JPH01502875A - 変性抗体のまたは変性抗体に関する改良 - Google Patents

変性抗体のまたは変性抗体に関する改良

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JPH01502875A
JPH01502875A JP63502461A JP50246188A JPH01502875A JP H01502875 A JPH01502875 A JP H01502875A JP 63502461 A JP63502461 A JP 63502461A JP 50246188 A JP50246188 A JP 50246188A JP H01502875 A JPH01502875 A JP H01502875A
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ウィンター，グレゴリー・ポール
ダンカン，アレクサンダー・ロバート
バートン，デニス・レイモンド
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エス・ビィ・２・インコーポレイテッド
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Abstract

(57)【要約】本公報は電子出願前の出願データであるため要約のデータは記録されません。

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【発明の詳細な説明】 変性抗体の、または変性抗体に関する改良発明の分野 本発明は変性抗体に関し、変性したエフェクター機能を有する抗体、該抗体を産 出する方法、および抗体のエフェクター機能を変性する方法に関連する。
発明の背景 抗体、即ち免疫グロブリンは、ジスルフィド結合により連結された二つのＨ（ｈ ｅａｖｙ）鎖と、二つのＬ　（ｌｉｇｈｔ）鎖からなり、各り鎖は各々のＨ鎖に ジスルフィド結合により結合している。ＩｇＧクラス（すなわち、ガンマ（Ｇ） クラスの免疫グロブリン（Ｉｇ））の抗体の一般構造を添付の第１図に模式的に 示す。
各Ｈ鎖は一端に一つの可変領域を有し、これに幾つかの定常領域が連なる。各り 鎖は一端に一つの可変領域を、他端に一つの定常領域を有し、Ｌ鎖の可変領域は Ｈ鎖の可変領域と連結し、Ｌ鎖の定常領域はＨ鎖の最初の定常領域と連結する。
抗原は、各対のＬ鎖およびＨ鎖の可変領域にある抗原結合部位を介して抗体に結 合する。エフェクター分子として知られる他の分子は、この分子の残りの部分、 即ち抗原結合部位以外の部位で他の部位に結合する。本明細書では抗体のこの部 分を抗体の「定常部」と呼ぶ。該部位は特にＬ鎖の端を越えて伸びるＨ鎖の部分 により構成されたＦｃ領域に位置する。
抗体は、エフェクター分子の結合を媒介として数個のエフェクター機能を有する 。例えば、補体のＣＩ酸成分抗体に対する結合は補体システムを活性化する。補 体の活性化はオプソニン作用および細胞病原体の溶解において重要である。また 、補体の活性化は炎症反応を刺激し、自己免疫の過度の感作を引き起こしうる。
さらに、抗体は、抗体Ｆｃ領域上のＰｃレセプター部位を細胞上のＦｃレセプタ ー（ＦｃＲ）に結合してＰｃ領域を介して細胞に結合する。ＩｇＧ（ガンマレセ プター）、ＩｇＥ（イータレセプター）、ＩｇＡ（アルファレセプター）および ＩｇＭ（ミューレセプター）を含む別々のクラスの抗体に対して特有の幾つかの Ｆｃレセプターが存在する。細胞表面上のＰｃレセプターに対する抗体の結合は 、抗体被覆粒子の食作用（ｅｎｇｕｌｆｍｅｎｔ）および破壊、免疫錯体の浄化 、キラー細胞による抗体被覆した標的細胞の溶解（抗体依存性細胞障害（ＡＤＣ Ｃ）と称される）、炎症メディエータの放出、胎盤トランスファーおよび免疫グ ロブリン産生の制御を含む幾つかの重要で多様な生物学的反応を引き起こす。
様々なＰｃレセプターおよびレセプター部位についである程度研究されてきたが 、それらの位置、構造および機能について未だ多くの未知のことがらがある。
及豆Δ双４ 本発明の一つの観点によれば、ＩｇＧクラスの変成抗体が提供され、ここで少な くとも一つの定常部のアミノ酸残基（本明細書にて定義）は異なる残基により置 換され、抗体のエフェクター機能を未変成の抗体に比較して変性するる。
抗体のエフェクター機能は変性、すなわち、Ｆｃレセプターまたは補体成分のよ うなエフェクター分子に対する抗体の親和性の強化または減少により変性しても よい。結合親和性は一般的にエフェクター分子の結合部位を変成することにより 変わり、この場合では、問題の部位の位置を確認し適当な方法で該部位の少なく とも一部を変成するのが好ましい。また、エフェクター分子に対する抗体上の結 合部位における変性は、全体的な結合親和性の変性を実質的に必要としないが、 幾何学的な相互作用を変え、エフェクターの機序を非生産的結合によって無効な ものとすることがあることも考えられる。
さらに、またエフェクター機能は、エフェクター分子結合にに直接に関連せず、 エフェクター機能の実行に関連する部位を変成することにより変えてもよいと考 えられる。
抗体のエフェクター機能を変えることにより、免疫反応の様々な面を制御するこ と、例えば、免疫系の様々な反応を強化または抑制することが可能となり、診断 および治療ｊこおいて有益な効果が得られる。
例えば、卵巣および畢丸のガンなどのような幾つかの充実性腫瘍を有する患者の 悪性障害の誘導性局在（ｇｕｉｄｅｄｌｏｃａｌｉｓａｔｉｏｎ）をはかるため にモノクローナル抗体を用いることが知られている。しかしながら、これらの一 般の用途は、偽陽性、偽陰性並びに非特異的局在のようないくつかの大きな問題 が広がっているため、限定されている。人体への静脈内投与後、その目標となる 組織に到達する放射性ヨウ素標識した腫瘍結合（ｔｕｍｏｕｒ　ａｓｓｏｃｉａ ｔｅｄ）モノクローナル抗体は、少量である（Ｅｐｅｎｅｔｏｓら、１９８６年 ）。これらの研究におかる１つの問題として、正常なリンパ節における高い非特 異的吸収、およびネズミモノクローナル抗体の速やかな異化がある。
また、ヒトモノクローナル抗体の使用は、リンパ管、肝臓および膵臓の高親和性 レセプター（ＦｃガンマＲ１）に対する非特異的結合のため高い背景レベル（バ ックグラウンド）を示すことがある。この高親和性レセプターに結合しない変性 モノクローナル抗体は、抗体の特異的な腫瘍への取り込みを増大し、一方ＦｃＲ への非特異的結合により背景レベルを低下させることにより抗体誘導（ｇｕｉｄ ｅｄ）Ｉｌ！瘍の局在化を改善する。　腫瘍の治療に用いられるモノクローナル 抗体は、理想的には放射性の標識がなされるか、ホスト自身のエフェクターの機 序の利用が行われる。単核細胞、特にに細胞によるＡＤＣＣは最も効果的と思わ れる（Ｂａｌら、１９８５年）が、抗体被覆した標的細胞にとって生体内でこれ らのいずれが晟も重要であるかは未だ明らかでない。ある形式のＦｃレセプター のみに反応する抗体を産生ずることは可能である。例えば、ＲｌＥ、ＳＬ：Ｉ） 細胞の高親和性ＦｃガンマＲ１を結合しない変成抗体は産生され得るが、表面に 凝集したときＦｃガンマＲ１＋表現細胞を結合し、ＡＤＣＣおよび標的細胞の特 異的破壊を引き起こす。
変成抗体の産生は、当業者に周知の技術を含むいかなる適当な技術によって行な ってもよい。例えば、ＣＨ２領域などの抗体の関連した定常領域の形成部または 全部など、抗体の適当なタンパク質配列は、適当な変性残基を含んで合成するこ とができ、ついで抗体分子の適当な場所に化学的に結合することができる。
しかしながら、遺伝子工学の技術を変性抗体の産生に用いるのが好ましい。現在 好ましいかかるこのような技術はつぎのちのからなる。
ａ）適当な残基が変性されたＩｇＧＨ鎖のＩｇＧのＶＨ％ＣＨＩ、Ｃａ２領域な ど、ＩｇＧＨ鎖またはＬ鎖の少なくとも一部をコード化するＤＮＡ配列にに操作 可能に結合した適当なプロモーターを含む第一の複製可能な表現ベクター（ｅｘ ｐｒｅｓｓｉｎ　ｖｅｃｔｏｒ）を産生ずること。
ｂ）必要により、相補的１ｇＬ＠またはＨ鎖をコード化するＤＮＡ配列に・操作 可能に結合する適当なプロモーターを含む第二の複製可能な表現ベクターを産生 ずること。
Ｃ）第一のまたは両方の産生ベクターを有する細胞系を形質転換すること、およ び ｄ）前記形質転換した細胞系を培養し変性抗体を産生ずること。
また、本発明は細胞系の形質転換に用いられるベクター、形質転換ベクターの産 生に用いられるベクター、形質転換ベクターを用いて形質転換された細胞系、プ レパラティブ（ｐｒｅｐａｒａｔｉｖｅ）ベクターを用いて形質転換された細胞 系、およびそれらを産生ずる方法を包含する。
好ましくは形質転換され変性されたエフェクター機能の抗体を産生ずる細胞系は 、不死化した哺乳動物の細胞系であり、これはミエローマ、ハイブリドーマ、ト リオーマまたはクアドローマ細胞系のごときリンパ系器官という利点を有する。
また、該細胞系はエプスタイン・バールウィルスのごときウィルスを用いた形質 転換により不死化されたＢ細胞などの正常なリンパ細胞からなってもよい。最も 好ましくは該不死化細胞系はミエローマ細胞系またはその誘導体である。
変性したエフェクター機能の抗体を産生ずるのに用いられる細胞系は哺乳動物の 細胞系であるのが好ましいが、細菌細胞系または酵母細胞系のごとき他のいかな る適当な細胞系をかわりに用いてもよい。特に、Ｅ、ｃｏｌｉ誘導細菌株を用い ることも考えられる。
正常状態にあるある種のミエローマ細胞系のごとき不死化したリンパ細胞系は、 分離したＩｇＬ鎖を分泌することが知られている。細胞系が前記方法のステップ ａ）にて産生されたベクターを用いて形質転換される場合、正常に分泌された鎖 はステップａ）にて産生されたベクターによりコード化された鎖に対し相補的で あるならば該方法のステップｂ）を行う必要はない。
しかしながら、不死化した細胞系が分泌しないかあるいは相補的な鎖を分泌しな い場合、ステップｂ）を実行する必要がある。このステップはステップａ）にお いて産生されたベクターをさらに操作することにより行なってもよく、その結果 このベクターはＨ鎖だけでなくＬ鎖もをコード化する。別法としては、不死化し た細胞系を形質転換するのに用いられる第二ベクターを産生ずることによりステ ップｂ）を実行する。
かかるベクターを産生じ、不死化した細胞系の形質転換に用いられる技術は、当 業者に公知であり本発明を構成するものではない。
不死化した細胞系が相補的り鎖を分泌する場合において、形質転換された細胞系 は例えばベクターを用いて適当な細菌の細胞を形質転換し、ついで該細菌の細胞 を不死化した細胞系を用いてスフェロプラスト融合により融合して産生じてよい 。別法としてＤＮＡを直接不死化した細胞系にエレクトロポレイション（ｅｌｅ ｅｔｒｏｐｏｒｅｔｉｏｎ）により導入してもよい。
抗体の関連変性タンパク質をコード化するＤＮＡ配列は、オリゴヌクレオチド合 成により産生じてよい。別法として変性したタンパク質をコード化するＤＮＡを プライマ一定方向オリゴヌクレオチド部位一定方向突然変異誘発により産生じて もよい。この技術は本質的に変異点を含有するＤＮＡの一本鎖を用いて所望の変 異に対してコードするオリゴヌクレオチドのハイブリッドを形成すること、およ び変異を含む鎖を産生ずるオリゴヌクレオチドの延長のために鋳型として一本鎖 を用いることを含む。この技術は、様々な形で記載されている［　Ｚｏｌ　ｌｅ ｒおよびＳｍ１ｔｈ　（１９８２年）　、Ｚ　ｏｌ　ｉｅｒおよびＳ　ｗｉｔｈ （１９８４年）　、Ｎｏｒｒｉｓら（１９８３年）　、Ｋｒａｍｅｒら（１９８ ２年）］。
最も単純な形態のこの技術は、様々な理由から必ずしも高い頻度で変異を生じな い。Ｍ１３に基づくベクターにおける単一および複合変異の両方を誘導する改良 技術がＣａｒｔｅｒら（１９８５ａ）により報告されている。
本発明は、異なる種、例えばヒト、げっ歯頚（マウス、ラット、ハムスター）な ど、および他の綱（ｃｌａｓｓ）の抗体に適用することができる。本発明はまた 自然発生抗体、キメラ抗体（例えばＰ　ＣＴ　／　Ｇ　Ｂ　８５／　００３９２ にて開示の形式の）、まｆこは他の方法（Ｇ　Ｂ　２１８８６３８に開示の形式 の）にて変性した変性抗体に用いることができる。
一例として、ＩｇＧについてＦｃガンマＲＩとして公知のレセプターに対する結 合親和性を変える研究がなされている。
ヒトおよびマウスにおいて、３種のＰｃガンマレセプターは部分的にＰｃガンマ ＲＩＳＦｃガンマＲＩＩ、およびＦｃガンマＲ１゜と呼ばれ、これらは全く異な って表現されるが造血細胞型（ｈｏｅｍａｔｏｐｏｅｔｉｃ　ｃｅｌｌ　ｔｙｐ ｅ）を重複する（Ａ　ｎｄｅｒｓｏｎおよびＬｏｏｎｅｙ、１９８６年）。さら に、これら異なるレセプターはＩｇＧサブクラスに対して異なった親和性を有す る。
前記のごとく、細胞表面のこれらレセプターへの抗体の結合は数々の重要かつ多 様な生物学的反応を引き起こす。存在するどのレセプターがどの効果に対して主 に反応性を有するかは知られていないが、これら生理的な作用に対して関連する 低親和性レセプターであることが反応の形跡から推定される。
ヒトおよびマウス中のレセプターは数々の物理的基準に基づき同族体として提案 されている。両者由来の低親和性ＦＣガン？ＲＩＩのクローニングおよび配列決 定（ｓｅｑｕｅｎｃｉｎｇ）は、この仮説（Ｌｅｗｉｓら、１９８６年）を支持 する。高親和性レセプターＰｃガンマＲ１は広範囲にわたり、かつヒトとマウス の両方の結合単量体１ｇＧ（ヒト＝ＩｇＧ１および１ｇＧ３、マウス＝１ｇＧ２ λ）について研究されており、同一の細胞型にて発見される。
ＩｇＧ（ＤＦｃ領域は、第り図に示すように二つの定常領域、ＣＨ２およびＣＨ ３からなる。マウス系を用いて、相互作用に対する二つの領域、Ｃガンマ２およ びＣガンマ３の各々の寄与の決定に多くの努力が払われた。分触されたｃｍ３領 域（ｐＦｃフラグメント）は、単球ロゼツトの形成において阻害作用を示さない ことが報告されている（　Ａ　ｂｒａｍｓｏｎら、１９７０年）。しかし他の報 告では、このフラグメントはＦｃガンマＲ結合を阻害しうることが示されており （Ｂａｒｎｅｔｔ　−Ｆｏｓｔｅｒら、１９８０年）、Ｃガンマ３領域はヒトＰ ｃガンマＲ１の結合に含まれることが示される。この考えは、この阻害活性がプ ロティンＡと抗−り鎖のカラムを通すことによるｐＦｃ−の大量精製により除去 され得ることをＷｏｏｆらが示すまで支配的となった。これらの精製サンプルは 単量体結合の阻害を示さなかった（Ｗｏｏｆら、１９８４年）。さらに、モノク ローナル抗体の能力は、再度Ｃ）＋３領域上の抗原決定基に向けられ抗体と結合 したＦｃＲと相互作用を行うが、Ｃ１１３上の抗原決定基に向かっていないもの はＣ＋＋２領域上の結合部位と一致する（Ｐａｒｔｒｉｄｇｅら、１９８６年） 。
また、ヒト単球（ＦｃガンマＲ１）上のヒトＩｇＧに対する高親和性レセプター の広範な研究において、Ｗｏｏｆ％ＢｕｒｔｏｎらはヒトＩｇＧ１のＣＨ２領域 に対する結合部位の位置決定を行った（Ｗｏｏｆら、１９８４年ＨＰ　ａｒｔｒ ｉｄｇｅら、１９８６年）。異なる種から得られたＩｇＧサブクラスの範囲はヒ ト免疫グロブリンのフラグメントと共に、直接結合微生物学的、検定においてヒ トＩｇＧとヒト単球との間の相互作用を阻害するためにその能力がテストされた 。ＩｇＧはヒト単球上のＦｃＲ（ＰｃガンマＲ１）に対して強い、中間のあるい は弱い結合を示すものに分類された。このような異なる親和性グループのアミノ 酸配列の比較により、ヒンジ結合領域（Ｌｅｕ２３４−Ｓｅｔ２３９）の潜在的 な単球結合部位が、残基ｃｔｙ３１６−Ｌｙｓ３３８により形成された二つのベ ータ鎖および結合屈曲部（ｊｏｉｎｉｎｇ　ｂｅｎｄ）の可能な複合体として提 案された（　Ｗｏｏｆら、１９８６）。後者の領域は既にＣ１ｑ結合部位として 提案されている（Ｂｕｒｔｏｎら、１９８０年）。ヒトＦｃガンマＲ１レセプタ ーは、ヒトＩｇＧ１とマウスＩｇＧ２ａとを単量体として結合するが、マウスＩ ｇＧ２ｂの結合は１００倍の弱さである（Ｉｏｏｆら、１９８６年）。ヒンジ結 合領域のこれらタンパク質の配列の比較は、強い結合中の配列（２３４から２３ ８）Ｌｅｕ−Ｌｅｕ−Ｇｌｙ−Ｇｌｙ−Ｐｒｏがマウスガンマ２ｂ中のＬｅｕ− Ｇｌｕ−Ｇｌｙ−Ｇｌｙ−Ｐｒｏになることを示す。
結合親和性を変性する試みにおいて、Ｇ１ｕ２３５のＬｅＵによる置換がマウス ＩｇＧ２ｂ０Ｈｔａ中にて行われた。Ｈ鎖中の残基の番号は、ＥＵインデックス の番号である（Ｋａｂａｔら、１９８３年参照）。正常マウス抗体はヒトＦｃガ ンマＲ１に結合しないが、残基２３５をグルタミン酸からロイシンに例えば部位 定方向変異誘発にて変えることにより、ヒトＰｃガンマＲ１に対する親和性は１ ００倍以上増大する。親和性の増加の大きさは予想以上に大きく、この領域にお ける単一のアミノ酸の変更が、ヒトおよび他の動物の生体内における適用領域に 対してより適合した変性抗体の産生に用いられ得ることを示唆する。この変更は 補体成分Ｃ１ｑなどの他のＩｇ結合部位を変性しない。
また、特定の残基をその側鎖上の不適当な機能を有する残基で置換することによ り、あるいはＧｌｕまたはＡｓｐなどの異なる官能基、あるいはＰｈｅＳＴｙｒ またはＴｒｐなどの芳香族非極性残基などを導入することによりＦｃガンマＲ１ 結合の親和性を変えることも可能である。
これらの変更は、異なる免疫グロブリンの間の配列の相同性が得られたマウス、 ヒトおよびラット系に対し等しく適用されると予想される。ヒトＦｃガンマＲ１ レセプターを結合するヒトＩ　ｇＧ３において、Ｌｅｕ２３５をＧｌｕに変性す ることは、レセプターに対する変異体の相互作用を破壊する。
このようにこのレセプターの結合部位はスイッチオン、スイッチオフが行われる 。
ヒンジ連結領域（例えばＡｌｔによる置換残基２３４．２３６または２３７）の 隣接または密着部位における変異は、残基２３４．２３５．２３６および２３７ における変性がＦＣガンマＲ１レセプターに対する親和性に少なくとも影響を与 えることを示す。
したがって、本発明の他の観点では、未変成抗体と比較してＰｃガンマＲ１に対 する変性結合親和性を備えた変性Ｆｃ領域を有するクラスＩｇＧの変成抗体が提 供される。
このような抗体は、残基２３４．２３５．２３６および２３７に修飾を有すのが 都合がよい。
他のＦｃレセプターに対する親和性は異なる方法における免疫反応を制御するな どの同様の方法で変性することができる。
さらに他の例として、補体のＣＩ酸成分結合によるＩｇＧの溶菌性を変性するこ とも研究された。
補体系、ＣＩの第一成分は実際にはＣ１ｑ、Ｃ１ｒおよびＣ１ｓとして公知の３ 種類のタンパク質からなり、これらは強く結合している。Ｃ１ｑは３種のタンパ ク質錯体のＩｇへの結合に対して応答性を有することがわかった。
分離されたＦｃフラグメントはＣ１ｑとｒｇとの相互作用を阻害することがわか った（　Ｙａｓｍｅｅｎら、１９７６年）。
また、ＣＩＱの結合はイオン強度に依存し、イオン相互作用が関連することがわ かった。
ｃｇ３領域を１ｇ分子の他の部分から切り取ることが可能であり、ＣＨ３領域の 欠失によってＣ１ｑ結合活性はなくならないことがわかった（Ｃｏｌｏｍｂおよ びＰｏｒｔｅｒ、　１９７５年）。
ＣＨ２領域をＩｇＧから分離することも可能である。このような分離ＣＩ２領域 は分離したＦＣフラグメントと同様にＣＩＡに対して同一の結合親和性を有する ことがわかった（Ｉｓｅｎｍａｎら、１９７５年）。
このような結果からＣＩＱに対する結合部位はＩｇのＣＨ２領域に位置すると推 測される。ＣＩＡ結合に含まれるＣ８２領域中の特定のアミノ酸残基を同定する ために様々な試みがなされた。最初の手法では、Ｃ１１２領域の短い部分に対応 する合成ペプチドがＣ１ｑ結合の阻止のために試された。これによって二つの可 能な結合部位が同定された（Ｂｏａｋｌｅら、１９７５年およびＬｕｋａｓら、 １９８１年）。
第二の手法では、数個のＩｇＣｎ２領域の配列の比較が、その三次元構造の研究 と共に行われた。この結果、ＣＩＱ結合の部位に関する二つの他の案の同定に至 った（ｆ３ｒｇｎｈｏｕｓｅおよびＣｅｂｒａ、　１９７９年ＨＢｕｒｔｏｎら 、１９８０年）。
抗体のＣ１ｑ結合活性は、変性したＣｌ４２領域を有する抗体を提供することに より変性することができ、ここでＨ鎖の少なくとも一つのアミノ酸残基３１ｇ、 ３２０および３２２は異なる側鎖を有する残基に変更されることがわかった。
Ｈ鎖中の残基の番号はＥＵインデックスの番号である（Ｋａｂａｔら、１９８３ 年参照）。
本発明者らは、以下に述べる特異的なＣ１ｑ結合ＩＮにおいて、３１８（Ｇｌｕ ）、３２０（Ｌｙｓ）および３２２（Ｌｙｓ）のいずれか一つの残基をＡｌａに 変えることによりＣＩＱ結合をなくすことが可能であることを見いだした。
さらに、これらの残基において変異を起こさせることにより、残基３１８が水素 結合側鎖を有し、かっ残基３２０および３２２の両者が正に荷電されｆこ側鎖を 有するかぎり、Ｃ１ｑ結合が保持されることがわかった。
本出願人らは、これら三つの残基はＩｇＧへのＣＩＱの結合に直接関連するので あろうと信する。しかしながら、またこれら残基はＣＩＱとの物理的接触には直 接関係しない可能性もある。これら残基は一つのＣｎ　２領域が、ＩｇＧ集合体 中の隣接領域に対して充填するのを補助し、この結果Ｃ１ｑ結合にともに必要な 少なくとも二つのＩｇＧ分子を産生ずる。
この場合、ＣＩＱは全く異なった領域中のＩｇＧと直接接触状態にあってもよい 。しかしながら、本出願人らはいずれにせよこれらの理論のいずれかに限定され ることを希望するものではない。
従来の研究では残基３３３（Ｇｌｕ）をＣＩＱ結合に関連づけているが、３つの 特定の残基に近接した残基３３３（Ｇｌｕ）、または３つの特定の残基から離れ た残基２５３　（Ｉｌｅ）の変性はＣ１ｑ結合活性を変性しない。
残基３１ｇ、３２０および３２２は、補体結合であるマウスおよびヒトＩｇＧ中 に高度に維持されることに注目すべきるだけで、抗原結合活性、プロティンＡ結 合活性（プロティンＡは０Ｍ２／Ｃ１１３インターフエースに結合する）または ＦＣのマウスマクロファージへの結合能力は変性させないことがわかった。
本発明の方法は、３つの特定の残基のいずれか１つをその側鎖上の不適当な機能 性を有する残基で置換することによりＣＩＱ結合活性をなくすことに用いること ができると確信する。Ａｌｔのみを有するイオン性残基をＣＩＡ結合で置換する 必要はない。また、ＣＩＱ結合をなくするため、３つの残基のいずれか１つの代 わりに他のＧｌｙ、Ｉ　ｌｅ、ＬｅｕまたはＶλＩなどのアルキル置換非イオン 性残基、あるいはＰｈｅ％Ｔｙｒ、ＴｙｐおよびＰｒｏなどの芳香族非極性残基 を用いることも可能である。また、Ｃ１ｑ結合活性をなくするために残基３２０ および３２２（３１８は除く）の代わりにＳｅｔ、Ｔｈｒ、ＣｙｓおよびＭｅｔ のような極性非イオン性残基を用いることも可能である。
イオン性または非イオン性極性残基上の側鎖はＧｌｕ残基により形成される結合 と同様の方法で水素結合を形成することができる。したがって、極性残基による ３１８（Ｇｌｕ）残基の置換は修正されてよいが、ＣＩＱ結合活性をなくすこと はない。
さらにＡｌａによる２９７（Ａｓｎ）の置換は、溶菌活性を除去し、一方ｃｔｑ に対する親和性を僅かだけ減少させる（約１／３に弱くなる）ことがわかった。
これは変性°がグリコジル化部位を破壊するたわであり、かつ補体活性化のため に炭化水素の存在が必要であると考えられる。この部位における他の置換いずれ もグリコジル化部位を破壊する。
さらに、Ｌｙｓ３２０のＧｉｎへの変異は、Ｃ１ｑに対する親和性を正常型に比 べ僅かだけ弱くするが非溶菌性である。
これは良好なＣ１ｑ結合が溶解には不充分でありかつ多分Ｃ１ｑの正確な配向が 要求されることを示す。
現在までの全ての抗体イソタイプは、マウスＩｇＧ２ｂ抗体に移植する場合、Ｃ ＩＱ結合要素（ｍｏｔｉｆ）またはＣＩＡの結合に効果的な密接に関連した要素 を備える。明らかに溶解の決定因子が他に存在するはずである。例えば、短いヒ ンジおよび低セグメント柔軟性を有する抗体イソタイプは非溶解性（Ｏｆら、１ ９８４年）であり、（ａ）モチーフを有するＣ１ｑの相互作用はＦａｂアームに よるＦｃの限定された手法のために立体的にブロックされ得る（　Ｌｅａｔｈｅ ｒｂａｒｒｏ智ら、１９８５年）か、または（ｂ）　Ｃ１ｑと抗体との相互作用 が溶解のために正確な配列を必要としこのためそれ自体幾分柔軟性を必要とする ことが示唆される。
つぎに本発明を添付の図面を参照し実施例により説明する。
第１図はＩｇの構造を示す。
第２図は変性したＦｃガンマＲ１結合活性の抗体を産生ずるために用いるクロー ニングステップの手順を示す。
第３図はマウスＩｇＧガンマ２ｂ遺伝子の配列を示す。
第４図はＵ９３７上の高親和性レセプターに対してマウスガンマ２ｂ免疫グロブ リンを用いて結合したＩｆｉＪにて標識したプール（ｐｏｏｌｅｄ）ヒトＩｇＧ の阻止を示すグラフである。
第５図はＵ９３７高親和性レセプターに結合したＩＩＪ−ＥＬ２３５のスキャッ チャードプロットである。
第６図はヒトガンマ３遺伝子のヌクレオチド配列およびタンパク質配列を示す。
第７図は変異を有するマウスＩｇＧ２ｂ抗体のｃａ２領域をコード化するオリゴ ヌクレオチド配列、および幾つかの後記変異体を構成するために用いられるオリ ゴヌクレオチドの配列を示す。
つぎにヒトＰｃガンマＲ１に対するその親和性を変性するマウスＩｇＧ２ｂに関 しての実験についで述べる。
抗体の可変および定常領域エクソンをコード化するＤＮＡは、ｉｎ　ｖｉｔｒｏ で操作し、リンパ細胞系中に再導入することができる（Ｎｅｕｂｅｒｇｅｒ、　 １９８５年）。ｐＳＶ−ｇｐｔに基づくベクター（ＭｕｌｌｉｇａｎおよびＢｅ ｒｇ、　１９８１年）およびＩｇＨ鎖プロモーター／エンハンサ−を用いると、 抗体は発現し分泌される。
このような一つのベクター、ｐ　Ｓ　Ｖ−ＶＮＰ　２　ｂ　（Ｎｅｕｂｅｒｇｅ ｒおよびｌ１ｌｌｉａｓｓ、　１９８５年）はニトロフェニルアセチル（ＮＰ） および正常マウスＩｇＧ２ｂ抗体の定常領域を結合する様々な領域をコード化す る。このベクターを用いて産生された抗体はヒトＰｃガンマＲ１に結合しない。
ｐＳＶ　ＶＮＰ　２ｂベクターの構造の一部を第２（ａ）図に示す。第２（ｂ） 図に示すごとく、該ベクターは５ａｃｌを用いて部分的に消化され、ＣＨ２およ びＣＨ３の両領域を含むフラグメントはプラスミド　Ｍ　１３　Ｋ　Ｉ　９　（ Ｃａｒｔｅｒら、１９８５ユ）にクローンされる。
Ｃ６３領域のＮ末端の５ａｃｌ部位は、このＮ末端にアミノ酸配列を保持したオ リゴヌクレオチドを用いた部位定方向突然変異誘発により除去された。
ついで、ＣＨ２領域における点変異は、第３図に示すように塩基９５６９７５問 および標識ＥＬ２３５にて示される領域にて合成オリゴヌクレオチドを用いて生 ずる。より詳細な変異の構造は以下に述べる。点変異の機構を第２（ｃ）図に示 す。　。
変異ＣＨ２ＣＩ！３７７グメントはｐＳＶ−ＶＮＰ　２ｂベクター中に再クロー ンされ、正常型ｃａ２−　ｃｌＩ３領域を置換する。変異体ｐＳＶ−ＶＮＰ　２ ｂベクターは、Ｊ５５８Ｌに取り込まれて培養され抗体を産生じ、ＥＬ２３５と して公知の抗体変異体がＮＩＰ−セファロース上に精製される。
Ｃガンマ２エクソン中の　異の構造 変異はＣａｒｔｅｒら（１９８５ａ）に記載のＭｌ　３Ｂ１９−Ｃガンマ　２／ Ｃガンマ３中にて行われた。この原理および方法は、Ｃａｒｔｅｒら（１９８５ ａ）およびＤｕｎｃａｎに詳細に記載されている。
該変異体ＥＬ２３５は、ヒトＩｇＧの結合の抑制およびヒト単球細胞系への直接 結合により検定されるＱｏｏｆら、１９８４；　１９８６）。、ヒト単球細胞系 、Ｕ９３７上の高親和性Ｆｃレセプターへの単量体の１″５Ｉで標識した正常プ ールヒト１ｇＧの結合の抑制は、定量的な微生物学的検定システムにて測定され 、ここで遊離あるいは細胞結合標識は水−非混和性オイルを用いて遠心分離によ り分離された。正常型ガンマ２ｂおよび変異体ＥＬ２３５の結合は、標識したポ リクローナルヒトＩｇＧの競合により比較される。第４図はこの実験の阻止曲線 を示す。第４図において白丸は正常型を示し、黒丸は変異体ＥＬ２３５を示す。
結果は阻害剤（ｉｎｈｉｂｉｔａｏｒ）の不存在下にＩ！Ｊ　ＩｇＧの結合分率 ＝１となるよう標準化した。変異体はヒトＩｇＧ１の結合を阻止し、正常型のタ ンパク質は阻止活性を示さなかった。放射性標識をした変異体ＥＬ２３５のＵ９ ３７細胞への直接結合は、結合定数３．１３Ｘ　１０　”Ｍ”を与え（第５図） 、同様の実験のプールヒト１ｇＧの値と非常に近似している。
第５図はＵ９３７高親和性ＦＣレセプターに結合する”’Ｉ　−ＥＬ　２３５の 典型的なスキャッチャードプロットである。細胞のモル当たりの”Ｊ−ＥＬ２３ ５結合のモル数、ｒはつぎの関係式を用いて計算した。
６×１０”ＸＩｇＧ　２ｂ 式中、ＩｇＧ２ｂ１：結合”’Ｉ　−ＥＬ　２３５ノ濃＆テｊ５ル。
Ａは遊離のｌ″Ｊ−ＥＬ２３５の濃度をあられす。プロットの相関関数は０．９ ５であった。
このように点変異は、ヒトＦｃガンマＲ１に対するマウスＩｇＧ２ｂの結合親和 性を１００倍以上変性する。
変異はヒトガンマ３遺伝子内にて行われ（Ｈｕｃｋら、１９８５年）、Ｈｉｎｄ Ｉ［ｌ−３ｐＨＩフラグメントは、ＢａｍＨ１リンカ−に付着した後、最初にＭ １３ｍｐ１９内にサブクローンされた。ついで、合成オリゴヌクレオチドが前記 のごとく使用され第６図に示すごとく変異： ２３４ＬｅｕからＡｌａ ２３５ＬｅｕからＧｌｕ ２３６Ｇ１ｙからＡｌｔ ２３７ＧｌｙからＡｌａ を形成した。
ＢλｍＨＩフラグメントは、ＢＩ３抗体の可変領域をコード化するＨｉｎｄｌｌ ｌ−ＢλｍＨＩフラグメントに付着しくＮｅｕｂｅｒｇｅｒら、１９８４および １９８５に記載）、ｐＳＶｇｐｔベクター中に発現するようクローンされる。
ＰｃガンマＲ１における結合の組替え抗体の性質は、第４図に関連して述べたよ うに競合検定法（ｃｏｍｐｅｔｉｔｉｏｎ　ａｓｓａｙ）にて間接的に決定した 。第１表はｌ！５！で標識したブールヒト１ｔｘＧの結合を阻止するに必要な抗 体のＵ９３７細胞に対する濃度を示す。
第１表 ■、。（Ｍ） 正常型 （Ｌ　ｅｕ２３４、Ｌ　ｅｕ２３５、Ｇ　１ｙ２３６、Ｇ　１ｙ２３７）　１０ −”変異体 Ａ１ａ２３４　４ｘｌＯ−” Ｇｌｕ　２３５　１０−・超 Ａ１ａ２３６　５ｘｔｏ−＠ Ａ１ａ２３７　５ｘｔｏ−’ 上記の表は夏、。（即ち、ＳＩで標識したブールヒトＩｇＧの結合分率が０．５ におけるＩ　ｇＧ３の濃度）の概数を示す。
これらの結果は前記のごとく、診断および治療においてマウスおよびヒトの両抗 体の使用に関し重要な意味を持つ。
この結果はＦｃガンマＲ１レセプターが選択的にスイッチオンまたはオフされる ことを示し、これは人および他の動物に用い得ることを示す。
同様の実験がＣＩＱの溶解活性、ついで結合を変性するためにマウスＩｇＧ２ｂ について行われた。さらにｐＳＶ−ＶＮＰ２ｂベクターの変異体は、前記の方法 にて産生され、点変異はｃ＊２領域中にて合成オリゴヌクレオチドを用いて第７ 図に示すごとく行われ、抗体が前記のごとく産生された。
ｐｓｉ−ＶＮＰ２ｂベクターを用い正常型Ｃ！１２−Ｃ１１３領域で産生された 抗体は、Ｃ１ｑを結合する（第２表参照）。
得られた精製抗体の特異的ＮＩＰ−ケファリン誘導ヒツジ赤血球（Ｗｅｌｔｚｉ ｅｎら、１９８４年）を溶解する能力は定量的溶血微生物学的検定法（Ｙｏｕｎ ｇら、１９８６年）により測定した。測定結果を第２表に示す。μｇ／ｍ１２抗 体で表した力価は、３０分後３７℃における５０％溶解に要する抗体の量をあら れす。
変異抗体の数は、Ｎ　Ｐ−Ａｆｆｉｎｇｅｌ上の抗ＮＰ抗体を凝集させた後、放 射性標識ＣＩＱに対する親和性で試験した（Ｌｅａｔｈｅｒｂａｒｒｏｖおよび Ｄｗｅｋ、　１９１１４年）。この結果も第２表に示す。
第２表 ＩｇＧ　力価Ｃμｇ／ｍ１２）　親和性ｎＭＭｏ１ｇＧ２ｂ　３　１０ Ｍ　ｏ　Ｉ　Ｅ　Ｍ　’　０．１５　−ＭｏｌｇＧＩ　Ｘ　− Ｍｏ１ｇＧ２ｂの無関係な変異体 Ｐｒｏ３３１−Ａｌａ　３　− Ｐｒｏ３３１−Ｇｌｙ　−１２ Ｇ１ｕ３３３−Ａｌａ　３　１２ Ｔｈｒ３３５−Ａｌａ　３　１０ Ｓｅｒ３３７−Ａｌａ　３　１１ Ｇｌｕ２８３−Ａｌａ　３　− Ｈ１ｓ２８５−Ａｌａ　３　１２ Ｈｉｓ２９０−Ａｌａ　３　１１ Ｇｌｕ２９４−Ａｌａ　３　− Ｇ１ｎ２３５−Ａｌａ　３　− Ｌｙｓ２４８−Ａｌａ　３　− １１ｅ２５３−Ａｌｉ　３　９ Ｓｅｒ２６７−Ａｌａ　３　− Ａｓｎ２９７−Ａｓｐ　３　− Ｇ１ｎ２７４−Ａｌａ　３　− Ｌｙｓ３１７−Ａｌａ　３　− Ｌｙｓ２３６−Ａｌａ　３　− Ｌｙｓ３４０−Ａｌａ　３　− 溶菌活性をなくすＭｏ１ｇＧ２ｂの変異体Ｇ１ｕ３１８−Ｖｉｌ　Ｘ　− Ｇ１ｕ３１Ｂ−Ａｌｉ　Ｘ　３００超 Ｌｙｓ３２０−Ａｌａ　Ｘ　３００超 Ｌｙｓ３２０−Ｇｌｎ　Ｘ　１３ Ｌｙｓ３２２−Ａｌａ　Ｘ　３００超 Ｌｙｓ３２２−Ｇｌｕ　Ｘ　− Ａｓｎ２９７−Ａｌａ　Ｘ　３１ 溶菌活性を保持するＭｏ１ｇＧ２ｂの変異体Ｇｌｕ３１Ｂ−Ｔｈｒ　３　１２ Ｌｙｓ３２０−Ａｒｇ　３　１１ Ｌｙｓ３２２−Ａｒｇ　３　１１ ヒトＩｇＧ１およびマウスＩｇＧ１に付着するＶＮＰ領域を有する抗体は、各々 エム、ブルゲマン博士（Ｍ、　Ｂｒｕｇｇｅｍａｎｎ）びＬｙｓ３２２−Ａｌａ は劇的に親和性が減少した（第２表）。
しかしながら、これらはＮＰハブテンおよびプロティンＡの結合を保持する（Ｃ Ｈ２−０，３インターフエイスで結合する）。
このことから、Ｃ１ｑ結合の損失は抗体の構造変化が主な原因ではないことが示 唆される。隣接残基（Ｇ１ｎ３３３−Ａｌａ）または遠隔の残基（Ｉ　１　ｅ２ ５３−Ａｌ　ａ）はｃｉｑ親和性を保持する。
この結果から残基３１８．３２０および３２２により定義された表面パッチは、 ＩｇＧがＣＩＱと相互に作用するか否かを決定することが示唆される。これらの 残基はヒトおよびマウスＩｇＧに高度に保持され、これら３箇所における側鎖の 変性は、補体を活性化しないか、または補体に対する強化された親和性を有する ヒト０Ｍ２領域の変異体を治療上有用に組み立てるために用い得ることがわかる 。
この表面パッチがＣＩＱに対する完全な結合部位である証拠は、Ｇ１ｕＸＬｙｓ ＸＬｙｓ要素を含むポリペプチド模造品から判明し、該要素はモデル系中でのＣ ＩＱ溶菌を阻止することがわかる。この研究は本出願と同日付にて提出の発明の 名称「補体結合ペプチド」として現在係属中のリサーチ・コーポレーシタンによ るＰＣＴ出願第　号に記載されている。
本発明は単に説明のために上記のごとく記載されたにすぎず、変形および変更は 本発明の範囲を逸脱しないかぎり可能であることがわかる。
アブラムソン、エヌ０、ゲルファント、イー、ダブリュー８、ヤンドル、ジェイ 、エイチ、およびローゼン、エフ、ニス。
（Ａｂｒａｍｓｏｎ、　ｌｉ、、　Ｇｅ１４ａｎｄ、　Ｅ、Ｙ、、　Ｊａｎｄｌ 、　Ｊ、Ｈ，、ａｎｄ　Ｒｏｓｅｎ。
Ｆ、Ｓ、　）、１９７０年、Ｊ、　Ｅｘｐ、　Ｍｅｄ、１３２巻、１２０７頁ア ンダーソン、シー、エル、およびルーエイ。アール、ジエイ、　（Ａｎｄｅｒｓ ｏｎ、　Ｃ，Ｌ、、　ａｎｄ　Ｌｏｏｎｅｙ　Ｒ，Ｊ、）、１９８７年、Ｉｍｍ ｕｎｏｌ、　Ｔｏｄａｙ、　７巻、２６４頁バーネット−フォスター、ディー、 イー１、ドーリントン。
ケイ、ジェイ、およびペインター、アール、エイチ。
（Ｂａｒｎｅｔｔ−Ｆｏｓｔｅｒ、　Ｄ、Ｅ、、　Ｄｏｒｒｉｎｇｔｏｎ、　Ｋ 、Ｊ、、　ａｎｄ　Ｐａ１ｎｔｅｒ。
Ｒ」、）、１９８０年、Ｊ、　Ｉｍｍｕｎｏｌ、　１２４巻、２１８６頁ポーク ルら（Ｂｏａｋｌｅ　ｅｔ　ａｔ、、）、１９７５年、！１ａｔｕｒｅ、　２８ ２巻、７４２〜７４３頁 ブルンハウスおよびセブラ（Ｂｒｕｎｈｏｕｓｅ　ａｎｄ　Ｃｅｂｒａ）、１９ ７９年、Ｍｏ１ｅｃ、Ｉｍｍｕｎ、　１６巻、９０７〜９１７頁バートンら（Ｂ ｕｒｔｏｎ　ｅｔ　ａｌ）、１９８０年、！１ｕｔｕｒｅ、　２８８巻、３３８ 〜３４４頁 バートン、ディー、アール、（Ｂｕｒｔｏｎ、　Ｄ、Ｒ，）、１９８５年、Ｍｏ １ｅｃ、　Ｉｍｍｕｎｏｌ、　２２巻、１６１頁バートン、ディー、アール１、 ボイド、ジエイ１、ブランブトン、エイ１、イースターブルック−スミス、ニス ０、エマニスエル。イー、ジェイ０、ノボトニー、ジエイ１、レイドマツカー、 ティー、ダブりニー１、ヴアン、スクラベンデュ−ク、アール１、ステルンベル グ、エム、ジェイ、イー、およびドウエツト、アール、エイ、（Ｂｕｒｔｏｎ、 　Ｄ、Ｒ，、Ｂｏｙｄ、　Ｊ、。
Ｓｔｅｒｎｂｅｒｇ、　Ｍｊ、Ｅ、、　ａｎｄ　Ｄｓｅｔ、　Ｒ，Ａ、）、１９ ８０年、Ｎａｔｕｒｅ。
２８８巻、３３８頁 カーター、ビー５．ベドール、エイチ、およびウィンター・　ジー、　（Ｃａｒ ｔｅｒ、　Ｐ、、　Ｂｅｄｏｕｅｌｌｅ、　Ｈ，、ａｎｄ　Ｗｉｎｔｅｒ、　Ｇ 、）、１９８５ａ％λｕｅｌｅｉｃ　Ａｃ１ｄｓ　Ｒｅｓ、１３巻、４４３１〜 ４４４３頁 カーター、ピー１、ベドール、エイチ０、ウェイ、エム。
ワイ、およびウィンター、ジー、（Ｃａｒｔｅｒ、　Ｐ、、　Ｂｅｄｏｕｅｌｌ ｅ。
■、、Ｗａｙｅ、Ｍ、Ｙ、、ａｎｄ　Ｗｉｎｔｅｒ、Ｇ、）　、　１９８５ｂ、 Ｉｎ：０１ｉｇｏｎｕｃｌｅｏｔｉｄｅ−ｓｉｔｅ−ｄｉｒｅｃｔｅｄ　ｍｕｔ ａｇｅｎｅｓｉｓ　ｉｎ　Ｍ１３゜Ａｎｇｌｉａｎ　Ｂｉｏｔｅｃｈｎｏｌｏｇ ｙ　Ｌｉｍ１ｔｅｄ、　Ｃｏ１ｃｈｅｓｔｅｒ、　Ｅｎｇｌａｎｄ。
コロンおよびポーター（（：（＋１ｏＨｂＢｎｄ　Ｐｏｒｔｅｒ）、１９７５年 、Ｂｉｏｃｈｅｍ　Ｊ、１４５巻、１７７〜１８３頁ダンカン　エイ、アール、 （Ｄｕｎｅａｎ　Ａ、Ｒ，、）　、Ｕｎｉｖｅｒｓｉｔｙｏｆ　Ｃａｍｂｒｉｄ ｇｅ　Ｐｈｅ　Ｔｈｅｓｉｓ　（ｔｏ　ｂｅ　ｐｕｂｌｉｓｈｅｄ）。
エペノトス、エイ０．スナック、ディー９．ダーバン、エイチ０．ジョンソン、 ピー、およびテイラーバパディミトロー、ジェイ、（Ｅｐｅｎｅｔｏｓ、　Ａ、 、　５ｎｏｏｋ、　Ｄ、、　Ｄｕｒｂｉｎ、　Ｈ，、Ｊｏｈｎｓｏｎ、　Ｐ、、 　ａｎｄ　Ｔａｙｌｅｒ−Ｐａｐａｄｉｍｉｔｒｉｏｕ、　Ｊ、）、１９８６年 、Ｃａｎｃｅｒ　Ｒｅｓ、　４６巻、３１８３頁ヘイル、ジー１、クラーク、エ ム、およびウオルドマン。
エイチ、（Ｈａｔｅ、　Ｇ、、　Ｃ１ａｒｋ、　Ｍ、、　ａｎｄ　Ｗａｌｄａｌ ａｎｎ、　Ｈ，）、１９８５年、Ｉｍｍｕｎｏｌ、１１３４巻、３０５６頁ヘイ ル、ジー、およびウォルドマン、エイチ、（Ｂａｌｅ、　Ｇ、。
ａｎｄ　Ｗａｌｄｍａｎｎ、Ｈ，）、１９８５年、ｉｎ　Ｈｙｂｒｉｄｏｍａ　 Ｔｅｃｈｎｏｌｏｇｙｉｎ　ｔｈｅ　Ｂｉｏｓｅｉｅｎｃｅｓ　ａｎｄ　Ｍｅｄ ｉｃｉｎｅ、Ｔ、　Ｓｐｒｉｎｇｅｒ、　ｅｄ、　ＰＩｅｎｕｍ　Ｐｒｅｓｓ、 　Ｎｅｔ　Ｙｏｒｋ。
フーバー、エイチ、およびフーデンベルグ、エイチ、エイチ、（Ｈｕｂｅｒ、　 Ｈ，、ａｎｄ　Ｆｕｄｅｎｂｅｒｇ、　Ｈ，Ｈ，）、１９６８年、Ｉｎｔ。
Ａｒｃｈ、　Ａｌｌｅｒｇｙ　Ａｐｐｌ、Ｉｍｍｕｎｏｌ、３４巻、１８頁ハッ クら（Ｂｕｃｋ　ｅｔ　ａｌ、、）、１９８５年、Ｎｕｃ、　Ａｃ１ｄｓ　Ｒｅ ｓ。
１４巻、１７７９〜１７８８頁 アイセンマンら（Ｉｓｅｎｍａｎ　ｅｔ　ａｌ、、）、１９７５年、Ｊ、　Ｉｍ ｍｕｎｑ１１４巻、１７２６〜１７２９頁 ケイバットら（Ｋａｂａｔ　ｅｔ　ａｌ、、）、１９８３年、”５ｅｑｕｅｎｃ ｅｓｏｆ　Ｐｒｏｔｅｉｎｓ　ｏｆ　１ｍｍｕｎｏｌｏｇｉｃａｌ　Ｉｎｔｅｒ ｅｓｔ’、　ＵＳ　Ｄｅｐｔ、Ｈｅａｌｔｈａｎｄ　Ｅｕｍａｎ　５ｅｒｖｉｃ ｅｓ。
キャロフォノ、エイチ、ピー、およびエペネイト、エイ。
（Ｋａｌｏｆｏｎｏｓ、　Ｈ，Ｐ、、　ａｎｄ　Ｅｐｅｎｅｔｏｓ、　Ａ、）、 １９８６年、ＣａｎｃｅｒＴｒｅａｔｍｅｎｔ　Ｒｅｎｅｗｓ、１３巻、２４３ 頁クレイマーら（Ｋｒａｍｅｒ　ｅｔ　ａｌ、、）、１９８２年、Ｎｕｅ。
Ａｃ１ｄｅｓ　Ｒｅｓ、１０巻、６４７５〜６４８５頁レザーバロウおよしデッ ク（Ｌｅａｔｈｅｒｂａｒｒｏｗ　ａｎｄ　Ｄｖｒｅｃｋ）、１９８４年、Ｍｏ １ｅｃ　Ｉｍｍｕｎ、　２１巻、３２１〜３２７頁レザーバロウしアール、ジェ イ０、レイドメイチャー、ティー、ダブリュー０、デック、アール、エイ９、ウ ォーフ、ジェイ、エム９、クラーク、エイ０、バートン、ディー、アール０、リ チャードソン、エヌ、およびファンスタン、エイ。
（Ｌｅａｔｈｅｒｂａｒｒｏｖ、　Ｒ，Ｊ、、　Ｒａｄｅｍａｃｈｅｒ、　Ｔ、 １．、　Ｄｗｅｋ、　Ｒ，Ａ、。
１ｏｏｆ、　Ｊ、Ｌ、　Ｃ１ａｒｋ、　Ａ、、　Ｂｕｒｔｏｎ、　Ｄ、Ｒ，、Ｒ ｉｃｈａｒｄｓｏｎ、　Ｌ、　ａｎｄ　Ｆｅ１ｎｓｔｅｉｎ、　Ａ、）、１９８ ５年、Ｍｏ１ｅｃ、　Ｉｍｍｕｎ、　２２巻、４０７〜４１５頁 ルイス、ブイ、エイ０、コック、ティー９、ブラトナー。
エイチ、およびメールマン、アイ、　（Ｌｅｂｉｓ、　Ｖ、Ａ、、　Ｋｏｃｈ、 　Ｔ、。
Ｐｌｕｔｎｅｒ、　Ｈ，、ａｎｄ　Ｍｅｌｌｍａｎ、　１．）、１９８６年、Ｎ ａｔｕｒｅ１３２４巻、３７２頁　″ ルーカスら（Ｌｕｋａｓ　ｅｔ　ａｌ、、）、１９８１年、Ｊ、　Ｉｍｍｕｎ。
１２７巻、２５５５〜２５６０頁 ムーリガン、アール、シー１．およびバーグ、ビー。
（Ｍｕｌｌｉｇａｎ、　Ｒ，Ｃ，、ａｎｄ　Ｂｅｒｇ、　Ｐ、）、１９８１年、 Ｐｒｏｃ。
Ｎａｔｌ、　Ａｃａｄ、　Ｓｃｉ、　ＵＳＡ、　７８巻、２０７２頁ニューバー ガー、エム、ニス、およびウィリアムス、ジー。
ティー、（？ｉｅｕｂｅｒｇｅｒ、　Ｍ、Ｓ、、　ａｎｄ　Ｖｉｌｌｉａｍｓ、 　Ｇ、Ｔ、）、１９８６年、Ｐｈ１１．　Ｔｒａｎｓ、　Ｒ，Ｓｏｃ、　Ｌｏｎ ｄ、　Ａ　３１７巻、４２５〜４３２頁 ニューバーガー、エム、ニス６、ウィリアムス、ジー、ティー６、ミッチェル、 イー、ビー１、ジョホール、ニス、ニス１、フラネーガン、ジェイ、ジー、およ びラビッツ、ティー、エイチ、　（Ｎｅｕｂｅｒｇｅｒ、　Ｍ、Ｓ、、　Ｗｉｌ ｌｉａｍｓ、　Ｇ、Ｔ、、　Ｍｉｔｃｈｅｌｌ、　Ｅ、Ｂ、。
Ｊｏｕｈａｌ、Ｓ、ご、、Ｆｌａｎａｇａｎ、Ｊ、Ｇ、、ａｎｄ　Ｒａｂｂｉｔ ｔｓ、Ｔ、Ｈ，）　、１９８５年、Ｎａｔｕｒｅ、　３１４巻、２６８頁ニュー バーガー、エム、ニス１、ウィリアムス、ジー、ティー、およびフｔックス、ア ール、オー、（Ｎｅｕｂｅｒｇｅｒ、　Ｍ、Ｓ、。
Ｖｉｌｌｉａｍｓ、　Ｇ、Ｔ、、　ａｎｄ　Ｆｏｘ、　Ｒ，Ｏ，）、１９８４年 、Ｎａｔｕｒｅ。
３１２巻、６０４〜６０８頁 ノリスら（Ｎｏｒｒｉｓ　ｅｔ　ａｌ、、）、夏９８３年、Ｎｕｃ、　Ａｃ１ｄ ｓＲｅｓ、１１巻、５１０３〜５１１２頁オイ、ブイ、ティー１、ミンーボング 、ティー９、バーディ。
アール、アール９、レイドラ−、ジェイ０、ダングル、ジェイ、エル０、ハーゼ ンベルブ　エル、エイ、およびストシー（Ｏｉ、　Ｖ、Ｔ、、　Ｍｉｎｈ−Ｖｕ ｏｎｇ、　Ｔ、、　Ｈａｒｄｙ、　Ｒ，Ｒ，、Ｒｅ１ｄｌｅｒ、　Ｊ、。
Ｄａｎｇｌ、　Ｊ、Ｌ、、　Ｈｅｒｚｅｎｂｅｒｇ　Ｌ、Ａ、　ａｎｄ　５ｔｒ ｙｅｒ）、１９８４年、Ｎａｔｕｒｅ、　３０７巻、１３６〜１４０頁バートリ ッジ、エル、ジェイ６、ワーフ、ジェイ、エム６、シェフエリ−、アール、およ びバートン、ディー、アール。
（Ｐａｒｔｒｉｄｇｅ、　Ｌ、Ｊ、、　Ｔｏｏｆ、　Ｊ、Ｍ、、　Ｊ＋Ｊｆｅｒ ｉｓ、　Ｒ，、ａｎｄ　Ｂｕｒｔｏｎ。
Ｄ、Ｒ，）、１９８６年、Ｍｏ１ｅｃ、　Ｉｍｍｕｎｏｌ、　２３巻、１３６５ 頁 ラベッチ、ジェイ、ブ礼、ラスター、エイ、ディー９、ウェインシャンク、アー ル１、コーチヤシ。エイ１、パブロベック、ディー、エイ１、ポートノイ、ジエ イ６、ハルメス。
ジェイ６、パン、グイ。エム、シー５、アンクレス、ジエイ。
（Ｒａｖｅｔｃｈ、　Ｊ、Ｖ、、　Ｌｕ５ｔｅｒ、　Ａ、Ｄ、、　Ｖｅｉｎｓｈ ａｎｋ、　Ｒ，、Ｋｏｃｈａｎ。
’Ａ、、　Ｐａｖｌｏｖｅｃ、　Ｄ、Ａ、、　Ｐｏｒｔｎｏｙ、　Ｊ、、　Ｈｕ ｌｍｅｓ、　Ｊ、、　Ｐａｎ、　Ｙ、Ｍ。
Ｃ，、Ｕｎｋｅｌｅｓｓ、　Ｊ、）、１９８６年、５ｃｉｅｎｃｅ、　２３４巻 、７１８頁 サッグス、ニス、ブイ１、ハイローズ、ティー０、ミャケ。
ティー０、カワシマ、イー、エイチ、４、ジョンソン、エム。
ジェイ０、イタクラ、ケイ、およびウォーレイス、アール。
ビー、（Ｓｕｇｇｓ、　Ｓ、Ｖ、、　ｌ１ｌｉｒｏｓｅ、　Ｔ、、　Ｍｉｙａｋ ｅ、　Ｔ、、　Ｋａｓａｓｈｉｍａ。
Ｅ、Ｈ，、Ｊｏｈｎｓｏｎ、　Ｍ、Ｊ、、　Ｉｔａｋｕｒａ、　Ｋ、、　ａｎｄ 　Ｗａｌｌａｃｅ、　Ｒ，Ｂ、）、１９８１年、Ｉｎ：　Ｄｅｖｅｌｏｐｍｅｎ ｔａｌ　Ｂｉｏｌｏｇｙ　ｕｓｉｎｇ　ＰｕｒｉｆｉｅｄＧｅｎｅｓ　（Ｄ、　 Ｂｒｏｗｎ、　ｅｄ、）　ＡｃａｄｅｖＡｉｃ　Ｐｒｅｓｓ、　Ｎｅｔｉ　Ｙｏ ｒｋ。
ウェルザンら０ｅｌｔｚｉｅｎ　ｅｔ　ａｌ、、）、１９８４年、Ｍｏ１ｅｃ。
Ｉｅｍｕｎｏｌ、　２１巻、８０１頁 ワーフ、ジェイ、エム８、ジェファー、エム、アイ１、シェフエリ−、アール、 およびバートン、ディー、アール。
（ｍｏｏｒ、　Ｊ、Ｍ、、　Ｊａｆａａｒ、　Ｍ、１．、　Ｊｅｆｒｅｒｉｓ、 　Ｒ，、ａｎｄ　Ｂｕｒｔｏｎ。
Ｄ、Ｒ，）、１９８４年、Ｍｏ１ｅｃ、　Ｉｍｍｕｎ、２１巻、５２３頁ワーフ 、ジェイ、エム０、バートリッジ、エル、ジエイ１、シェフエリ−、アール、お よびバートン、ディー、アール。
（ｌｆｏｏｆ、　Ｊ、Ｍ、、　Ｐａｒｔｒｉｄｇｅ、　Ｌ、Ｊ、、　Ｊｅｆｆｅ ｒｉｓ、　Ｒ，、ａｎｄ　ＢｕｒｔｏｎＤ、Ｒ，）、１９８６年、Ｍｏ１ｅｃ、 　Ｉｍｍｕｎ、　２３巻、３１９頁ヤスミーンら（Ｙａｓｍｅｅｎ　ｅｔ　ａｌ 、、）、１９７６年、Ｊ。
Ｉｍ＋ａｕｎ、１１６巻、５１８〜５２２頁ヤングら（Ｙｏｕｎｇ　ｅｔ　ａｌ 、、）、１９８６年、Ａｎａｌ、　Ｂｉｏｃｈｅｍ。
特表平１−５０２８７５　（ＩＱ） １５４巻、６４９〜６５４頁 シーラーおよびスミス（Ｚｏｌｌｅｒ　ａｎｄ　Ｓｍ１ｔｈ）、１９８２年、Ｎ ｕｃ、　Ａｃ１ｄｓ　Ｒｅｓ％１０巻、６４８７〜６５０頁シーラーおよびスミ ス（Ｚｏｌｌｅｒ　ａｎｄ　５ｉｉｔｈ）、１９８４年、ＤＮＡ、３巻、４９７ 〜４８８頁 尚　領鐵間卸 ５ａｃｌ　Ｓａｃｌ ＲＰＮ ＣＣＣＴＧＴ？ＲＴＧＧ日ＧＧＲＴＲＰ、５ＣＣＡＴＧＴＡＣＰＩＦＩＲＴＣＣ ＡＴＴＴＣＣＦＩＴ口ＴＣＴＣＣＴＣら＝Ｃ５ＧこＴＣＣＴH’１ ３１匡ｒＲｃＧｃＧＧｃＡＧＴＴＧ　５’　Ｌｙｓ３２２−Ｆｌｌａ３゛区…匡 匡■戸コｓ　１Ｓｅｒ３３７−ＦＩ　Ｉ　。
国際調査報告 一呻一一１静内ｍｍｍ、　ＰＣＴ／Ｇヨ８Ｂ１００２：ＬＬ

Claims (19)

    【特許請求の範囲】
  1. １．定常部分（本明細書で定義する）中の少なくとも１つのアミノ酸残基が、非 変成抗体と比較して抗体のエフェクター機能を変性する異なる残基により置換さ れたクラスＩｇＧの変成抗体。
  2. ２．抗体がエフェクター分子に対する親和性を非変成抗体と比較して変性した請 求項１の抗体。
  3. ３．抗体が正常抗体、キメラ抗体または変性抗体である請求項１の抗体。
  4. ４．非変成抗体と比放してＦｃレセプターに対して変性した結合親和性を備えた 変性Ｆｃ領域を有するクラスＩｇＧの変成抗体。
  5. ５．非変成抗体と比較してＦｃガンマＲＩレセプターに対して変性した結合親和 性を備えた変性Ｆｃ領域を有するクラスＩｇＧの変成抗体。
  6. ６．Ｈ鎖のアミノ酸残基２３４、２３５、２３６および２３７の少なくとも１つ が、単数または複数の異なる残基により置換された請求項５の抗体。
  7. ７．残基２３５がＧｌｕにより置換された請求項６の抗体。
  8. ８．残基２３４、２３６および２３７の少なくとも１つがＡ１ａにより置換され た請求項６の抗体。
  9. ９．非変成抗体と比較してＣｌｑに対して変性した結合親和性を備えた変性Ｆｃ 領域を有するクラスＩｇＧの変成抗体。
  10. １０．Ｈ鎖のアミノ酸残基３１８、３２０および３２２の少なくとも１つが、異 なる側鎖を有する残基に代わった変性ＣＨ２領域を有する請求項９の抗体。
  11. １１．残基３１８、３２０および３２２の少なくとも１つがＣｌｑ結合親和性を 減少するＡ１ａに変えた請求項１０の抗体。
  12. １２．残基３１８がＶａ１に変わった請求項１０の抗体。
  13. １３．残基３２２がＧｌｎに変わった請求項１０の抗体。
  14. １４．非変成抗体と比較して変性した溶解能を備えた変性Ｆｃ領域を有するクラ スＩｇＧの変成抗体。
  15. １５．Ｈ鎖のアミノ酸残基２９７が変性された変性ＣＨ２領域を有する請求項１ ５の抗体。
  16. １６．残基２９７がＡｌａにより置換された請求項１５の抗体。
  17. １７．げっ歯類またはヒトＩｇＧからなる請求項１の抗体。
  18. １８．定常部分（本明細書で定義する）の少なくとも１つのアミノ酸残基を異な る残基で置換し、抗体のエフェクター機能を非変成抗体に比較して変性すること からなるエフェクター分子に対するクラスＩｇＧの抗体のエフェクター機能を変 性する方法。
  19. １９．（ａ）ＩｇＨ鎖またはＬ鎖の定常部の少なくとも一部をコード化し、かつ 少なくとも１つのアミノ酸残基が非変成抗体中の対応する残基と異なるＤＮＡ配 列に作動可能に結合した適当なプロモーターを含む第一の複製可能な表現ベクタ ーを産生し； （ｂ）必要により、相補的ＩｇＬ鎖またはＨ鎖をコード化するＤＮＡ配列に作動 可能に待合した適当なプロモーターを含む第二の複製可能な表現ベクターを産生 し；（ｃ）第一または両方の産生ベクターを有する細胞系を形質転換し： （ｄ）前記形質転換した細胞系を培養して変成抗体を産生する 工程からなる非変成抗体に比較して変性したエフェクター機能を備えたクラスＩ ｇＧの変成抗体を産生する方法。
JP63502461A 1987-03-18 1988-03-18 変性抗体の、または変性抗体に関する改良 Expired - Lifetime JP3101690B2 (ja)

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GB8825480D0 (en) 1989-01-05
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US5624821A (en) 1997-04-29
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