JP6235521B2 - Fcレセプター結合親和性およびエフェクター機能の増加を有する抗原結合分子 - Google Patents
Fcレセプター結合親和性およびエフェクター機能の増加を有する抗原結合分子 Download PDFInfo
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Description
ヒトを含む脊椎動物の免疫系は、多数の器官および細胞型からなり、これらは、侵入する外来性の微生物(抗原)を正確かつ特異的に認識し、これらに結合し、およびこれらを破壊するように進化してきた。リンパ球は、免疫系の適切な機能のために決定的である。これらの細胞は、胸腺、脾臓、および骨髄(成人)において産生され、そして成人の循環系の中に存在する全体の白血球細胞の約30%を表す。2つの主要なリンパ球の亜集団が存在している。T細胞およびB細胞である。T細胞は細胞媒介性免疫の原因であるのに対して、B細胞は抗体産生(体液性免疫)の原因である。しかし、典型的な免疫応答においては、T細胞およびB細胞は相互依存的に機能する。T細胞は、T細胞レセプターが、抗原提示細胞の表面上の主要組織適合性複合体(「MHC」)糖タンパク質に結合される抗原のフラグメントに結合するときに活性化される;このような活性化は、生物学的メディエーターの放出を引き起こし、これは、分化し、かつその抗原に対する抗体(「免疫グロブリン」)を産生するようにB細胞を刺激する。
オリゴサッカリド成分は、物理的安定性、プロテアーゼ攻撃に対する抵抗性、免疫系との相互作用、薬物動態学、および特異的生物学的活性を含む、治療用糖タンパク質の効力に関連する特性に有意に影響を与える。このような特性は、オリゴサッカリドの存在または非存在に依存するのみならず、オリゴサッカリドの特異的構造にもまた依存する可能性がある。オリゴサッカリド構造と糖タンパク質機能との間のある程度の一般化がなされ得る。例えば、特定のオリゴサッカリド構造は、特異的炭水化物結合タンパク質との相互作用を通して血流からの糖タンパク質の急速なクリアランスを媒介するが、他の構造は、抗体によって結合され得、そして望ましくない免疫反応を誘発し得る(Jenkinsら、Nature Biotechnol.14:975−81(1996))
1)このアッセイは、抗体の抗原結合領域によって認識される標的抗原を発現することが知られている標的細胞を使用する;
2)このアッセイは、エフェクター細胞として、ランダムに選択された健常ドナーの血液から単離されたヒト末梢血単球細胞(PBMC)を使用する;
3)このアッセイは以下のプロトコールに従って使用される。
i)PBMCを、標準的な密度遠心分離手順を使用して単離し、RPMI細胞培養培地中、5×106細胞/mlで懸濁する;
ii)標的細胞を、90%よりも高い生存度を有する指数増殖期から、標準的な培養方法によって増殖させ、RPMI細胞培養培地中で洗浄し、100マイクロキュリーの51Crで標識し、細胞培養培地で2回洗浄し、そして105細胞/mlの密度で細胞培養培地中に再懸濁する;
iii)100マイクロリットルの上記の最終的な標的細胞懸濁物を、96ウェルマイクロタイタープレートの各ウェルに移す;
iv)抗体を、細胞培養培地中で4000ng/mlから0.04ng/mlまで段階希釈し、得られる抗体溶液の50マイクロリットルを96ウェルマイクロタイタープレート中の標的細胞に加えて、上記の全体の濃度範囲を網羅する種々抗体濃度を3連で試験する;
v)最大放出(MR)コントロールのために、標識された標的細胞を含む、プレート中の3つのさらなるウェルは、抗体溶液(上記の要点iv)の代わりに、50マイクロリットルの2%(V/V)非イオン性界面活性剤(Nonidet,Sigma,St.Louis)の水溶液を受容する;
vi)自発性放出(SR)コントロールのために、標識された標的細胞を含む、プレート中の3つのさらなるウェルに、抗体溶液(上記の要点iv)の代わりに、50マイクロリットルのRPMI細胞培養培地を受容する;
vii)次いで、96ウェルマイクロタイタープレートを、50×gで1分間遠心分離し、そして1時間4℃でインキュベートする;
viii)50マイクロリットルのPBMC懸濁液(上記の要点i)を各ウェルに加えて25:1のエフェクター:標的細胞比を生じ、そしてプレートをインキュベーター中、5% CO2大気、37℃下に4時間配置する;
ix)各ウェルからの無細胞上清を収集し、実験的に放出された放射能をガンマカウンターを使用して定量する;
x)特異的溶解のパーセンテージを、計算式(ER−MR)/(MR−SR)×100に従って各抗体について計算し、ここで、ERは抗体濃度について定量された平均放射能(上記の要点ixを参照のこと)であり、MRはMRコントロール(上記の要点vを参照のこと)についての定量された平均放射能(上記の要点ixを参照のこと)であり、そしてSRはSRコントロール(上記の要点viを参照のこと)についての定量された平均放射能(上記の要点ixを参照のこと)である;
4)「ADCCの増加」は、上記の試験された抗体濃度範囲内で観察される特異的溶解の最大パーセンテージの増加、および/または上記の試験された抗体濃度範囲内で観察される特異的溶解の最大パーセンテージの半分を達成するために必要とされる抗体の濃度の減少のいずれかとして定義される。ADCCの増加は、上記のアッセイを用いて測定される、当業者に公知である同じ標準的な産生、精製、製剤、および保存の方法を使用して、同じ型の宿主細胞によって産生される、同じ型の抗体によって媒介されるADCCに比例するが、これは、GnTIIIを過剰発現するように操作された宿主細胞によって産生されなかった。
本発明は、グリコシル化パターンの修飾を有する本発明のABMの生成のための宿主発現系を提供する。特に、本発明は、改善された治療的価値を有する本発明のABMの糖型の生成のための宿主細胞系を提供する。それゆえに、本発明は、GnTIII活性を有するポリペプチドを発現するように選択または操作された宿主細胞発現系を提供する。1つの実施形態において、GnTIII活性を有するポリペプチドは、異種ゴルジ存在性ポリペプチドのゴルジ局在化ドメインを含む融合ポリペプチドである。詳細には、このような宿主細胞発現系は、構成的または調節されるプロモーター系に作動可能に連結された、GnTIIIを有するポリペプチドをコードする組換え核酸分子を含むように操作され得る。
マウスB−Ly1抗体の実質的に同じ結合特異性を有し、かつ生物学的に活性な遺伝子産物を発現するキメラABMのコード配列を含む宿主細胞は、少なくとも4つの一般的アプローチ:(a)DNA−DNAまたはDNA−RNAのハイブリダイゼーション;(b)「マーカー」遺伝子機能の存在または非存在;(c)宿主細胞中のそれぞれのmRNA転写物の発現によって測定されるような転写物のレベルを評価すること;および(d)免疫アッセイによって、またはその生物学的活性によって測定されるような遺伝子産物の検出によって同定されてもよい。
好ましい実施形態において、本発明は、マウスB−Ly1抗体の実質的に同じ結合特異性を有し、かつ抗体依存性細胞傷害性を含むエフェクター機能の増加を有するキメラABMの糖型を提供する。抗体のグリコシル化操作は以前に記載されている。例えば、米国特許第6,602,684号(その全体が参照により本明細書に組み込まれる)を参照のこと。
本発明のABMは、インビボで腫瘍細胞を標的化および殺傷するために単独で使用され得る。このABMはまた、ヒト癌腫を治療するために、適切な治療剤とともに使用され得る。例えば、このABMは、化学療法、放射線療法などの標準的または従来的な治療方法と組み合わせて使用され得るか、または癌腫の部位への治療剤の送達のために、治療薬物または毒素、ならびにリンホカインまたは腫瘍阻害性増殖因子に、結合体化または連結され得る。最も重要である本発明のABMの結合体は(1)免疫毒素(ABMおよび細胞傷害性部分の結合体)および(2)標識が標識されたABMを含む免疫複合体を同定するための手段を提供する、標識された(例えば、放射標識、酵素標識、または蛍光標識)ABMである。ABMはまた、天然の補体プロセスを通して溶解を誘導するため、および通常存在する抗体依存性細胞傷害性細胞と相互作用するために使用され得る。
材料および方法
組換え抗体B−Ly1のクローニングおよび発現
B−Ly1発現ハイブリドーマ細胞を、10% FBSおよび4mM L−グルタミンを含むRPMI中で増殖させた。>90%生存度を有する6×106細胞を収集し、全RNAを、Qiagen RNA easy midiキットを使用して単離した。B−Ly1の可変軽鎖および重鎖をコードするcDNAをRT−PCRによって増幅した。RT−PCR反応は、以下の条件:第1鎖cDNA合成のための30分間50℃;15分間95℃の初期変性;30サイクルの1分間94℃、1分間45℃、1.5分間72℃;および10分間72℃の最終伸長工程を使用して実行した。PCR産物の予想サイズは、ゲル電気泳動によって確認した。このPCR産物を適切な大腸菌ベクターにクローニングし、そしてDNA配列決定は、可変軽鎖および重鎖をコードする遺伝子が単離されたことを確認した。
オリゴサッカリドを、PNGアーゼF消化によって抗体から酵素的に遊離させた。抗体はPVDF膜に固定化したか、または溶液中にあるかのいずれかであった。
PVDF(Immobilon P,Millipore,Bedford,Massachusetts)膜で作られた96ウェルプレートのウェルを、100μlメタノールで湿潤させ、そして液体を、Multiscreen vacuum manifold(Millipore,Bedford,Massachusetts)に適用された真空を使用してPVDF膜を通して吸引した。このPVDF膜を、300μlの水で3回洗浄した。次いで、ウェルを、50μl RCM緩衝液(8M 尿素、360mM Tris、3.2mM EDTA、pH 8.6)で洗浄した。30〜40μgの間の抗体を、10μl RCM緩衝液を含むウェル中に負荷した。ウェル中の液体を、適用した真空によって膜を通して吸引し、この膜を、引き続いて50μl RCM緩衝液で2回洗浄した。ジスルフィド架橋の還元を、50μlのRCM中0.1M ジチオスレイトールの付加、および37℃で1時間のインキュベーションによって実行した。
40〜50μgの間の抗体を、2mM Tris、pH7.0中2.5mUのPNGアーゼF(Glyko,U.S.A.)と、25マイクロリットルの最終容量中で混合し、そして混合物を3時間37℃でインキュベートした。
PNGアーゼF遊離オリゴサッカリドを、エンドグリコシダーゼH(EC 3.2.1.96)で引き続き消化した。EndoH消化のために、15mUのEndoH(Roche,Switzerland)をPNGアーゼF消化物(上記の溶液方法における抗体)に加え、30マイクロリットルの最終容量を得、この混合物を3時間37℃でインキュベートした。EndoHは、N連結オリゴサッカリドのキトビオースコアのN−アセチルグルコサミン残基の間を切断する。この酵素は、オリゴマンノースおよび大部分のハイブリッド型グリカンを消化できるのみであるのに対して、複合体型オリゴサッカリドは加水分解されない。
遊離したオリゴサッカリドを含む酵素消化物を、150mMの最終濃度までの酢酸の付加後に、さらに3時間室温でインキュベートし、引き続き、カチオンおよびタンパク質を取り除くために、マイクロバイオスピン(micro−bio−spin)クロマトグラフィーカラム(BioRad,Switzerland)に充填された0.6mlのカチオン交換レジン(AG50W−X8レジン、水素型、100〜200メッシュ、BioRad,Switzerland)に通した。1mlの得られるサンプルを、ステンレス鋼標的プレートに適用し、プレート上で1μlのsDHBマトリックスと混合した。sDHBマトリックスを、1mlのエタノール/10mM 塩化ナトリウム水溶液1:1(v/v)中に2mgの2,5−ジヒドロキシ安息香酸および0.1mgの5−メトキシサリチル酸を溶解することによって調製した。サンプルを風乾し、0.2μlエタノールを適用し、そしてサンプルを最終的に空気中で再結晶させた。
質量スペクトルを得るために使用したMALDI/TOF−MS質量スペクトル分析装置はVoyager Elite(Perspective Biosystems)であった。この機器を、20kVの加速および80nsのディレイを用いて直線状配置で操作した。オリゴサッカリド標準を使用する外部較正を、イオンの質量割り当てのために使用した。200個のレーザーショットからのスペクトルを、最終的なスペクトルを得るために加算した。
健常ドナーからの495μlのヘパリン化血液を、5mlポリスチレンチューブ中でアリコートし、5μlの100倍濃縮抗体サンプル(1〜1000ng/ml最終濃度)またはPBSのみを加え、そしてチューブを37℃でインキュベートした。24時間後、50μlの血液を新鮮なチューブに移し、抗CD3−FITC、抗CD19−PEおよび抗CD45−CyChrome(Becton−Dickinson)で、15分間、室温にて、暗所で染色した。分析の前に、500μlのFACS緩衝液(2% FCSおよび5mM EDTAを含むPBS)をチューブに加えた。血液サンプルのCD3−FITCおよびCD19−PE蛍光を、閾値をCD45−CyChromeに設定することによって、フローサイトメトリーによって分析した。B細胞枯渇を、CD3+T細胞に対するCD19+B細胞の比率をプロットすることによって決定した。
180μlのFACS緩衝液(2% FCSおよび5mM EDTAを含むPBS)中の500.000を5mlのポリスチレンチューブに移し、20μlの10倍濃縮抗CD20抗体サンプル(1〜5000ng/ml最終濃度)またはPBSのみを加え、チューブを4℃で30分間インキュベートした。続いて、FACS緩衝液で2回洗浄し、300×gで3分間ペレット化した。上清を吸引して除き、細胞を100μlのFACS緩衝液中に取り、1μlの抗Fc特異的F(ab’)2−FITCフラグメント(Jackson Immuno Research Laboratories,USA)を加え、そしてチューブを4℃で30分間インキュベートした。サンプルをFACS緩衝液で2回洗浄し、フローサイトメトリーによる分析のために、0.5μg/ml PIを含む500μlのFACS緩衝液に取り込んだ。結合を、抗体濃度に対して幾何平均蛍光をプロットすることによって決定した。
高相同性アクセプターアプローチ
高相同性抗体アクセプターフレームワーク検索を、ヒト生殖系列配列のコレクションに対してB−ly1タンパク質配列をアラインさせること、および最大の配列同一性を示したヒト配列を取り出すことによって実行した。ここで、VBaseデータベースからの配列VH1 10を重鎖フレームワークアクセプター配列として選択し、そしてVK 2 40配列を、軽鎖についてのフレームワークアクセプターであると選択した。これらの2つのアクセプターフレームワークに、マウス重鎖および軽鎖の可変ドメインの3つの相補性決定領域(CDR)を移植した。フレームワーク4領域は生殖系列V遺伝子の可変領域の一部ではないので、この位置のアラインメントは個別に行った。JH4領域を重鎖について選択し、JK4領域を軽鎖について選択した。設計された免疫グロブリンドメインの分子モデリングは、1つのスポットが、CDRの外側のヒトアミノ酸残基の代わりにマウスアミノ酸残基を潜在的に必要とすることを明らかにした。ヒトフレームワークにマウスアミノ酸残基を再導入することは、いわゆる復帰突然変異を生成する。例えば、Kabat27位のヒトアクセプターアミノ酸残基はチロシン残基に復帰突然変異した。復帰突然変異を含むかまたはそれを除外したかのいずれかである、ヒト化抗体改変体を設計した。ヒト化抗体軽鎖はいかなる復帰突然変異も必要としなかった。タンパク質配列を設計した後で、これらのタンパク質をコードするDNA配列を、以下に詳述するように合成した。
ヒトアクセプターフレームワークの決定的である(良好な抗原結合親和性または抗体機能を保持するために決定的である)アミノ酸残基位置で復帰突然変異を導入することを回避するために、全体のフレームワーク領域1(FR1)またはフレームワーク領域1(FR1)および2(FR2)が一緒でのいずれかが、天然のヒト生殖系列配列中のこれらの重要な位置において、ドナー残基または機能的に等価な残基をすでに有するヒト抗体配列によって置き換えられ得るか否かを調べた。この目的のために、マウスBly1配列のVHフレームワーク1および2を、ヒト生殖系列配列に対して個々にアラインした。ここで、最大の配列同一性は重要ではなく、アクセプターフレームワークを選択するために使用しなかったが、その代わりに、いくつかの重要な残基の一致をより重要であると仮定した。これらの決定的な残基には、残基24、71、および94(Kabat番号付け)が含まれ、およびまた、27位、28位、および30位(Kabat番号付け)の残基も含まれ、これは、KabatによるCDR1の定義の外側に存在するが、しばしば、抗原結合に関与している。IMGT配列VH 3 15を適切なものとして選択した。タンパク質配列を設計した後、これらのタンパク質をコードするDNA配列を、以下に詳述するように合成した。このアプローチを使用すると、良好なレベルの抗原結合を保持するために、軽鎖または重鎖のいずれかについても、復帰卒然変異は必要とされなかった。
ヒト化抗体V領域のアミノ酸配列を設計した後、DNA配列が生成されなくてはならなかった。個々のフレームワーク領域のDNA配列データは、ヒト生殖系列配列についてのデータベース中で見い出した。CDR領域のDNA配列は、対応するマウスcDNAデータから取った。これらの配列を用いて、全体のDNA配列を仮想的にアセンブルした。このDNA配列データを有するので、サイレント変異を導入することによって仮想配列に診断用制限部位を導入し、制限エンドヌクレアーゼのための認識部位を作製した。物質のDNA鎖を得るために、遺伝子合成を実行した(例えば、Wheelerら、1995)。この方法において、オリゴヌクレオチドは目的の遺伝子から設計され、一連のオリゴヌクレオチドがコード鎖に由来し、1つの他の一連のものは非コード鎖由来である。各オリゴヌクレオチドの3’末端および5’末端(行におけるまさに最初および最後を除く)は、反対の鎖に由来する2つのプライマーに対する相補的配列を常に示す。これらのオリゴヌクレオチドを、任意の熱安定ポリメラーゼのために適切な反応緩衝液中に配置し、およびMg2+、dNTP、およびDNAポリメラーゼを加えるときに、各オリゴヌクレオチドはその3’末端から伸長される。次いで、一方のプライマーの新規に形成された3’末端が反対の鎖の次のプライマーとアニールし、そして鋳型依存的なDNA鎖伸長のために適切な条件下でその配列をさらに伸長する。最終産物を大腸菌中での増殖のために従来的なベクターにクローニングした。
ヒト重鎖および軽鎖リーダー配列(分泌のため)を上記の可変領域配列の上流に加え、次いでこれらを、標準的な分子生物学技術を使用して、それぞれ、ヒトIgG1κ定常重鎖および軽鎖配列の上流に結合した。得られる完全な抗体重鎖および軽鎖DNA配列を、MPSVプロモーターの制御下で、かつ合成ポリA部位の上流で、哺乳動物発現ベクター(1つが軽鎖用、および1つが重鎖用)にサブクローニングした。各ベクターは、上記の実施例1に記載されるように、EBV OriP配列を有していた。上記の実施例1に記載されるように、すなわち、HEK293−EBNAを哺乳動物抗体重鎖および軽鎖発現ベクターとトランスフェクトすること、トランスフェクションの5〜7日後、順化培養培地を収集すること、ならびに純粋なモノマー性IgG1抗体を単離するためにプロテインAアフィニティークロマトグラフィー、続いてカチオン交換クロマトグラフィーおよび最終的なサイズ排除クロマトグラフィーの工程によって分泌抗体を精製することによって、抗体を産生した。抗体を25mM リン酸カリウム、125mM 塩化ナトリウム、100mM グリシン溶液、pH 6.7中で製剤化した。上記の実施例1においてキメラ抗体について記載されているように、GnT−IIIグリコシルトランスフェラーゼ発現ベクターとともに、またはGnT−III発現ベクターおよびゴルジマンノシダーゼII発現ベクターとともに、抗体発現ベクターの同時トランスフェクションによって、ヒト化抗体改変体の糖付加操作改変体を産生した。糖付加操作抗体を、非糖付加操作抗体について上記に記載されたように精製および製剤化した。抗体のFc領域に結合されたオリゴサッカリドを、以下に記載されるようにMALDI/TOF−MSによって分析した。
溶液中の抗体に対するオリゴサッカリド遊離方法
40〜50μgの間の抗体を、2mM Tris、pH7.0中の2.5mU PNGアーゼF(Glyko,U.S.A.)と、25マイクロリットルの最終容量で混合し、そしてこの混合物を3時間37℃でインキュベートした。
遊離したオリゴサッカリドを含む酵素消化物を、150mMの最終濃度までの酢酸の付加後に、さらに3時間室温でインキュベートし、引き続き、カチオンおよびタンパク質を取り除くために、マイクロバイオスピン(micro−bio−spin)クロマトグラフィーカラム(BioRad,Switzerland)に充填された0.6mlのカチオン交換レジン(AG50W−X8レジン、水素型、100〜200メッシュ、BioRad,Switzerland)に通した。1mlの得られるサンプルを、ステンレス鋼標的プレートに適用し、プレート上で1μlのsDHBマトリックスと混合した。sDHBマトリックスを、1mlのエタノール/10mM 塩化ナトリウム水溶液1:1(v/v)中に2mgの2,5−ジヒドロキシ安息香酸および0.1mgの5−メトキシサリチル酸を溶解することによって調製した。サンプルを風乾し、0.2μlエタノールを適用し、そしてサンプルを最終的に空気中で再結晶させた。
質量スペクトルを得るために使用したMALDI/TOF−MS質量スペクトル分析装置はVoyager Elite(Perspective Biosystems)であった。この機器を、20kVの加速および80nsのディレイを用いて直線状配置で操作した。オリゴサッカリド標準を使用する外部較正を、イオンの質量割り当てのために使用した。200個のレーザーショットからのスペクトルを、最終的なスペクトルを得るために加算した。
上記の実施例1においてキメラB−ly1抗体について記載されるようなフローサイトメトリーベースのアッセイを使用して、精製したモノマー性ヒト化抗体改変体を、Raji B細胞リンパ腫標的細胞上でのヒトCD20への結合について試験した。
CD16−およびCD56陽性細胞(MACS system,Miltenyi Biotec GmbH,Bergisch Gladbach/Germany)についてネガティブ選択富化を適用して、ヒトNK細胞を、新鮮に単離された末梢血単核細胞(PBMC)から単離した。CD56発現によって決定された純度は、88〜95%の間であった。新鮮に単離されたNK細胞を、カルシウムイオンおよびマグネシウムイオンを含まないPBS中で(3×10 5 細胞/ml)、20分間37℃にてインキュベートして、NK細胞結合IgGを除去した。細胞を、10 6 細胞/mlにて、PBS、0.1% BSA中の異なる濃度の抗CD20抗体(0、0.1、0.3、1、3、10μg/ml)でインキュベートした。数回の洗浄後、抗体結合を、1:200 FITC結合体化F(ab’)ヤギ抗ヒト、F(ab’)2特異的IgG(Jackson ImmunoResearch,West Grove,PA/USA)および抗ヒトCD56−PE(BD Biosciences,Allschwil/Switzerland)とともにインキュベートすることによって検出した。抗FcγRIIIA 3G8F(ab’)2フラグメント(Ancell,Bayport,MN/USA)を、抗体糖改変体(3μg/ml)の結合と競合させるために10μg/mlの濃度で加えた。結合抗体改変体を参照する蛍光強度を、CD56陽性細胞について、FACSCalibur(BD Biosciences,Allschwil/Switzerland)上で決定した。CHO細胞を、FcγRIIIa−Val158α−鎖およびγ−鎖をコードする発現ベクターを用いるエレクトロポレーション(280V、950μf、0.4cm)によってトランスフェクトした。トランスフェクト体を、6μg/mlピューロマイシンの添加によって選択し、安定なクローンを、FACSによって、106細胞について10μl FITC結合体化抗FcγRIII 3G8モノクローナル抗体(BD Biosciences,Allschwil/Switzerland)を使用して分析した。FCγRIIIA−Val158−発現CHO細胞へのIgG1の結合を、上記に記載されるNK細胞結合と類似して実行した。
ヒト末梢血単核細胞(PBMC)をエフェクター細胞として使用し、ならびにHistopaque−1077(Sigma Diagnostics Inc.,St.Louis,MO63178 USA)を使用して、および本質的に製造業者の指示書に従って調製した。手短に述べると、静脈血をボランティアからヘパリン化シリンジを用いて採取した。血液をPBS(Ca++またはMg++を含まない)で1:0.75〜1.3に希釈し、Histopaque−1077に重層した。グラジエントを、壊すことなく400×gで30分間室温(RT)で遠心分離した。PBMCを含む界面を収集し、PBSで洗浄し(2つのグラジエントからの細胞あたり50ml)、そして室温にて10分間の300×gの遠心分離によって収集した。PBSを用いるペレットの再懸濁後、PBMCを計数し、RTで10分間、200×gで遠心分離によって2回目の洗浄を行った。次いで、細胞を、引き続く手順のために適切な培地中に再懸濁した。
標的細胞を計数し、PBSで洗浄し、AIM−V(Invitrogen)中に100万細胞/mlで再懸濁した。50μl細胞を、平底96ウェルプレート中のウェルあたりにプレートした。抗体希釈物をAIM−V中で調製し、50μlで細胞に加えた。抗体を、10分間室温で細胞に結合させた。ヒト血清補体(Quidel)を新鮮に融解し、AIM−Vで3倍希釈し、そして50μlでウェルに加えた。ウサギ補体(Cedarlane Laboratories)を、製造業者によって記載されるように調製し、AIM−Vで3倍希釈し、そして50μlでウェルに加えた。コントロールとして、補体供給源を30分間56℃に加熱し、その後アッセイへの添加を行った。
アッセイプレートを2時間37℃でインキュベートした。細胞の殺傷を、LDH放出を測定することによって決定した。手短に述べると、プレートを、300×gで3分間遠心分離した。ウェルあたり50μlの上清を新たな96ウェルプレートに移し、そして細胞傷害性キット(Roche)からの50μlのアッセイ試薬を加えた。ELISAリーダーを用いる反応速度論的測定は、上清中のLDH濃度に対応するVmaxを決定した。最大放出を、1% Triton X−100の存在下で細胞をインキュベートすることによって決定した。
抗CD20抗体による全血中での正常B細胞枯渇を、上記の実施例1に記載されるように実行した。
抗体のアポトーシス効力を、10μg/ml(抗原結合に関して飽和状態)である抗体を標的細胞(5×10 5 細胞/mlの標的細胞濃度)とともに一晩(16〜24時間)インキュベートすることによってアッセイした。サンプルをAnnV−FITCで染色し、FACSによって分析した。アッセイを3連で行った。
キメラB−ly1軽鎖(上記の実施例1に記載されるようなmVL)で、またはヒト化B−ly1軽鎖(KV1)でのいずれかで複合体化された、抗体改変体B−HH1、B−HH2、B−HH3、および親のキメラ抗体chB−ly1(上記の実施例1に記載されている)のヒトCD20抗原への結合の比較は、全ての抗体が同様のEC50値を有するが、B−HH1構築物は改変体B−HH2およびB−HH3よりも低い強度/化学量論結合することを示す(図11)。B−HH1は、その部分的なヒトCDR1およびCDR2領域(Kabat定義)、ならびに28位(Kabat番号付け)におけるAla/Thr多型によって、B−HH2およびB−HH3から区別され得る。これは、28位、完全CDR1、および/または完全CDR2のいずれかが、抗体/抗原相互作用のために重要であることを示す。
Claims (15)
- (a)配列番号40の重鎖可変領域;及び
(b)配列番号76のKV1軽鎖可変領域
を含む、ヒト化II型抗−CD20抗体であって、
糖鎖工学的処理されたFc領域を含む、
抗体。 - 前記糖鎖工学的処理されたFc領域に付着した非フコシル化オリゴサッカリドの分画において増加している、請求項1に記載の抗体。
- 前記糖鎖工学的処理されたFc領域に付着した二分枝、非フコシル化オリゴサッカリドの分画において増加している、請求項1に記載の抗体。
- 糖鎖工学的処理されていない抗体に比較して、ヒトFcガンマRIII受容体への有意に高い結合レベルをもつ、請求項1に記載の抗体。
- 糖鎖工学的処理されていない抗体に比較して、有意に高い結合レベルのADCC活性をもつ、請求項1に記載の抗体。
- 配列番号40の重鎖可変領域をコードするポリヌクレオチド、及び
配列番号76の軽鎖可変領域をコードするポリヌクレオチド
を含む、発現ベクター。 - 請求項6に記載の発現ベクターを含む宿主細胞。
- B細胞枯渇により治療可能な障害を治療するための医薬の製造のための、請求項1〜5のいずれか1項に記載の抗体の使用。
- 前記障害が、血液学的悪性腫瘍又は自己免疫疾患である、請求項8に記載の抗体の使用。
- 前記血液学的悪性腫瘍が、B細胞リンパ腫、非ホジキンリンパ種、又はB細胞慢性リンパ球白血病である、請求項9に記載の抗体の使用。
- 前記自己免疫疾患が、リウマチ様関節炎又はろうそうである、請求項9に記載の抗体の使用。
- 請求項1〜5のいずれか1項に記載の抗体、及び医薬として許容される担体を含む医薬組成物。
- B細胞障害を治療するための医薬として使用するための、請求項1〜5のいずれか1項に記載の抗体。
- 前記障害が、B細胞リンパ腫である、請求項13に記載の抗体。
- 抗−CD20抗体の製造方法であって、以下のステップ:
a.前記抗体の生産を許容する条件下で請求項7に記載の宿主細胞を培養し、そして
b.該抗体を単離すること、
を含む前記方法。
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