロピレングリコールまたはポリオキシアルキレンにU.S. 4,640,835; 4,496,689; 4,301,144; 4,670,417; 4,791,192または4,179,337に示されている方法で結合させることからなる。
本発明の抗体は、特定の細胞または組織における抗原の発現に対する診断的アッセイにおいて有用である。抗体は検出可能にラベル化し、さらに/または不溶性マトリックス上に固定化する。
さらに本発明は、本発明の抗体の免疫化学的誘導体、例えばイムノトキシン(抗体と細胞障害性部分の結合物)に関する。また、適当なエフェクター機能を、例えばその定常ドメインなどによって保持する抗体を用いて、天然の補体プロセスを通じて溶解を惹起し、さらに通常存在する抗体依存性細胞障害性細胞と相互作用させる。
本発明の特定の態様には、(a)特定の抗原に対して指向性の抗体、および(b)抗体分子が結合する細胞の溶解を媒介し得るサブクラスまたはイソタイプに属している抗体が含まれる。さらに詳細には、これらの抗体は、細胞表面タンパク質と複合体化した上で、血清の補体を活性化および/またはナチュラルキラー細胞またはマクロファージなどのエフェクター細胞を活性化することにより抗体依存性細胞障害(ADCC)を媒介するサブクラスまたはイソタイプに属しているべきである。
本発明の抗体を治療のためにインビボで用いるときには、抗体は治療的に有効な量(すなわち、所望の治療的効果を有する量)で患者に投与する。通常、それらは非経口的に投与されるであろう。投与量および投与処法は、感染の程度、用いられる個々の抗体またはイムノトキシンの性質、例えばその治療的指標、患者、患者の病歴に依存するであろう。抗体またはイムノトキシンを1〜2週間の間連続的に、血管系内の細胞を治療するために静脈内投与を、そして局所のリンパ節を治療するために皮下および腹腔内投与を行うのが有利である。所望により投与は、随伴する治療、例えば併用される照射のサイクル、化学療法的処置、または腫瘍壊死因子、インターフェロンもしくは他の細胞保護的薬物もしくは免疫調節薬物の投与の経過の間に行う。
上記の様に、muMAb4D5の培養物はAmerican Type Culture Collection(12301 Parklawn Drive, Rockville, MD, USA)(ATCC)に寄託されている。
本実施例において、muMAb4D5(chMAb4D5)のキメラ化ならびに重(VH)および軽(VL)鎖可変領域遺伝子の迅速かつ同時のヒト化(新規な「遺伝子変換突然変異誘発」法を用いる)を報告する。8つのヒト化変異体(huMAb4D5)を構築して、我々の分子モデル化によって同定されたかまたは特定のCDRの立体配座に必須であることが既に示唆されているいくつかのFR残基の重要性を精査した[Chothia,C.およびLesk,A.M., J.Mol.Biol. 196: 901-917 (1987); Chothia,C.ら, Nature 342: 877-883 (1989); Tramontano,A.ら, J.Mol.Biol. 215: 175-182 (1990)を参照]。非骨髄腫細胞におけるヒト化変異体の効率的かつ一時的な発現が、p185HER2ECDに対する結合親和性とp185HER2過発現癌細胞に対する抗増殖活性の間の関係を迅速に調べることを可能にした。
可変領域遺伝子のクローニング
muMAb4D5 VHおよびVL遺伝子を、Orlandiら[Orlandi,R.ら, Proc.Natl.Acad.Sci.USA 86: 3833-3837 (1989)]の記載のように、対応するハイブリドーマ[Fendly,B.M.ら, Cancer Res. 50: 1550-1558 (1990)]由来のmRNAのポリメラーゼ連鎖反応(PCR)増幅によって単離した。muMAb4D5 VLおよびVHのアミノ末端配列決定を用いてセンス鎖PCRプライマーを設計し、一方、アンチセンスPCRプライマーはネズミの枠組み構造(フレームワーク)残基[Orlandi,R.ら, Proc.Natl.Acad.Sci.USA 86: 3833-3837 (1989); Kabat,E.A.ら, 「免疫学的に重要なタンパク質の配列」(National Institutes of Health, Bethesda, MD, 1987)]の共通(コンセンサス)配列に基づいており、以下の配列に下線を引くことによって示し、そして配列の後に挙げた指向性クローニングのための制限部位を導入した:
:EcoRV;
VLアンチセンス:5'-GTTTGATCTCCAGCTTGGTACCHSCDCCGAA-3'(配列番号8)
:Asp718;
VHセンス:5'-AGGTSMARCTGCAGSAGTCWGG-3'(配列番号9)
:PstI;および
VHアンチセンス:5'-TGAGGAGACGGTGACCGTGGTCCCTTGGCCCCAG-3'(配列番号10)
:BstEII
(配列中、HはAまたはCまたはTであり、SはCまたはGであり、DはAまたはGまたはTであり、MはAまたはCであり、RはAまたはGであり、そしてWはAまたはTである)。これらPCR生成物をpUC119[Vieira,J.およびMessing,J., Methods Enzymol. 153: 3-11 (1987)]中にクローン化し、それぞれの可変ドメインについて5つのクローンをジデオキシ法[Sanger,F.ら, Proc.Natl.Acad.Sci.USA 74: 5463-5467 (1977)]によって配列決定した。
muMAb4D5 VHおよびVLドメインのモデルを、Brookhavenタンパク質データバンクからの7つのFab構造(登録 1FB4、2RHE、2MCP、3FAB、1FBJ、2HFL、および1REI)に基づく共通の座標(コオーディネート)から別々に構築した。初めにFabフラグメントKOL[Marquart,M.ら, J.Mol.Biol. 141: 369-391 (1980)]をVLおよびVHドメインの鋳型として選択し、次いで追加の構造をそれらの主鎖原子座標(INSIGHTプログラム、Biosym Technologies)を用いてこの構造上に重ね合わせた。それぞれの重ね合わせた構造中の鋳型Cαから類似Cαまでの距離を、それぞれの残基位置について算出した。ある残基の全て(またはほとんど全て)のCα−Cα距離が<1Åであるときには、この位置を共通構造中に包含させた。ほとんどの場合、βシート枠組み構造残基はこれら基準を満たしたが、CDRループは満たさなかった。これら選択した残基のそれぞれについて、個々のN、Cα、C、OおよびCβ原子の平均座標を算出し、次いで固定したCα座標およびAMBER力場(forcefield)[Weiner,S.J.ら, J.Amer.Chem.Soc. 106: 765-784 (1984)]を用いるDISCOVERプログラム(Biosym Technologies)を用いて50サイクルのエネルギー最小化により非標準結合幾何からの得られる偏差を補正した。次いで、ジスルフィド架橋したシステイン残基などの保存性の高い残基の側鎖を、得られた共通構造中に導入した。次に、muMAb4D5 VLおよびVHの配列を、指針としてChothiaら[Chothia,C.ら, Nature 342: 877-883 (1989)]からのCDR立体配座の表を用い、CDR残基から出発して導入した。側鎖の立体配座は、Fab結晶構造、ロータマー(rotamer)ライブラリー[Ponder,J.W.およびRichards,F.M., J.Mol.Biol. 193: 775-791 (1987)]および充填の考慮に基づいて選択した。VH-CDR3はこれら基準から明確な背骨立体配座を割り当てることができなかったので、INSIGHTプログラムを用いた同様の大きさのループの探索から2つのモデルを創製した。第3のモデルを、充填および溶媒暴露の考慮を用いて導いた。次いで、それぞれのモデルを5000サイクルのエネルギー最小化にかけた。
chMAb4D5の軽および重鎖をコードしている遺伝子を、ヒトサイトメガロウイルスエンハンサーおよびプロモーター、5'イントロンならびにSV40ポリアデニル化シグナルを含有する先に記したファージミドベクター[Gorman,C.M.ら, DNA & Prot.Engin.Tech. 2: 3-10 (1990)]中で別々に組立てた。簡単に説明すると、単純なサブクローニング[Boyle,A., 「分子生物学の最近のプロトコール」第3章(F.A.Ausubelら編, Greene Publishing & Wiley-Interscience, New York, 1990)]および部位指向性の突然変異誘発[Carter,P., 「突然変異誘発:実際的アプローチ」第1章(IRL Press, Oxford, UK 1991)]によって、muMAb4D5 VL(図1A)およびREIヒトκ1軽鎖CL[Palm,W.およびHilschmann,N., Z.Physiol.Chem. 356: 167-191 (1975)]をコードしている遺伝子セグメントを正確に結合させ、同様にmuMAb4D5 VH(図1B)およびヒトγ1定常領域[Capon,D.J.ら, Nature 337: 525-531 (1989)]の遺伝子も結合させた。このγ1アイソタイプは、対応させた組のキメラ[Bruggemann,M.ら, J.Exp.Med. 166: 1351-1361 (1987)]またはヒト化抗体[Riechmann,L., Nature 332: 323-327 (1988)]を用いる補体依存性細胞毒性およびADCCを支持するために好ましいヒトアイソタイプであることがわかっているので選択した。次いで、PCR生成させたVLおよびVHフラグメント(図1)を突然変異させて、これらがタンパク質レベルで決定したmuMAb4D5の配列を忠実に表すようにした(VH Q1E、VL V104LおよびT109A;変異体はアミノ酸残基と数、それに続く置換アミノ酸で表示する)。ヒトγ1定常領域は、突然変異E359DおよびM361L[Kabat,E.A.ら, 「免疫学的に重要なタンパク質の配列」(National Institutes of Health, Bethesda, MD, 1987)のようなEu番号付与]を除いてEllisonら[Ellison,J.W., Nucleic Acids Res. 13: 4071-4079 (1982)]が報告したものと同一であるが、この抗体を天然に希なAアロタイプからさらに普通のものである非Aアロタイプ[Tramontano,A.ら, J.Mol.Biol. 215: 175-182 (1990)]に変換した。これは、治療を妨げる抗アロタイプ抗体の危険を減少させるためであった。
chMAb4D5の軽鎖および重鎖Fdフラグメント(VHおよびCH1ドメイン)をコードしている遺伝子を一緒にpUC119[Vieira,J.およびMessing,J., Methods Enzymol. 153: 3-11 (1987)]中にサブクローン化して、1回の工程でpAK1を創製し、同時にヒト化した(図2)。簡単に説明すると、VHおよびVLをヒト化するために6つの連続オリゴヌクレオチドの組を設計した(図1)。これらのオリゴヌクレオチドは、長さが28〜83ヌクレオチドであり、ネズミ抗体鋳型に対して0〜19のミス対合を含み、そして両末端に8または9個の完全に対合する残基を有するようにして、効率的なアニーリングおよび隣接オリゴヌクレオチドの連結を促進する。VHおよびVLヒト化オリゴヌクレオチドの組(それぞれ5pモル)をATPまたはγ-32P-ATPのどちらかでホスホリル化し[Carter,P., Methods Enzymol. 154: 382-403 (1987)]、40μlの10mMトリス-HCl(pH8.0)および10mM MgCl2中、〜30分間かかって100℃から室温まで冷却することによって別々にpAK1鋳型(3.7pモル)とアニーリングさせた。このアニーリングさせたオリゴヌクレオチドを、5mM ATP(2μl)および0.1M DTT(2μl)の存在下に14℃で10分間、T4 DNAリガーゼ(12単位;New England Biolabs)とインキュベートすることによって結合させた。6%アクリルアミド配列化ゲルで電気泳動した後、組立てたオリゴヌクレオチドをオートラジオグラフィーで位置決定し、電気溶離によって回収した。組立てたオリゴヌクレオチド(それぞれ、〜0.3pモル)を、Kunkelら[Kunkel,T.A.ら, Methods Enzymol. 154: 367-382 (1987)]に従って調製した一本鎖デオキシウリジン含有pAK1(0.15pモル)と、10μlの40mMトリス-HCl(pH7.5)および16mM MgCl2中、上記のように同時にアニーリングさせた。T7 DNAポリメラーゼを用いてプライマーを延長することによってヘテロ二本鎖DNAを構築し、既に記載されているように大腸菌BMH71-18mutL中に導入した[Carter,P., 「突然変異誘発:実際的アプローチ」第1章(IRL Press, Oxford, UK 1991)]。得られたファージミドDNAプールを、Carter,P.[「突然変異誘発:実際的アプローチ」第1章(IRL Press, Oxford, UK 1991)]およびWells,J.A.ら[Phil.Trans.R.Soc.Lond.A 317: 415-423 (1986)]の記載のように、初めにXhoIを用いて制限精製することによってhuVLについて、次いでStuIを用いて制限選択することによってhuVHについて豊富化した。huVLおよびhuVHの両遺伝子を含有する得られたクローンをヌクレオチド配列決定法[Sanger,F.ら, Proc.Natl.Acad.Sci.USA 74: 5463-5467 (1977)]によって同定し、pAK2と命名した。別のヒト化変異体を部位指向性突然変異誘発[Carter,P., 「突然変異誘発:実際的アプローチ」第1章(IRL Press, Oxford, UK 1991)]によって創製した。次いで、上記の一時的な発現ベクター中のmuMAb4D5 VLおよびVH遺伝子セグメントを、それらのヒト化修飾体と正確に置換した。
適切なMAb4D5軽および重鎖cDNA発現ベクターを、効率の高い方法[Gorman,C.M.ら, DNA & Prot.Engin.Tech. 2: 3-10 (1990); Gorman,C.,「DNAクローニング」vol.II, pp.143-190 (D.M.Glover編, IRL Press, Oxford, UK, 1985)]を用いて、アデノウイルス形質転換したヒト胚腎セルライン293[Graham,F.L.ら, J.Gen.Virol. 36: 59-72 (1977)]中に同時トランスフェクションした。培地を5日目まで毎日集め、細胞を血清不含の培地で再培養した。抗体を培地から回収し、製造元の記載のようにプロテインAセファロースCL-4B(Pharmacia)でアフィニティー精製した。溶出した抗体をG25ゲル濾過によってリン酸緩衝化食塩水に緩衝液交換し、限外濾過(Centriprep-30またはCentricon-100、Amicon)によって濃縮し、滅菌濾過(Millex-GV、Millipore)し、4℃で保存した。抗体濃度は、全免疫グロブリンおよび抗原結合ELISAの両方を用いて測定した。使用した標準はhuMAb4D5-5であり、その濃度はアミノ酸組成分析によって決定しておいた。
ヒト乳腺癌セルラインSK-BR-3の増殖に及ぼすMAb4D5変異体の作用を、飽和MAb4D5濃度を用いて、既に記載されているようにして調べた[Fendly,B.M.ら, Cancer Res. 50: 1550-1558 (1990)]。
MAb4D5変異体の抗原結合親和性を、Fendly,B.M.ら[J.Biol.Resp.Mod. 9: 449-455 (1990)]の記載のように調製した分泌型のp185HER2ECDを用いて測定した。簡単に説明すると、抗体とp185HER2ECDを、平衡に到達したことがわかるまで溶液中でインキュベートした。次いで、Friguetら[Friguet,B.ら, J.Immunol.Methods 77: 305-319 (1985)]に従い、遊離抗体の濃度を固定化p185HER2ECDを用いるELISAによって測定し、これを用いて親和性(Kd)を算出した。
muMAb4D5のヒト化
muMAb4D5 VLおよびVH遺伝子セグメントを、最初にPCRによってクローン化し、配列決定した(図1)。次いで、予め組立てたオリゴヌクレオチドを用いる遺伝子変換突然変異誘発によって可変遺伝子を同時にヒト化した(図2)。鋳型に対して39のミス対合を含む311-merのオリゴヌクレオチドが、muMAb4D5 VLのヒト化に必要な24の同時アミノ酸変化を導いた。muMAb4D5 VHのヒト化には32のアミノ酸変化が必要であり、これはmuMAb4D5鋳型に対して59のミス対合を含む361-merを用いて行なった。配列決定した8つのクローンのうちの2つがhuMAb4D5-5を正確にコードしているが、これらクローンの1つは1個のヌクレオチド欠陥を含んでいた。他の6つのクローンは本質的にヒト化されているが、少数の誤りを含んでいた(キロ塩基あたりに<3のヌクレオチド変化および<1の単一ヌクレオチド削除)。別のヒト化変異体(表3)をhuMAb4D5-5の部位指向性突然変異誘発によって構築した。
通常、FR残基は共通ヒト配列[Kabat,E.A.ら, 「免疫学的に重要なタンパク質の配列」(National Institutes of Health, Bethesda, MD, 1987)]から、そしてCDR残基はmuMAb4D5から選択した。huMAb4D5-1中の選択したヒト残基をそれらのmuMAb4D5対応残基に置換することによって別の変異体を構築した。本発明者らの分子モデル化によって同定されたVH残基71、73、78、93と102ならびにVL残基55と66が存在する。VH残基71は、他の研究者[Tramontano,A.ら, J.Mol.Biol. 215: 175-182 (1990)]により、VH-CDR2の立体配座に必須であることが既に示唆されている。huMAb4D5変異体分子の間のアミノ酸配列の相違は、それらのp185HER2ECD結合親和性およびSK-BR-3細胞に対する最大の抗増殖活性と共に表3に示す。SK-BR-3細胞またはp185HER2ECDへのMAb4D5変異体の結合に対して極めて近似したKd値が得られた(表3)。しかし、p185HER2ECDへのMAb4D5変異体の結合から得られるKd評価値はより再現性が高く、小さい標準誤差を有しており、全細胞による結合測定値に比べてかなり少ない量の抗体を消費した。
muMAb4D5は、p185HER2を過発現するヒト乳腫瘍細胞の増殖を阻害する[Hudziak,R.M.ら, Molec.Cell.Biol. 9: 1165-1172 (1989)]。しかし、この抗体は直接的な腫瘍細胞毒性作用の可能性を与えるものではない。この可能性は、huMAb4D5-8の高い親和性(Kd=0.1μM)およびそのヒトIgG1サブタイプの結果としてhuMAb4D5-8に生じる。表4は、正常肺上皮セルラインWI-38(低レベルのp185HER2を発現する)およびSK-BR-3(高レベルのp185HER2を発現する)におけるhuMAb4D5-8により媒介されるADCCをmuMAb4D5と比較するものである。これらの結果により次のことが示される:(1)huMAb4D5はそのネズミの親と比較したときにADCCを行なう能力を大きく増強する;および(2)この活性はp185HER2を過発現する細胞種に選択的でありうる。
muMAb4D5は、それがHER2にコードされているp185HER2受容体様チロシンキナーゼを過発現しているヒト乳および卵巣腫瘍系統に対して細胞増殖抑制性であるので、潜在的にヒト治療に有用である。乳および卵巣癌の両方は慢性疾患であるので、治療用の最適MAb4D5変異体分子が低い免疫原性を有し、作用が専ら細胞増殖抑制性にあるのではなく細胞毒性であることが予想される。muMAb4D5のヒト化はこれら目的を達成するはずである。本発明者らは、p185HER2ECDに強固に結合し(Kd<1nM)、有意の抗増殖活性を有する5つの異なるhuMAb4D5変異体を同定した(表3)。さらに、huMAb4D5-8はmuMAb4D5とは異なり、ヒトγ1アイソタイプに対して予想されるように[Bruggemann,M.ら, J.Exp.Med. 166: 1351-1361 (1987); Riechmann,L.ら, Nature 332: 323-327 (1988)]、ヒトエフェクター細胞の存在下にp185HER2を過発現しているヒト腫瘍セルラインに対してADCCを媒介する(表4)。
本実施例は、上記のヒト化配列を創製するための方法の1つの段階的な仕上げを説明する。これら工程の全てが請求の範囲に記載した発明に必須ではなく、また、各工程を異なる順序で採用してもよいことは理解されるであろう。
2.移入(ヒト化しようとする非ヒトドメイン)可変ドメイン配列のモデルを調製し、共通ヒトモデルとの関連で構造上の相違を観察する。
3.Kabat(上記、1987)および結晶構造基準の両方を用いてヒトおよび移入体中のCDR配列を同定する。これら異なる基準によりCDR同一性にいずれかの相違が存在するときには、CDRの結晶構造規定を用いるが、Kabat残基を移入に重要な枠組み構造残基として保持する。
4.移入CDR配列をヒトCDR配列の代わりに用いて最初の「ヒト化」配列を得る。
5.移入非CDR可変ドメイン配列をヒト化配列と比較し、相違を観察する。
6.移入体がヒト化体と異なっている各アミノ酸残基について以下の分析を行なう:
a.ヒト化残基が全ての種にわたって広くかつ高く保存されている残基であるときには、この残基をヒト化配列中に用いる。この残基が全ての種にわたって保存されていないときには、6bに記載した分析を進める。
b.残基が全ての種にわたって広く保存されていないときには、この残基がヒトにおいて広く保存されているか否かを調べる。
i.この残基がヒトにおいて広く保存されているが移入残基が異なっているときには、移入およびヒト配列の構造モデルを調べ、(1)抗原に直接結合しうるか否か、および(2)CDRの立体配座に影響しうるか否か、を考察することによって、この移入残基がCDRの結合または生物学的活性に影響を及ぼす可能性があるか否かを決定する。この結果がCDRに対する影響がありそうであるというものであるときには、この移入残基を置換する。結果がCDRに対する影響がなさそうであるというものであるときには、このヒト化残基を変えることなく残す。
ii.この残基がヒトにおいても広く保存されていないときには、移入およびヒト配列の構造モデルを調べ、(1)抗原に直接結合しうるか否か、および(2)CDRの立体配座に影響しうるか否か、を考察することによって、この移入残基がCDRの結合または生物学的活性に影響を及ぼす可能性があるか否かを決定する。この結果がCDRに対する影響がありそうであるというものであるときには、この移入残基を置換する。結果がCDRに対する影響がなさそうであるというものであるときには、次の工程に進む。
a)移入およびヒト配列の構造モデルを調べ、残基がドメインの表面に露出しているかまたはその内部に埋没しているかを決定する。残基が露出しているときには、この残基をヒト化配列中に用いる。残基が埋没しているときには、次の工程に進む。
(i) 移入およびヒト配列の構造モデルを調べ、残基がVL-VH界面に影響を及ぼす可能性があるか否かを決定する。界面に関係している残基には、34L、36L、38L、43L、33L、36L、85L、87L、89L、91L、96L、98L、35H、37H、39H、43H、45H、47H、60H、91H、93H、95H、100H、および103Hが含まれる。影響が全くなさそうであるときには、この残基をヒト化配列中に用いる。いくらかの影響がありそうなときには、この移入残基を置換する。
7.CDRの外側のグリコシル化部位について移入配列、共通配列およびヒト化配列を探索し、このグリコシル化部位が抗原結合および/または生物学的活性に何らかの影響を有している可能性があるか否かを決定する。影響が全くなさそうであるときには、このヒト配列を該部位に用い、いくらかの影響がありそうであるときには、このグリコシル化部位を削除するかまたは該部位に移入配列を用いる。
8.上記の分析を完了した後、計画したヒト化配列を決定し、試料を調製し、試験する。この試料が標的抗原に十分に結合しないときには、移入およびヒト化残基の間の残基同一性の問題にかかわらず、以下に挙げる特定の残基を調べる。
a.位置的に巨大分子抗原と直接相互作用する可能性がある特定の周辺(非CDR)可変ドメイン残基を調べる。これには次の残基が含まれる(ここで、*は結晶構造に基づいて抗原と相互作用することが見い出された残基を示す):
i.可変軽鎖ドメイン:36、46、49*、63−70
ii.可変重鎖ドメイン:2、47*、68、70、73−76。
b.可変ドメインCDRの立体配座と相互作用しうるか、または他の方法でこれに影響を及ぼしうる特定の可変ドメイン残基を調べる。これには次の残基が含まれる(CDR残基それ自体は含まない;これは、CDRが互いに相互作用するので、あるCDR中のあらゆる残基が別のCDR残基の立体配座に影響を及ぼしうると考えられるためである)[Lは軽鎖であり、Hは重鎖であり、下線で示した残基はChothiaら, Nature 342: 877 (1989)により構造的に重要であることが示されており、そして、( )内の残基はQueenら(PDL), Proc.Natl.Acad.Sci.USA 86: 10029 (1989)およびProc.Natl.Acad.Sci.USA 88: 2869 (1991)によりヒト化中に変化させた]:
i.可変軽ドメイン:
a)CDR-1(残基24L−34L):2L、4L、66L−69L、
71L
b)CDR-2(残基50L−56L):35L、46L、(47L)、
48L、(49L)、58L、62L、64L−66L、71L、
73L
c)CDR-3(残基89L−97L):2L、4L、36L、98L、
37H、45H、47H、58H、60H
ii.可変重ドメイン:
a)CDR-1(残基26H−35H):2H、4H、24H、36H、
71H、73H、76H、78H、92H、(94H)
b)CDR-2(残基50H−55H):49H、69H、69H、
71H、73H、78H
c)CDR-3(残基95H−102H):このループは他のCDRよりも大きさ
と立体配座が大きく変化するので、このループとの可能な相互作用パートナ
ーとして全ての残基を調べる。
9.工程8の後にヒト化した可変ドメインがなお所望の結合を欠いているときには、工程8を繰り返す。さらに、VL−VH界面に影響を与えうるがCDR立体配座に直接影響を与えることはないであろう全ての埋没残基を再吟味する。また、非CDR残基の溶媒への接近性を評価する。
本実施例は、それぞれのFab'アームの別々の大腸菌発現とその後のインビトロでの指向性化学結合によるヒト化二重特異性抗体BsF(ab')2v1の構築を示すものである。BsF(ab')2v1(抗CD3/抗p185HER2)は、ヒト乳腫瘍セルラインSK-BR-3(癌原遺伝子HER2のp185HER2産物を過発現する)に対するインビトロでのCD3+ CTLの細胞毒活性を再標的化することが示された。本実施例は、ネズミの親抗体と同等の抗原結合親和性および生物学的性質を回復するためにヒト抗体中にできるだけ少ないネズミ残基を設置する最少ヒト化法を示すものである。この方法は、BsF(ab')2v1の抗p185HER2アームに対して非常にうまくいくことがわかった。対照的にBsF(ab')2v1は、ネズミ親の抗CD3抗体の可変ドメインを含有するキメラBsF(ab')2よりもさらに効率悪くその抗CD3アームを介してT細胞に結合する。本実施例において我々は、T細胞に対する抗体結合を改善する試みの中で、選択したネズミ残基を復活させた変異抗CD3アームを含有する別のBsF(ab')2フラグメントを構築した。このような変異体の1つであるBsF(ab')2v9を、BsF(ab')2v1の抗CD3重鎖可変ドメインの第2の超可変ループ中の6個の残基をネズミの親の抗CD3抗体由来の対応残基と置換することによって創製した。BsF(ab')2v9は、BsF(ab')2v1よりもさらに効率的にT細胞(Jurkat)に結合し、キメラBsF(ab')2とほぼ同じ効率で結合する。ヒト化BsF(ab')2のT細胞結合の効率におけるこの改善は、これをp185HER2過発現性癌の治療のための可能性ある治療薬物として展開する際に重要な工程となる。
抗CD3可変領域遺伝子中の突然変異の構築
ファージミドpUC119におけるヒト化抗CD3変異体1(v1)の可変軽(VL)および重(VH)鎖ドメインをコードする遺伝子の構築は開示されている[Shalabyら;上記]。独特の制限部位を設置または除去するミス対合オリゴヌクレオチドを用いる効率的な部位指向性突然変異誘発法[Carter,P., 「突然変異誘発:実際的アプローチ」, (M.J.McPherson編), 第1章, IRL Press, Oxford, UK (1991)]を用いて、別の抗CD3変異体を創製した。用いたオリゴヌクレオチドを以下に挙げる(標的の突然変異を示すために小文字を用いた)。対応する暗号の変化は、1文字コードの出発アミノ酸、続いてKabat,E.A.ら[「免疫学的に重要なタンパク質の配列」, 第5版, National Institutes of Health, Bethesda, MD, USA (1991)]に従って付与した残基番号、次いで置換アミノ酸、そして最後に抗CD3変異体の識別によって示す:
HX11:5'GTAGATAAATCCtctAACACAGCCTAtCTGCAAATG 3' (配列番号11)
:VH K75S、v6;
HX12:5'GTAGATAAATCCAAAtctACAGCCTAtCTGCAAATG 3' (配列番号12)
:VH N76S、v7;
HX13:5'GTAGATAAATCCtcttctACAGCCTAtCTGCAAATG 3' (配列番号13)
:VH K75S:N76S、v8;
X14 :5'CTTATAAAGGTGTTtCcACCTATaaCcAgAaatTCAA
GGatCGTTTCACgATAtcCGTAGATAAATCC 3' (配列番号14)
:VH T57S:A60N:D61Q:S62K:V63F:
G65D、v9;
LX6 :5'CTATACCTCCCGTCTgcatTCTGGAGTCCC 3' (配列番号15)
:VL E55H、v11。
オリゴヌクレオチドHX11、HX12およびHX13のそれぞれはBspMIの部位を除去し、一方、LX6はXhoIの部位を除去し、HX14はEcoRV(下線部)の部位を設置する。抗CD3変異体v10は、オリゴヌクレオチドHX13を用いる部位指向性突然変異誘発によってv9から構築した。突然変異体は、ジデオキシヌクレオチド配列決定法によって確認した[Sanger,F.ら, Proc.Natl.Acad.Sci.USA 74: 5463-5467 (1977)]。
最も好ましいヒト化抗p185HER2変異体HuMAb4D5-8の軽鎖および重鎖Fd'フラグメントの同時分泌のための発現プラスミドpAK19はCarterら(1992b;上記)が開示している。簡単に説明すると、Fab'発現ユニットは、phoAプロモーターの転写支配下で両鎖と二シストロン性である。ヒト化VLおよびVHドメインをコードする遺伝子を、それらの5'側のところで熱安定性エンテロトキシンIIシグナル配列をコードする遺伝子セグメントに、そしてそれらの3'側のところでヒトk1 CLおよびIgG1 CH1定常ドメイン遺伝子にそれぞれ正確に融合させる。このCH1遺伝子のすぐ後にはヒンジ配列CysAlaAlaをコードする配列が続き、バクテリオファージλt0転写ターミネーターが続く。サブクローニングおよび部位指向性突然変異誘発によって、抗p185HER2VLおよびVH遺伝子セグメントを抗CD3抗体のネズミおよび対応するヒト化変異体をコードする遺伝子セグメントとそれぞれ正確に置換することにより、pAK19からキメラおよびヒト化抗CD3変異体[v1〜v4(Shalabyら;上記);v6〜v12(本研究)]のためのFab'発現プラスミドを創製した。本研究において同定された最も強力なヒト化抗CD3変異体(v9)のためのFab'発現プラスミドをpAK22と命名する。この抗p185HER2Fab'フラグメントを、通気した10Lの発酵器中、37℃で32〜40時間増殖させたプラスミドpAK19を含む大腸菌K12株25F2から分泌させた。最終細胞密度は120〜150 OD550であり、可溶性および機能的な抗p185HER2Fab'の力価は抗原結合ELISA[Carterら(1992b);上記]で判定して1〜2g/Lであった。抗CD3 Fab'変異体は、非常に近似した発酵プロトコールを用いて対応する発現プラスミドを含む大腸菌から分泌させた。キメラおよびヒト化抗CD3変異体の最高発現力価は、全免疫グロブリンELISAで判定して、それぞれ200mg/Lおよび700mg/Lであった。
EDTAの存在下にpH5において連鎖球菌プロテインGでアフィニティー精製することによって[Carterら(1992b);上記]、Fab'フラグメントを遊離チオールの形態(Fab'-SH)で大腸菌発酵ペーストから直接回収した。チオエーテル結合したBsF(ab')2フラグメント(抗p185HER2/抗CD3)を、以下の修飾を伴うGlennieら(上記)の方法によって構築した。100mMトリス-酢酸、5mM EDTA(pH5.0)中の抗p185HER2Fab'-SHを、ジメチルホルムアミド中の0.1容量の40mM N,N'-1,2-フェニレンジマレミド(o-PDM)と20℃で〜1.5時間反応させた。過剰のo-PDMを、Fab'マレイミド誘導体(Fab'-mal)のプロテインG精製とその後のcentriprep-30濃縮器(Amicon)を用いる20mM酢酸ナトリウム、5mM EDTA(pH5.3)(結合緩衝液)への緩衝液交換によって除去した。Fab'変異体の全濃度は280nmで測定した吸光度から概算した[HuMAb4D5-8 Fab'e(0.1%)=1.56;Carterら(1992b);上記]。Fab'調製物の遊離のチオール含量は、Creighton,T.E.[「タンパク質構造:実際的アプローチ」, (T.E.Creighton編), 第7章, IRL Press, Oxford, UK (1990)]の記載のように、5,5'-ジチオビス(2-ニトロ安息香酸)との反応によって評価した。等モル量の抗p185HER2Fab'-mal(Fab'-SHとo-PDMの定量反応を仮定)およびそれぞれの抗CD3 Fab'-SH変異体を、4℃で14〜48時間、結合緩衝液中の混合濃度1〜2.5mg/mlで結合させた。この結合反応液をpH7.0の4mMシステインに調節し、20℃で15分間インキュベートして、生成した所望でない全てのジスルフィド結合F(ab')2を還元した。これらの還元条件は、軽鎖と重鎖の間のジスルフィドを実質的に還元することなく重鎖間のジスルフィド結合を還元するのに十分である。次いで、生成した遊離チオールの全てを50mMヨードアセトアミドでブロックした。BsF(ab')2を、PBSの存在下にS100-HR(Pharmacia)サイズ排除クロマトグラフィー(2.5cm×100cm)によって結合反応液から単離した。このBsF(ab')2試料を液体窒素中で凍結させた0.2mmフィルター・フラッシュに通し、−70℃で保存した。
Jurkatヒト急性T細胞白血病セルラインをAmerican Type Culture Collection(Rockville, MD)(ATCC TIB 152)から入手し、ATCC推奨のように増殖させた。106個のJurkat細胞を、適当な濃度のBsF(ab')2(抗p185HER2/抗CD3変異体)または対照の単一特異性抗p185HER2F(ab')2と、0.1%(w/v)ウシ血清アルブミンと10mMアジ化ナトリウムを加えたPBS中、4℃で45分間インキュベートした。この細胞を洗浄し、次いでフルオレセイン-コンジュゲート化したヤギ抗ヒトF(ab')2[Organon Teknika, West Chester, PA]と4℃で45分間インキュベートした。細胞を洗浄し、FACScanR[Becton Dickinson and Co., Mountain View, CA]で分析した。細胞(8×103)をリスト・モードで捕捉し、死んだ細胞と残骸を除外する前方光散乱と側方光散乱によってゲート処理した。
ヒト化抗CD3変異体の設計
先に同定された最も強力なヒト化抗CD3変異体v1は、ネズミの親抗体UCHT1とVL内の107アミノ酸残基のうち19が、そしてVH内の122位置のうち37が異なっている[Shalabyら(1992);上記]。本研究において、我々はCD3に対する結合親和性を改善する試みの中で抗CD3 v1に追加のネズミ残基を復活させた。選択した方法は、復活させる追加のネズミ残基の数と分析すべき抗CD3変異体の数の両方を最少化する折衷法であった。我々の最少限ヒト化処方において当初はヒト配列として維持されていた数個のCDR残基に注意を向けた。即ち、抗CD3 v1のVH CDR2中のヒト残基をそれらのネズミ対応残基と一括して置換し、抗CD3 v9:T57S:A60N:D61Q:S62K:V63F:G65Dを得た(図5)。同様に、抗CD3 v1のVL CDR2中のヒト残基E55をネズミ抗CD3抗体由来のヒスチジンと置換して抗CD3 v11を得た。さらに、抗CD3 v1中のVH枠組み構造領域(FR)残基75および76もそれらのネズミ対応残基と置換して抗CD3 v8:K75S:N76Sを得た。VH残基75および76はVH CDR1およびCDR2に近接したループ中に位置し、従って抗原結合に影響を与えることがある。これら3つの部位の突然変異を組合せることによって創製した別の変異体を以下に記載する。
EDTAの存在下にpH5において連鎖球菌プロテインGでアフィニティー精製することによって[Carterら(1992b);上記]、可溶性および機能的な抗p185HER2および抗CD3 Fab'フラグメントを、主として遊離チオールの形態(Fab'-SHが75〜100%)で1個のヒンジシステインを伴って大腸菌発酵ペーストから直接回収した。次いで、チオエーテル結合したBsF(ab')2フラグメントを、Glennieら(上記)の記載のようにo-PDMを用いる指向性結合によって構築した。一方のアームは常に最も強力なヒト化抗p185HER2変異体HuMAb4D5-8[Carterら(1992b);上記]であり、他方は抗CD3抗体のキメラまたはヒト化変異体のいずれかであった。抗p185HER2Fab'-SHをo-PDMと反応させてマレイミド誘導体(Fab'-mal)を得、次いでそれぞれの抗CD3変異体のFab'-SHに結合させた。次に、F(ab')2を、代表的な調製[BsF(ab')2 v8](データは示さず)に対して示したように、サイズ排除クロマトグラフィーによって未反応のFab'から精製した。このF(ab')フラグメントは、クロマトグラフィーのピークの積分によって判断すると、〜54%の全抗体フラグメント量(質量)を示す。
異なる抗CD3変異体を含むBsF(ab')2のJurkat細胞(ヒト急性T細胞白血病)への結合をフローサイトメトリーにより調べた(データは示さず)。BsF(ab')2 v9は我々の出発分子であるBsF(ab')2 v1よりもさらに高効率で、そしてキメラBsF(ab')2とほぼ同じ効率でJurkat細胞に結合する。追加のネズミ残基を抗CD3 v9中に設置してv10(VH K75S:N76S)およびv12(VH K75S:N76S+VL E55H)を創製しても、対応するBsF(ab')2のJurkat細胞への結合をさらに改善することはなかった。これらネズミ残基を抗CD3 v1中に復活させてもJurkat結合を改善しなかった:VH K75S(v6)、VH N76S(v7)、VH K75S:N76S(v8)、VL E55H(v11)(示さず)。BsF(ab')2 v9はJurkat細胞への結合において最も効率の高い変異体であり、ヒト化抗CD3アームに最も少ないネズミ残基を含んでいるので、これを今後の研究のために選択した。単一特異性の抗p185HER2F(ab')2は、抗CD3アームに媒介される相互作用に一致するJurkat細胞への有意の結合を示さなかった。
臨床においてヒト化抗体の免疫原性の可能性を最少にするための試みの中、本研究においてBsF(ab')2の抗p185HER2[Carterら(1992b);上記]および抗CD3アーム[Shalabyら;上記]をヒト化するために最少限法を選択した。即ち、我々は最少数のネズミCDRおよびFR残基を、共通ヒト可変ドメイン配列構造中に設置することを試みた(ネズミの親抗体と同等の抗原結合親和性および生物学的性質を復活させるのに必要なように)。初めに分子モデル化を用いて抗原結合に重要と思われるネズミFR残基を予測し、第2に必要でないと思われるネズミCDR残基を予測した。次いで、少数のヒト化変異体を構築してこれらの予測を試験した。
白血球付着受容体β鎖に対して指向性のネズミ抗体(H52抗体として既知)を上記の方法に従ってヒト化した。図6Aおよび6Bに、ネズミおよびヒト化抗体の軽鎖および重鎖のアミノ酸配列の比較を示す。
(1) 一般的情報
(i) 特許出願人: ジェネンテク,インコーポレイテッド
(ii) 発明の名称: 免疫グロブリン変異体
(iii) 配列の数: 25
(iv) 連絡先:
(A) 名宛人:ジェネンテク,インコーポレイテッド
(B) 通り:ポイント・サン・ブルーノ・ブールバード460番
(C) 市:サウス・サン・フランシスコ
(D) 州:カリフォルニア
(E) 国:アメリカ合衆国
(F) ZIP:94080
(v) コンピューター解読書式:
(A) 媒体型:5.25インチ、360Kbフロッピーディスク
(B) コンピューター:IBM PC適合
(C) オペレーティング・システム:PC-DOS/MS-DOS
(D) ソフトウエア:patin (ジェネンテク)
(vi) 本出願のデータ:
(A) 出願番号:未 定
(B) 出願日:本 日
(C) 分類:未 定
(vii) 優先権主張出願のデータ:
(A) 出願番号:07/715272
(B) 出願日:1991年6月14日
(viii) 弁理士/代理人 情報:
(A) 氏名:アドラー,キャロライン・アール
(B) 登録番号:32,324
(C) 参照/整理番号:709P1
(ix) 電話連絡先情報:
(A) 電話番号:415/225−2614
(B) ファックス番号:415/952−9881
(C) テレックス番号:910/371−7168
(2) 配列番号1の情報
(i) 配列の特徴:
(A) 長さ:109アミノ酸
(B) 型:アミノ酸
(D) トポロジー:直鎖状
(xi) 配列:配列番号1:
Asp Ile Gln Met Thr Gln Ser Pro Ser Ser Leu Ser Ala Ser Val
1 5 10 15
Gly Asp Arg Val Thr Ile Thr Cys Arg Ala Ser Gln Asp Val Asn
20 25 30
Thr Ala Val Ala Trp Tyr Gln Gln Lys Pro Gly Lys Ala Pro Lys
35 40 45
Leu Leu Ile Tyr Ser Ala Ser Phe Leu Glu Ser Gly Val Pro Ser
50 55 60
Arg Phe Ser Gly Ser Arg Ser Gly Thr Asp Phe Thr Leu Thr Ile
65 70 75
Ser Ser Leu Gln Pro Glu Asp Phe Ala Thr Tyr Tyr Cys Gln Gln
80 85 90
His Tyr Thr Thr Pro Pro Thr Phe Gly Gln Gly Thr Lys Val Glu
95 100 105
Ile Lys Arg Thr
109
(2) 配列番号2の情報
(i) 配列の特徴:
(A) 長さ:120アミノ酸
(B) 型:アミノ酸
(D) トポロジー:直鎖状
(xi) 配列:配列番号2:
Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly
1 5 10 15
Gly Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Phe Asn Ile Lys
20 25 30
Asp Thr Tyr Ile His Trp Val Arg Gln Ala Pro Gly Lys Gly Leu
35 40 45
Glu Trp Val Ala Arg Ile Tyr Pro Thr Asn Gly Tyr Thr Arg Tyr
50 55 60
Ala Asp Ser Val Lys Gly Arg Phe Thr Ile Ser Ala Asp Thr Ser
65 70 75
Lys Asn Thr Ala Tyr Leu Gln Met Asn Ser Leu Arg Ala Glu Asp
80 85 90
Thr Ala Val Tyr Tyr Cys Ser Arg Trp Gly Gly Asp Gly Phe Tyr
95 100 105
Ala Met Asp Val Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser
110 115 120
(2) 配列番号3の情報
(i) 配列の特徴:
(A) 長さ:109アミノ酸
(B) 型:アミノ酸
(D) トポロジー:直鎖状
(xi) 配列:配列番号3:
Asp Ile Gln Met Thr Gln Ser Pro Ser Ser Leu Ser Ala Ser Val
1 5 10 15
Gly Asp Arg Val Thr Ile Thr Cys Arg Ala Ser Gln Asp Val Ser
20 25 30
Ser Tyr Leu Ala Trp Tyr Gln Gln Lys Pro Gly Lys Ala Pro Lys
35 40 45
Leu Leu Ile Tyr Ala Ala Ser Ser Leu Glu Ser Gly Val Pro Ser
50 55 60
Arg Phe Ser Gly Ser Gly Ser Gly Thr Asp Phe Thr Leu Thr Ile
65 70 75
Ser Ser Leu Gln Pro Glu Asp Phe Ala Thr Tyr Tyr Cys Gln Gln
80 85 90
Tyr Asn Ser Leu Pro Tyr Thr Phe Gly Gln Gly Thr Lys Val Glu
95 100 105
Ile Lys Arg Thr
109
(2) 配列番号4の情報
(i) 配列の特徴:
(A) 長さ:120アミノ酸
(B) 型:アミノ酸
(D) トポロジー:直鎖状
(xi) 配列:配列番号4:
Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly
1 5 10 15
Gly Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Ser
20 25 30
Asp Tyr Ala Met Ser Trp Val Arg Gln Ala Pro Gly Lys Gly Leu
35 40 45
Glu Trp Val Ala Val Ile Ser Glu Asn Gly Gly Tyr Thr Arg Tyr
50 55 60
Ala Asp Ser Val Lys Gly Arg Phe Thr Ile Ser Ala Asp Thr Ser
65 70 75
Lys Asn Thr Ala Tyr Leu Gln Met Asn Ser Leu Arg Ala Glu Asp
80 85 90
Thr Ala Val Tyr Tyr Cys Ser Arg Trp Gly Gly Asp Gly Phe Tyr
95 100 105
Ala Met Asp Val Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser
110 115 120
(2) 配列番号5の情報
(i) 配列の特徴:
(A) 長さ:109アミノ酸
(B) 型:アミノ酸
(D) トポロジー:直鎖状
(xi) 配列:配列番号5:
Asp Ile Val Met Thr Gln Ser His Lys Phe Met Ser Thr Ser Val
1 5 10 15
Gly Asp Arg Val Ser Ile Thr Cys Lys Ala Ser Gln Asp Val Asn
20 25 30
Thr Ala Val Ala Trp Tyr Gln Gln Lys Pro Gly His Ser Pro Lys
35 40 45
Leu Leu Ile Tyr Ser Ala Ser Phe Arg Tyr Thr Gly Val Pro Asp
50 55 60
Arg Phe Thr Gly Asn Arg Ser Gly Thr Asp Phe Thr Phe Thr Ile
65 70 75
Ser Ser Val Gln Ala Glu Asp Leu Ala Val Tyr Tyr Cys Gln Gln
80 85 90
His Tyr Thr Thr Pro Pro Thr Phe Gly Gly Gly Thr Lys Leu Glu
95 100 105
Ile Lys Arg Ala
109
(2) 配列番号6の情報
(i) 配列の特徴:
(A) 長さ:120アミノ酸
(B) 型:アミノ酸
(D) トポロジー:直鎖状
(xi) 配列:配列番号6:
Glu Val Gln Leu Gln Gln Ser Gly Pro Glu Leu Val Lys Pro Gly
1 5 10 15
Ala Ser Leu Lys Leu Ser Cys Thr Ala Ser Gly Phe Asn Ile Lys
20 25 30
Asp Thr Tyr Ile His Trp Val Lys Gln Arg Pro Glu Gln Gly Leu
35 40 45
Glu Trp Ile Gly Arg Ile Tyr Pro Thr Asn Gly Tyr Thr Arg Tyr
50 55 60
Asp Pro Lys Phe Gln Asp Lys Ala Thr Ile Thr Ala Asp Thr Ser
65 70 75
Ser Asn Thr Ala Tyr Leu Gln Val Ser Arg Leu Thr Ser Glu Asp
80 85 90
Thr Ala Val Tyr Tyr Cys Ser Arg Trp Gly Gly Asp Gly Phe Tyr
95 100 105
Ala Met Asp Tyr Trp Gly Gln Gly Ala Ser Val Thr Val Ser Ser
110 115 120
(2) 配列番号7の情報
(i) 配列の特徴:
(A) 長さ:27塩基
(B) 型:核酸
(C) 鎖の数:一本鎖
(D) トポロジー:直鎖状
(xi) 配列:配列番号7:
TCCGATATCC AGCTGACCCA GTCTCCA 27
(2) 配列番号8の情報
(i) 配列の特徴:
(A) 長さ:31塩基
(B) 型:核酸
(C) 鎖の数:一本鎖
(D) トポロジー:直鎖状
(xi) 配列:配列番号8:
GTTTGATCTC CAGCTTGGTA CCHSCDCCGA A 31
(2) 配列番号9の情報
(i) 配列の特徴:
(A) 長さ:22塩基
(B) 型:核酸
(C) 鎖の数:一本鎖
(D) トポロジー:直鎖状
(xi) 配列:配列番号9:
AGGTSMARCT GCAGSAGTCW GG 22
(2) 配列番号10の情報
(i) 配列の特徴:
(A) 長さ:34塩基
(B) 型:核酸
(C) 鎖の数:一本鎖
(D) トポロジー:直鎖状
(xi) 配列:配列番号10:
TGAGGAGACG GTGACCGTGG TCCCTTGGCC CCAG 34
(2) 配列番号11の情報
(i) 配列の特徴:
(A) 長さ:36塩基
(B) 型:核酸
(C) 鎖の数:一本鎖
(D) トポロジー:直鎖状
(xi) 配列:配列番号11:
GTAGATAAAT CCTCTAACAC AGCCTATCTG CAAATG 36
(2) 配列番号12の情報
(i) 配列の特徴:
(A) 長さ:36塩基
(B) 型:核酸
(C) 鎖の数:一本鎖
(D) トポロジー:直鎖状
(xi) 配列:配列番号12:
GTAGATAAAT CCAAATCTAC AGCCTATCTG CAAATG 36
(2) 配列番号13の情報
(i) 配列の特徴:
(A) 長さ:36塩基
(B) 型:核酸
(C) 鎖の数:一本鎖
(D) トポロジー:直鎖状
(xi) 配列:配列番号13:
GTAGATAAAT CCTCTTCTAC AGCCTATCTG CAAATG 36
(2) 配列番号14の情報
(i) 配列の特徴:
(A) 長さ:68塩基
(B) 型:核酸
(C) 鎖の数:一本鎖
(D) トポロジー:直鎖状
(xi) 配列:配列番号14:
CTTATAAAGG TGTTTCCACC TATAACCAGA AATTCAAGGA TCGTTTCACG 50
ATATCCGTAG ATAAATCC 68
(2) 配列番号15の情報
(i) 配列の特徴:
(A) 長さ:30塩基
(B) 型:核酸
(C) 鎖の数:一本鎖
(D) トポロジー:直鎖状
(xi) 配列:配列番号15:
CTATACCTCC CGTCTGCATT CTGGAGTCCC 30
(2) 配列番号16の情報
(i) 配列の特徴:
(A) 長さ:107アミノ酸
(B) 型:アミノ酸
(D) トポロジー:直鎖状
(xi) 配列:配列番号16:
Asp Ile Gln Met Thr Gln Thr Thr Ser Ser Leu Ser Ala Ser Leu
1 5 10 15
Gly Asp Arg Val Thr Ile Ser Cys Arg Ala Ser Gln Asp Ile Arg
20 25 30
Asn Tyr Leu Asn Trp Tyr Gln Gln Lys Pro Asp Gly Thr Val Lys
35 40 45
Leu Leu Ile Tyr Tyr Thr Ser Arg Leu His Ser Gly Val Pro Ser
50 55 60
Lys Phe Ser Gly Ser Gly Ser Gly Thr Asp Tyr Ser Leu Thr Ile
65 70 75
Ser Asn Leu Glu Gln Glu Asp Ile Ala Thr Tyr Phe Cys Gln Gln
80 85 90
Gly Asn Thr Leu Pro Trp Thr Phe Ala Gly Gly Thr Lys Leu Glu
95 100 105
Ile Lys
107
(2) 配列番号17の情報
(i) 配列の特徴:
(A) 長さ:107アミノ酸
(B) 型:アミノ酸
(D) トポロジー:直鎖状
(xi) 配列:配列番号17:
Asp Ile Gln Met Thr Gln Ser Pro Ser Ser Leu Ser Ala Ser Val
1 5 10 15
Gly Asp Arg Val Thr Ile Thr Cys Arg Ala Ser Gln Asp Ile Arg
20 25 30
Asn Tyr Leu Asn Trp Tyr Gln Gln Lys Pro Gly Lys Ala Pro Lys
35 40 45
Leu Leu Ile Tyr Tyr Thr Ser Arg Leu Glu Ser Gly Val Pro Ser
50 55 60
Arg Phe Ser Gly Ser Gly Ser Gly Thr Asp Tyr Thr Leu Thr Ile
65 70 75
Ser Ser Leu Gln Pro Glu Asp Phe Ala Thr Tyr Tyr Cys Gln Gln
80 85 90
Gly Asn Thr Leu Pro Trp Thr Phe Gly Gln Gly Thr Lys Val Glu
95 100 105
Ile Lys
107
(2) 配列番号18の情報
(i) 配列の特徴:
(A) 長さ:107アミノ酸
(B) 型:アミノ酸
(D) トポロジー:直鎖状
(xi) 配列:配列番号18:
Asp Ile Gln Met Thr Gln Ser Pro Ser Ser Leu Ser Ala Ser Val
1 5 10 15
Gly Asp Arg Val Thr Ile Thr Cys Arg Ala Ser Gln Ser Ile Ser
20 25 30
Asn Tyr Leu Ala Trp Tyr Gln Gln Lys Pro Gly Lys Ala Pro Lys
35 40 45
Leu Leu Ile Tyr Ala Ala Ser Ser Leu Glu Ser Gly Val Pro Ser
50 55 60
Arg Phe Ser Gly Ser Gly Ser Gly Thr Asp Phe Thr Leu Thr Ile
65 70 75
Ser Ser Leu Gln Pro Glu Asp Phe Ala Thr Tyr Tyr Cys Gln Gln
80 85 90
Tyr Asn Ser Leu Pro Trp Thr Phe Gly Gln Gly Thr Lys Val Glu
95 100 105
Ile Lys
107
(2) 配列番号19の情報
(i) 配列の特徴:
(A) 長さ:129アミノ酸
(B) 型:アミノ酸
(D) トポロジー:直鎖状
(xi) 配列:配列番号19:
Glu Val Gln Leu Gln Gln Ser Gly Pro Glu Leu Val Lys Pro Gly
1 5 10 15
Ala Ser Met Lys Ile Ser Cys Lys Ala Ser Gly Tyr Ser Phe Thr
20 25 30
Gly Tyr Thr Met Asn Trp Val Lys Gln Ser His Gly Lys Asn Leu
35 40 45
Glu Trp Met Gly Leu Ile Asn Pro Tyr Lys Gly Val Ser Thr Tyr
50 55 60
Asn Gln Lys Phe Lys Asp Arg Phe Thr Ile Ser Lys Ala Thr Leu
65 70 75
Thr Val Asp Lys Ser Ser Ser Thr Ala Tyr Leu Met Glu Leu Leu
80 85 90
Asn Ser Leu Thr Ser Glu Asp Ser Ala Val Tyr Tyr Cys Ala Arg
95 100 105
Ser Gly Tyr Tyr Gly Asp Ser Asp Trp Tyr Phe Asp Val Trp Gly
110 115 120
Ala Gly Thr Thr Val Thr Val Ser Ser
125 129
(2) 配列番号20の情報
(i) 配列の特徴:
(A) 長さ:122アミノ酸
(B) 型:アミノ酸
(D) トポロジー:直鎖状
(xi) 配列:配列番号20:
Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly
1 5 10 15
Gly Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Tyr Ser Phe Thr
20 25 30
Gly Tyr Thr Met Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu
35 40 45
Glu Trp Val Ala Leu Ile Asn Pro Tyr Lys Gly Val Ser Thr Tyr
50 55 60
Asn Gln Lys Phe Lys Asp Arg Phe Thr Ile Ser Val Asp Lys Ser
65 70 75
Lys Asn Thr Ala Tyr Leu Gln Met Asn Ser Leu Arg Ala Glu Asp
80 85 90
Thr Ala Val Tyr Tyr Cys Ala Arg Ser Gly Tyr Tyr Gly Asp Ser
95 100 105
Asp Trp Tyr Phe Asp Val Trp Gly Gln Gly Thr Leu Val Thr Val
110 115 120
Ser Ser
122
(2) 配列番号21の情報
(i) 配列の特徴:
(A) 長さ:122アミノ酸
(B) 型:アミノ酸
(D) トポロジー:直鎖状
(xi) 配列:配列番号21:
Glu Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly
1 5 10 15
Gly Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Ser
20 25 30
Ser Tyr Ala Met Ser Trp Val Arg Gln Ala Pro Gly Lys Gly Leu
35 40 45
Glu Trp Val Ser Val Ile Ser Gly Asp Gly Gly Ser Thr Tyr Tyr
50 55 60
Ala Asp Ser Val Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser
65 70 75
Lys Asn Thr Leu Tyr Leu Gln Met Asn Ser Leu Arg Ala Glu Asp
80 85 90
Thr Ala Val Tyr Tyr Cys Ala Arg Gly Arg Val Gly Tyr Ser Leu
95 100 105
Ser Gly Leu Tyr Asp Tyr Trp Gly Gln Gly Thr Leu Val Thr Val
110 115 120
Ser Ser
122
(2) 配列番号22の情報
(i) 配列の特徴:
(A) 長さ:454アミノ酸
(B) 型:アミノ酸
(D) トポロジー:直鎖状
(xi) 配列:配列番号22:
Gln Val Gln Leu Gln Gln Ser Gly Pro Glu Leu Val Lys Pro Gly
1 5 10 15
Ala Ser Val Lys Ile Ser Cys Lys Thr Ser Gly Tyr Thr Phe Thr
20 25 30
Glu Tyr Thr Met His Trp Met Lys Gln Ser His Gly Lys Ser Leu
35 40 45
Glu Trp Ile Gly Gly Phe Asn Pro Lys Asn Gly Gly Ser Ser His
50 55 60
Asn Gln Arg Phe Met Asp Lys Ala Thr Leu Ala Val Asp Lys Ser
65 70 75
Thr Ser Thr Ala Tyr Met Glu Leu Arg Ser Leu Thr Ser Glu Asp
80 85 90
Ser Gly Ile Tyr Tyr Cys Ala Arg Trp Arg Gly Leu Asn Tyr Gly
95 100 105
Phe Asp Val Arg Tyr Phe Asp Val Trp Gly Ala Gly Thr Thr Val
110 115 120
Thr Val Ser Ser Ala Ser Thr Lys Gly Pro Ser Val Phe Pro Leu
125 130 135
Ala Pro Ser Ser Lys Ser Thr Ser Gly Gly Thr Ala Ala Leu Gly
140 145 150
Cys Leu Val Lys Asp Tyr Phe Pro Glu Pro Val Thr Val Ser Trp
155 160 165
Asn Ser Gly Ala Leu Thr Ser Gly Val His Thr Phe Pro Ala Val
170 175 180
Leu Gln Ser Ser Gly Leu Tyr Ser Leu Ser Ser Val Val Thr Val
185 190 195
Pro Ser Ser Ser Leu Gly Thr Gln Thr Tyr Ile Cys Asn Val Asn
200 205 210
His Lys Pro Ser Asn Thr Lys Val Asp Lys Lys Val Glu Pro Lys
215 220 225
Ser Cys Asp Lys Thr His Thr Cys Pro Pro Cys Pro Ala Pro Glu
230 235 240
Leu Leu Gly Gly Pro Ser Val Phe Leu Phe Pro Pro Lys Pro Lys
245 250 255
Asp Thr Leu Met Ile Ser Arg Thr Pro Glu Val Thr Cys Val Val
260 265 270
Val Asp Val Ser His Glu Asp Pro Glu Val Lys Phe Asn Trp Tyr
275 280 285
Val Asp Gly Val Glu Val His Asn Ala Lys Thr Lys Pro Arg Glu
290 295 300
Glu Gln Tyr Asn Ser Thr Tyr Arg Val Val Ser Val Leu Thr Val
305 310 315
Leu His Gln Asp Trp Leu Asn Gly Lys Glu Tyr Lys Cys Lys Val
320 325 330
Ser Asn Lys Ala Leu Pro Ala Pro Ile Glu Lys Thr Ile Ser Lys
335 340 345
Ala Lys Gly Gln Pro Arg Glu Pro Gln Val Tyr Thr Leu Pro Pro
350 355 360
Ser Arg Glu Glu Met Thr Lys Asn Gln Val Ser Leu Thr Cys Leu
365 370 375
Val Lys Gly Phe Tyr Pro Ser Asp Ile Ala Val Glu Trp Glu Ser
380 385 390
Asn Gly Gln Pro Glu Asn Asn Tyr Lys Thr Thr Pro Pro Val Leu
395 400 405
Asp Ser Asp Gly Ser Phe Phe Leu Tyr Ser Lys Leu Thr Val Asp
410 415 420
Lys Ser Arg Trp Gln Gln Gly Asn Val Phe Ser Cys Ser Val Met
425 430 435
His Glu Ala Leu His Asn His Tyr Thr Gln Lys Ser Leu Ser Leu
440 445 450
Ser Pro Gly Lys
454
(2) 配列番号23の情報
(i) 配列の特徴:
(A) 長さ:557アミノ酸
(B) 型:アミノ酸
(D) トポロジー:直鎖状
(xi) 配列:配列番号23:
His His Gln Val Gln Leu Gln Gln Ser Gly Pro Glu Leu Val Lys
1 5 10 15
Pro Gly Ala Ser Val Lys Ile Ser Cys Lys Thr Ser Gly Tyr Thr
20 25 30
Phe Thr Glu Met Gly Trp Ser Cys Ile Ile Leu Phe Leu Val Ala
35 40 45
Thr Ala Thr Gly Val His Ser Glu Val Gln Leu Val Glu Ser Gly
50 55 60
Gly Gly Leu Val Gln Pro Gly Gly Ser Leu Arg Leu Ser Cys Ala
65 70 75
Thr Ser Gly Tyr Thr Phe Thr Glu Tyr Thr Met His Trp Met Arg
80 85 90
Gln Ala Pro Gly Lys Gly Leu Glu Trp Val Ala Gly Ile Asn Pro
95 100 105
Lys Asn Gly Gly Thr Ser His Asn Gln Arg Phe Met Asp Arg Phe
110 115 120
Thr Ile Ser Val Asp Lys Ser Thr Ser Thr Ala Tyr Met Gln Met
125 130 135
Asn Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Tyr Cys Ala Arg
140 145 150
Trp Arg Gly Leu Asn Tyr Gly Phe Asp Val Arg Tyr Phe Asp Val
155 160 165
Trp Gly Gln Gly Thr Leu Val Thr Val Ser Ser Ala Ser Thr Lys
170 175 180
Gly Pro Ser Val Phe Pro Leu Ala Pro Cys Ser Arg Ser Thr Ser
185 190 195
Glu Ser Thr Ala Ala Leu Gly Cys Leu Val Lys Asp Tyr Phe Pro
200 205 210
Glu Pro Val Thr Val Ser Trp Asn Ser Gly Ala Leu Thr Ser Gly
215 220 225
Val His Thr Phe Pro Ala Val Leu Gln Ser Ser Gly Leu Tyr Ser
230 235 240
Leu Ser Ser Val Val Thr Val Thr Ser Ser Asn Phe Gly Thr Gln
245 250 255
Thr Tyr Thr Cys Asn Val Asp His Lys Pro Ser Asn Thr Lys Val
260 265 270
Asp Lys Thr Val Glu Arg Lys Cys Cys Val Thr Cys Pro Pro Cys
275 280 285
Pro Ala Pro Glu Leu Leu Gly Gly Pro Ser Val Phe Leu Phe Pro
290 295 300
Pro Lys Pro Lys Asp Thr Leu Met Ile Ser Arg Thr Pro Glu Val
305 310 315
Thr Cys Val Val Val Asp Val Ser His Glu Asp Pro Glu Val Lys
320 325 330
Glu Cys Pro Pro Cys Pro Ala Pro Pro Val Ala Gly Pro Ser Val
335 340 345
Phe Leu Phe Pro Pro Lys Pro Lys Asp Thr Leu Met Ile Ser Arg
350 355 360
Thr Pro Glu Val Thr Cys Val Val Val Asp Val Ser His Glu Asp
365 370 375
Pro Glu Val Gln Phe Asn Trp Tyr Val Asp Gly Met Glu Val His
380 385 390
Asn Ala Lys Thr Lys Pro Arg Glu Glu Gln Phe Asn Ser Thr Phe
395 400 405
Arg Val Val Ser Val Leu Thr Val Val His Gln Asp Trp Leu Asn
410 415 420
Gly Lys Glu Tyr Lys Cys Lys Val Ser Asn Lys Gly Leu Pro Ala
425 430 435
Pro Ile Glu Lys Thr Ile Ser Lys Thr Lys Gly Gln Pro Arg Glu
440 445 450
Pro Gln Val Tyr Thr Leu Pro Pro Ser Arg Glu Glu Met Thr Lys
455 460 465
Asn Gln Val Ser Leu Thr Cys Leu Val Lys Gly Phe Tyr Pro Ser
470 475 480
Asp Ile Ala Val Glu Trp Glu Ser Asn Gly Gln Pro Glu Asn Asn
485 490 495
Tyr Lys Thr Thr Pro Pro Met Leu Asp Ser Asp Gly Ser Phe Phe
500 505 510
Leu Tyr Ser Lys Leu Thr Val Asp Lys Ser Arg Trp Gln Gln Gly
515 520 525
Asn Val Phe Ser Cys Ser Val Met His Glu Ala Leu His Asn His
530 535 540
Tyr Thr Gln Lys Ser Leu Ser Leu Ser Pro Gly Lys
545 550 555
(2) 配列番号24の情報
(i) 配列の特徴:
(A) 長さ:214アミノ酸
(B) 型:アミノ酸
(D) トポロジー:直鎖状
(xi) 配列:配列番号24:
Asp Val Gln Met Thr Gln Thr Thr Ser Ser Leu Ser Ala Ser Leu
1 5 10 15
Gly Asp Arg Val Thr Ile Asn Cys Arg Ala Ser Gln Asp Ile Asn
20 25 30
Asn Tyr Leu Asn Trp Tyr Gln Gln Lys Pro Asn Gly Thr Val Lys
35 40 45
Leu Leu Ile Tyr Tyr Thr Ser Thr Leu His Ser Gly Val Pro Ser
50 55 60
Arg Phe Ser Gly Ser Gly Ser Gly Thr Asp Tyr Ser Leu Thr Ile
65 70 75
Ser Asn Leu Asp Gln Glu Asp Ile Ala Thr Tyr Phe Cys Gln Gln
80 85 90
Gly Asn Thr Leu Pro Pro Thr Phe Gly Gly Gly Thr Lys Val Glu
95 100 105
Ile Lys Arg Thr Val Ala Ala Pro Ser Val Phe Ile Phe Pro Pro
110 115 120
Ser Asp Glu Gln Leu Lys Ser Gly Thr Ala Ser Val Val Cys Leu
125 130 135
Leu Asn Asn Phe Tyr Pro Arg Glu Ala Lys Val Gln Trp Lys Val
140 145 150
Asp Asn Ala Leu Gln Ser Gly Asn Ser Gln Glu Ser Val Thr Glu
155 160 165
Gln Asp Ser Lys Asp Ser Thr Tyr Ser Leu Ser Ser Thr Leu Thr
170 175 180
Leu Ser Lys Ala Asp Tyr Glu Lys His Lys Val Tyr Ala Cys Glu
185 190 195
Val Thr His Gln Gly Leu Ser Ser Pro Val Thr Lys Ser Phe Asn
200 205 210
Arg Gly Glu Cys
214
(2) 配列番号25の情報
(i) 配列の特徴:
(A) 長さ:233アミノ酸
(B) 型:アミノ酸
(D) トポロジー:直鎖状
(xi) 配列:配列番号25:
Met Gly Trp Ser Cys Ile Ile Leu Phe Leu Val Ala Thr Ala Thr
1 5 10 15
Gly Val His Ser Asp Ile Gln Met Thr Gln Ser Pro Ser Ser Leu
20 25 30
Ser Ala Ser Val Gly Asp Arg Val Thr Ile Thr Cys Arg Ala Ser
35 40 45
Gln Asp Ile Asn Asn Tyr Leu Asn Trp Tyr Gln Gln Lys Pro Gly
50 55 60
Lys Ala Pro Lys Leu Leu Ile Tyr Tyr Thr Ser Thr Leu His Ser
65 70 75
Gly Val Pro Ser Arg Phe Ser Gly Ser Gly Ser Gly Thr Asp Tyr
80 85 90
Thr Leu Thr Ile Ser Ser Leu Gln Pro Glu Asp Phe Ala Thr Tyr
95 100 105
Tyr Cys Gln Gln Gly Asn Thr Leu Pro Pro Thr Phe Gly Gln Gly
110 115 120
Thr Lys Val Glu Ile Lys Arg Thr Val Ala Ala Pro Ser Val Phe
125 130 135
Ile Phe Pro Pro Ser Asp Glu Gln Leu Lys Ser Gly Thr Ala Ser
140 145 150
Val Val Cys Leu Leu Asn Asn Phe Tyr Pro Arg Glu Ala Lys Val
155 160 165
Gln Trp Lys Val Asp Asn Ala Leu Gln Ser Gly Asn Ser Gln Glu
170 175 180
Ser Val Thr Glu Gln Asp Ser Lys Asp Ser Thr Tyr Ser Leu Ser
185 190 195
Ser Thr Leu Thr Leu Ser Lys Ala Asp Tyr Glu Lys His Lys Val
200 205 210
Tyr Ala Cys Glu Val Thr His Gln Gly Leu Ser Ser Pro Val Thr
215 220 225
Lys Ser Phe Asn Arg Gly Glu Cys
230 233
Claims (18)
- 非ヒト移入抗体およびヒト抗体のアミノ酸配列からなるヒト化抗体の製造方法であって、以下の工程を含む法:
a.少なくとも一部の移入可変ドメインおよびヒト重鎖免疫グロブリンサブグループの共通ヒト可変ドメインのアミノ酸配列を得;
b.この移入およびヒトアミノ可変ドメイン配列中の相補性決定領域(CDR)アミノ酸配列を同定し;
c.ヒトCDRアミノ酸配列を対応する移入CDRアミノ酸配列に置き換え;
d.移入抗体の枠組み構造領域(FR)および対応する共通抗体のFRのアミノ酸配列を並べ;
e.対応する共通抗体残基に非相同である並べたFR配列中の移入抗体FR残基を同定し;
f.この非相同の移入アミノ酸残基が、次の効果:
1.直接的に抗原に非共有結合する;
2.CDRと相互作用する;または
3.VL−VH界面に関与する;
の少なくとも1つを有することが合理的に予測されるか否かを決定し;そして
g.これら効果の少なくとも1つを有することが合理的に予測されるいずれかの非同種移入抗体アミノ酸残基について、共通抗体FR配列中の対応するアミノ酸残基を該残基に置き換える。 - いずれかの該非同種残基がドメインの表面に露出しているかまたはその内部に埋没しているかを決定し、残基が露出しているときには共通残基を保持する追加の工程を有する請求項1に記載の方法。
- 非ヒト移入抗体およびヒト抗体のアミノ酸配列からなるヒト化抗体の製造方法であって、以下の工程を含む方法:
a.少なくとも一部の移入可変ドメインおよびヒト重鎖免疫グロブリンサブグループの共通ヒト可変ドメインのアミノ酸配列を得;
b.この移入およびヒトアミノ可変ドメイン配列中の相補性決定領域(CDR)アミノ酸配列を同定し;
c.ヒトCDRアミノ酸配列を対応する移入CDRアミノ酸配列に置き換え;
d.移入抗体の枠組み構造領域(FR)および対応する共通抗体のFRのアミノ酸配列を並べ;
e.対応する共通抗体残基に非同種である並べたFR配列中の移入抗体FR残基を同定し;
f.この非同種の移入アミノ酸残基が、次の効果:
1.直接的に抗原に非共有結合する;
2.CDRと相互作用する;または
3.VL−VH界面に関与する;
の少なくとも1つを有することが合理的に予測されるか否かを決定し;
g.これら効果の少なくとも1つを有することが合理的に予測されるいずれかの非同種移入抗体アミノ酸残基について、共通抗体FR配列中の対応するアミノ酸残基を該残基に置き換え:そして
h.いずれかの非同種移入抗体アミノ酸残基について、いずれかの該非同種残基がドメインの表面に露出しているかまたはその内部に埋没しているかを決定し、残基が露出しているときには共通残基を保持する。 - グリコシル化部位について移入可変ドメイン配列を探索し、いずれかの該グリコシル化部位が抗体の親和性または抗原結合に影響を及ぼすことが合理的に予測されるか否かを決定し、予測されるときには共通配列中でこのグリコシル化部位に置き換える追加の工程を有する請求項1または3に記載の方法。
- 移入配列中の対応するアミノ酸のところに存在しないグリコシル化部位について共通可変ドメイン配列を探索し、このグリコシル化部位が移入配列中に存在しないときには共通グリコシル化部位を含有するアミノ酸残基をこの移入アミノ酸残基に置き換える追加の工程を有する請求項1または3に記載の方法。
- 移入抗体および共通抗体のFR配列を並べ、この並べた共通FR配列と非同種の移入抗体FR残基を同定し、該非同種移入抗体FR残基のそれぞれについて、対応する共通抗体残基がその部位において全ての種にわたって高度に保存されている残基であるか否かを決定し、それが高度に保存されているときには該部位に該共通抗体アミノ酸残基を含有するヒト化抗体を製造することからなる追加の工程を有する請求項1または3に記載の方法。
- 対応する共通抗体残基が、4L、35L、36L、38L、43L、44L、46L、58L、62L、63L、64L、65L、66L、67L、68L、69L、70L、71L、73L、85L、87L、98L、2H、4H、24H、36H、37H、39H、43H、45H、49H、58H、60H、67H、68H、69H、70H、73H、74H、75H、76H、78H、91H、92H、93H、および103Hからなる群から選ばれる請求項1に記載の方法。
- CDRおよびFRを有する移入非ヒト抗体可変ドメインアミノ酸配列の少なくとも一部を得、CDRおよびFRを有する共通ヒト抗体可変ドメインの少なくとも一部のアミノ酸配列を得、この共通ヒト抗体可変ドメイン中のヒトCDRを非ヒトCDRに置き換え、次いで以下の部位:
4L、35L、36L、38L、43L、44L、46L、58L、62L、63L、64L、65L、66L、67L、68L、69L、70L、71L、73L、85L、87L、98L、2H、4H、24H、36H、37H、39H、43H、45H、49H、58H、60H、67H、68H、69H、70H、73H、74H、75H、76H、78H、91H、92H、93H、および103H
の少なくとも1つにおいて共通アミノ酸残基をアミノ酸残基に置き換えることを含む方法。 - 置換された残基が、非ヒト抗体の対応する位置に見い出される残基である請求項8に記載の方法。
- 共通ヒト可変ドメインが、ヒト可変ドメインおよびヒト以外の種に由来する別の可変ドメインに基づく共通である請求項1または8に記載の方法。
- 改善が、Kabatにおける番号付与系における4L、35L、36L、38L、43L、44L、46L、58L、62L、_64L、65L、66L、67L、68L、69L、70L、71L、73L、85L、87L、98L、2H、4H、24H、36H、37H、39H、43H、45H、49H、58H、60H、68H、69H、70H、73H、74H、75H、76H、78H、_92H、および93H_からなる群から選ばれる部位においてヒト残基をアミノ酸残基に置き換えることを含む、ヒト抗体可変ドメイン中に導入された非ヒトCDRを有するヒト化抗体可変ドメイン。
- 置換された残基が、非ヒトCDRを得た非ヒト抗体の対応する位置に見い出される残基である請求項11に記載のヒト化抗体可変ドメイン。
- 群中に挙げた残基以外のヒトFR残基を全く置換しない請求項11に記載のヒト化抗体可変ドメイン。
- 移入抗体可変ドメイン由来のアミノ酸残基を、ヒト重鎖免疫グロブリンサブグループの共通ヒト可変ドメインを示すアミノ酸配列中に導入することを含むヒト化抗体を設計する方法。
- 約4.7M Kdの親和力又はそれより良い親和力でp185HER2を結合するヒト化抗体。
- 抗原を結合する抗体又は抗体断片であって、その重鎖可変ドメインは、枠組み構造領域(FR)に導入された抗原を結合する非ヒト重鎖可変ドメイン相補性決定領域(CDR)アミノ酸残基を含んでなり、枠組み構造領域(FR)はヒト重鎖免疫グロブリンサブグループの共通ヒト可変ドメインを含み、そして場合によりFRアミノ酸置換を更に含み、その置換残基は、(1)非共有結合的に直接抗原を結合するか、(2)CDRと相互作用するか、(3)VL−VH界面に関与するか、又は(4)抗体の抗原結合又は親和性に影響するグリコシル化部位である、抗体又は抗体断片。
- 請求項16に記載の抗体又は抗体断片であって、その軽鎖可変ドメインは、FRに導入された非ヒト軽可変ドメインCDRアミノ酸残基を含み、FRはヒト軽鎖イムノグロブリンサブグループの共通ヒト可変ドメインを含み、そして場合によりFRアミノ酸置換を更に含み、その置換残基は、(1)非共有結合的に直接抗原を結合するか、(2)CDRと相互作用するか、(3)VL−VH界面に関与するか、又は(4)抗体の抗原結合又は親和性に影響するグリコシレーション部位である、抗体又は抗体断片。
- 請求項16又は17に記載の抗体又は断片であって、置換されたFR残基が、非ヒトCDRアミノ酸残基が得られる非ヒト抗体の対応する位置で見出される残基である抗体又は断片。
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2000
- 2000-11-02 US US09/705,686 patent/US6639055B1/en not_active Expired - Fee Related
- 2000-11-02 US US09/705,392 patent/US6719971B1/en not_active Expired - Fee Related
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2004
- 2004-04-05 NL NL300145C patent/NL300145I1/nl unknown
- 2004-06-07 JP JP2004168507A patent/JP2005000169A/ja not_active Withdrawn
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2005
- 2005-01-14 CY CY0500006A patent/CY2500B1/xx unknown
- 2005-10-26 JP JP2005311080A patent/JP2006083180A/ja active Pending
-
2006
- 2006-01-16 CY CY2006001C patent/CY2006001I2/el unknown
- 2006-07-07 GE GEAP20069499A patent/GEP20074141B/en unknown
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2008
- 2008-06-18 JP JP2008158861A patent/JP4836147B2/ja not_active Expired - Lifetime
Cited By (2)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
WO2014126198A1 (ja) | 2013-02-15 | 2014-08-21 | 株式会社ペルセウスプロテオミクス | 抗cdh3ヒト化抗体、その薬剤コンジュゲート、及びそれらの使用 |
US9644028B2 (en) | 2013-02-15 | 2017-05-09 | Perseus Proteomics Inc. | Anti-CDH3 humanized antibody, drug conjugate thereof, and use thereof |
Also Published As
Publication number | Publication date |
---|---|
CA2103059A1 (en) | 1992-12-15 |
JP2008291036A (ja) | 2008-12-04 |
JP4124480B2 (ja) | 2008-07-23 |
AU2250992A (en) | 1993-01-12 |
NL300145I1 (nl) | 2004-06-01 |
ES2206447T3 (es) | 2004-05-16 |
DE69233254D1 (de) | 2004-01-08 |
CY2006001I2 (el) | 2011-02-02 |
ATE255131T1 (de) | 2003-12-15 |
DK0590058T3 (da) | 2004-03-29 |
US5821337A (en) | 1998-10-13 |
CY2500B1 (en) | 2005-09-02 |
EP0590058B1 (en) | 2003-11-26 |
CY2006001I1 (el) | 2010-07-28 |
WO1992022653A1 (en) | 1992-12-23 |
DE122004000008I1 (de) | 2005-06-09 |
DE69233254T2 (de) | 2004-09-16 |
JPH06508267A (ja) | 1994-09-22 |
US6407213B1 (en) | 2002-06-18 |
AU675916B2 (en) | 1997-02-27 |
GEP20074141B (en) | 2007-07-10 |
EP0590058A1 (en) | 1994-04-06 |
US6719971B1 (en) | 2004-04-13 |
JP2006083180A (ja) | 2006-03-30 |
EP0940468A1 (en) | 1999-09-08 |
US6639055B1 (en) | 2003-10-28 |
JP4836147B2 (ja) | 2011-12-14 |
LU91067I2 (fr) | 2004-04-02 |
CA2103059C (en) | 2005-03-22 |
EP1400536A1 (en) | 2004-03-24 |
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