JPH07194384A - 免疫グロブリンｄｎａ含有発現ベクター及び組換え宿主細胞 - Google Patents
免疫グロブリンｄｎａ含有発現ベクター及び組換え宿主細胞Info
- Publication number
- JPH07194384A JPH07194384A JP6241576A JP24157694A JPH07194384A JP H07194384 A JPH07194384 A JP H07194384A JP 6241576 A JP6241576 A JP 6241576A JP 24157694 A JP24157694 A JP 24157694A JP H07194384 A JPH07194384 A JP H07194384A
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- antibody
- dna
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Abstract
(57)【要約】
【目的】 有効な構成成分を有する免疫グロブリンを生
産し得る発現ベクターを提供する。 【構成】 第１の抗体クラス又は第１の哺乳動物種の抗
体の不変領域にホモローガスな不変領域と、第２の異な
った抗体クラス又は哺乳動物種の抗体の可変領域にホモ
ローガスな可変領域を有する免疫グロブリンをコードし
ているＤＮＡを含有している発現ベクター。
産し得る発現ベクターを提供する。 【構成】 第１の抗体クラス又は第１の哺乳動物種の抗
体の不変領域にホモローガスな不変領域と、第２の異な
った抗体クラス又は哺乳動物種の抗体の可変領域にホモ
ローガスな可変領域を有する免疫グロブリンをコードし
ているＤＮＡを含有している発現ベクター。
Description
【０００１】本発明は、免疫グロブリン産生の分野及び
天然に生ずる免疫グロブリンアミノ酸配列の改変に関す
るものである。詳細には、本発明は、組換技術を使用し
て、脊椎動物系に通常見られるものと同類(analogous)
である双方の免疫グロブリンを産生すると共に、これら
遺伝子改変技術を利用してキメラ型又はその他の改変型
を作成することに関するものである。
天然に生ずる免疫グロブリンアミノ酸配列の改変に関す
るものである。詳細には、本発明は、組換技術を使用し
て、脊椎動物系に通常見られるものと同類(analogous)
である双方の免疫グロブリンを産生すると共に、これら
遺伝子改変技術を利用してキメラ型又はその他の改変型
を作成することに関するものである。
【０００２】Ａ．免疫グロブリン及び抗体 抗体は、外来蛋白質,糖蛋白質,細胞又はその他の抗原性
外来物質による攻撃に反応して脊椎動物免疫系により産
生される特異的な免疫グロブリンポリペプチドである。
生物が外来細胞による侵入を克服し或るいは外来物質を
その生物系から除去し得る一連の過程は、少なくとも部
分的に理解されている。この過程の重要な部分は、特定
の外来物質に対して特異的に結合する抗体の製造であ
る。特定抗原に対するこの種のポリペプチドの結合特異
性は極めて精巧なものであり、個々の脊椎動物により発
生し得る特異性の多様性は著しく複雑で変化に富むもの
である。多数の抗原が反応を誘発し得るが、それらの反
応は殆んどそれを誘発した特定抗原のみに対するもので
ある。
外来物質による攻撃に反応して脊椎動物免疫系により産
生される特異的な免疫グロブリンポリペプチドである。
生物が外来細胞による侵入を克服し或るいは外来物質を
その生物系から除去し得る一連の過程は、少なくとも部
分的に理解されている。この過程の重要な部分は、特定
の外来物質に対して特異的に結合する抗体の製造であ
る。特定抗原に対するこの種のポリペプチドの結合特異
性は極めて精巧なものであり、個々の脊椎動物により発
生し得る特異性の多様性は著しく複雑で変化に富むもの
である。多数の抗原が反応を誘発し得るが、それらの反
応は殆んどそれを誘発した特定抗原のみに対するもので
ある。
【０００３】免疫グロブリンは、上記したような抗体と
抗原特異性を欠如した同類の蛋白物質との両者を包含す
る。後者はリンパ系では低レベルで産生されるが骨髄腫
では高レベルで産生される。
抗原特異性を欠如した同類の蛋白物質との両者を包含す
る。後者はリンパ系では低レベルで産生されるが骨髄腫
では高レベルで産生される。
【０００４】Ａ．１．起源及び用途 現在、脊椎動物抗体の２種の主な起源が利用されてい
る:即ち、哺乳動物Ｂリンパ球によるin situ生成及びＢ
細胞ハイブリッドによる細胞培養物(cell culture)にお
ける生成である。抗体は未熟のＢリンパ球がプラズマ細
胞(形質細胞)へ分化する結果としてin situで生成さ
れ、これは特異抗原による刺激に反応して生ずる。未分
化のＢ細胞では、免疫グロブリン鎖上の種々の領域をコ
ードしているＤＮＡ部分はゲノムＤＮＡ内で隔てられて
存在している。これら配列は転写前に順次再配列され
る。この過程の概略はＧough, Ｔrends in Ｂiochem．
Ｓci．,６:２０３(１９８１)に記載されている。得られ
る再配列ゲノムは、成熟Ｂリンパ球内で発現し所望の抗
体を産生することができる。然しながら、単一の抗原の
みが特定哺乳動物の免疫系圏内に入る場合でさえ、均一
な抗体群が生じるわけではない。特定抗原に対するin s
ituでの免疫反応は、抗原に存在する各種決定因子に対
する反応のモザイクにより規定される。単一群(single
population)のＢ細胞が相同抗体(homologous antibody)
の各サブセットに寄与し、従ってin situでの抗体の生
成は「ポリクローナル」である。
る:即ち、哺乳動物Ｂリンパ球によるin situ生成及びＢ
細胞ハイブリッドによる細胞培養物(cell culture)にお
ける生成である。抗体は未熟のＢリンパ球がプラズマ細
胞(形質細胞)へ分化する結果としてin situで生成さ
れ、これは特異抗原による刺激に反応して生ずる。未分
化のＢ細胞では、免疫グロブリン鎖上の種々の領域をコ
ードしているＤＮＡ部分はゲノムＤＮＡ内で隔てられて
存在している。これら配列は転写前に順次再配列され
る。この過程の概略はＧough, Ｔrends in Ｂiochem．
Ｓci．,６:２０３(１９８１)に記載されている。得られ
る再配列ゲノムは、成熟Ｂリンパ球内で発現し所望の抗
体を産生することができる。然しながら、単一の抗原の
みが特定哺乳動物の免疫系圏内に入る場合でさえ、均一
な抗体群が生じるわけではない。特定抗原に対するin s
ituでの免疫反応は、抗原に存在する各種決定因子に対
する反応のモザイクにより規定される。単一群(single
population)のＢ細胞が相同抗体(homologous antibody)
の各サブセットに寄与し、従ってin situでの抗体の生
成は「ポリクローナル」である。
【０００５】この限られてはいるが固有の異質性は、多
くの特定の場合に、ハイブリドーマ技術を用いて「モノ
クローナル」抗体を生成させることにより克服された(Ｋ
ohleret al．,Ｅur．Ｊ．Ｉmmunol．,６:５１１(１９７
６))。この方法に於いては、抗原を注射した哺乳動物に
由来する脾細胞又はリンパ球を腫瘍細胞系(セルライン)
と融合させてハイブリッド細胞即ち「ハイブリドーマ」を
作製する。これらハイブリッド細胞は、不滅(永久的に
増殖可能)であると共にＢ細胞の遺伝学的にコードされ
た抗体を産生することができる。このように生成された
ハイブリッドを選択、希釈及び再増殖により遺伝的に単
一の株に分離すると、各株は単一の遺伝系を示す。従っ
て、これらは所望の抗原に対し免疫反応性の抗体を産生
し、これら抗体は同質であることが確証され、その純粋
な遺伝起源(genetic parentage)に基いて「モノクローナ
ル」と呼ばれる。細胞融合技術は現在まで主としてネズ
ミ系の融合に集中しているが、ヒト−ヒトハイブリドー
マ(Ｌ．Ｏlsson et al．,Ｐroc．Ｎatl．Ａcad．Ｓci．
ＵＳＡ,７７:５４２９(１９８０))、並びにヒト−ネズ
ミハイブリドーマ(Ｊ．Ｓchlom et al．,同上,７７:６
８４１(１９８０))及びその他数種の異種間ハイブリッ
ド組合せも同様に作成されている。或いは抗体産生一次
Ｂ細胞(primary Ｂ cell)が、ウィルスＤＮＡでの形質
転換によるin vitroで永久株化されている。
くの特定の場合に、ハイブリドーマ技術を用いて「モノ
クローナル」抗体を生成させることにより克服された(Ｋ
ohleret al．,Ｅur．Ｊ．Ｉmmunol．,６:５１１(１９７
６))。この方法に於いては、抗原を注射した哺乳動物に
由来する脾細胞又はリンパ球を腫瘍細胞系(セルライン)
と融合させてハイブリッド細胞即ち「ハイブリドーマ」を
作製する。これらハイブリッド細胞は、不滅(永久的に
増殖可能)であると共にＢ細胞の遺伝学的にコードされ
た抗体を産生することができる。このように生成された
ハイブリッドを選択、希釈及び再増殖により遺伝的に単
一の株に分離すると、各株は単一の遺伝系を示す。従っ
て、これらは所望の抗原に対し免疫反応性の抗体を産生
し、これら抗体は同質であることが確証され、その純粋
な遺伝起源(genetic parentage)に基いて「モノクローナ
ル」と呼ばれる。細胞融合技術は現在まで主としてネズ
ミ系の融合に集中しているが、ヒト−ヒトハイブリドー
マ(Ｌ．Ｏlsson et al．,Ｐroc．Ｎatl．Ａcad．Ｓci．
ＵＳＡ,７７:５４２９(１９８０))、並びにヒト−ネズ
ミハイブリドーマ(Ｊ．Ｓchlom et al．,同上,７７:６
８４１(１９８０))及びその他数種の異種間ハイブリッ
ド組合せも同様に作成されている。或いは抗体産生一次
Ｂ細胞(primary Ｂ cell)が、ウィルスＤＮＡでの形質
転換によるin vitroで永久株化されている。
【０００６】ポリクローナル又は特に好ましくはモノク
ローナル抗体は、本発明の抗体と同様な多くの有用な性
質を有する。例えばこれらは、Ｂ細胞ゲノムの初期プロ
セッシングを誘発する抗原の存在を、この抗原−抗体反
応を適当な検出技術、例えば検定(ＲＩＡ,ＥＭＩＴ及び
ＥＬＩＳＡ)を可能にする放射性同位元素又は酵素によ
る標識と組合せることによって、検出するための特異的
免疫沈澱試薬として使用することができる。このよう
に、抗体は多くの抗原物質に対する免疫診断試験の基礎
となる。他の重要な用途において、抗体は問題とする抗
原を含有する物質又は有機体による攻撃を受けた対象被
検体に直接注射して、この攻撃に対処することができ
る。この方法は現在その実験段階にあるが、その有力性
は明らかである。第３に、全身診断及び処置も可能とな
る。何故なら、注射された抗体は特定の標的病気組織に
指向させられ、従って、これらと共に適当な標識を運ぶ
ことにより病気の存在を決定し、或いは適当な薬剤を運
ぶことにより病気組織を攻撃するために使用することが
できる。
ローナル抗体は、本発明の抗体と同様な多くの有用な性
質を有する。例えばこれらは、Ｂ細胞ゲノムの初期プロ
セッシングを誘発する抗原の存在を、この抗原−抗体反
応を適当な検出技術、例えば検定(ＲＩＡ,ＥＭＩＴ及び
ＥＬＩＳＡ)を可能にする放射性同位元素又は酵素によ
る標識と組合せることによって、検出するための特異的
免疫沈澱試薬として使用することができる。このよう
に、抗体は多くの抗原物質に対する免疫診断試験の基礎
となる。他の重要な用途において、抗体は問題とする抗
原を含有する物質又は有機体による攻撃を受けた対象被
検体に直接注射して、この攻撃に対処することができ
る。この方法は現在その実験段階にあるが、その有力性
は明らかである。第３に、全身診断及び処置も可能とな
る。何故なら、注射された抗体は特定の標的病気組織に
指向させられ、従って、これらと共に適当な標識を運ぶ
ことにより病気の存在を決定し、或いは適当な薬剤を運
ぶことにより病気組織を攻撃するために使用することが
できる。
【０００７】ハイブリドーマにより産生されるモノクロ
ーナル抗体は、理論的には上記したように有効であり且
つその特異性によりポリクローナル抗体よりも明らかに
好適であるが、或る種の欠点を有する。第１に、これら
はハイブリドーマ(従って、哺乳動物)起源の他の蛋白質
及び細胞物質で汚染される傾向がある。これらの細胞は
更に、発癌性を高め、発生し又は媒介し得る物質、特に
核酸断片を含有し、更に蛋白質断片も含有する。第２
に、モノクローナル抗体を産生するハイブリドーマ系は
不安定な傾向があり、産生される抗体の構造が変化した
り、抗体産生が完全に停止したりする(Ｇ．Ｋohler et
al．,Ｐroc．Ｎatl．Ａcad．Ｓci．,ＵＳＡ,７７:２１
９７(１９８０);Ｓ．Ｌ．Ｍorrison,Ｊ．Ｉmmunol．１
２３:７９３(１９７９))。細胞系ゲノムは、現在その性
質が未知であるような刺激に反応してそれ自体で変化(a
lteration)すると思われ、その結果誤った配列を産生し
得る。第３に、ハイブリドーマ及びＢ細胞は共に或る種
の抗体をグリコシル化型で産生することが避けられず
(Ｆ．Ｍelchers, Ｂiochemistry,１０:６５３(１９７
１))、これは或る場合には望ましくないものである。第
４に、モノクローナル抗体及びポリクローナル抗体の産
生はいずれも比較的高価である。第５に、恐らく最も重
要なことであるが、現在の技術(ハイブリドーマ又はＢ
細胞反応)による産生では、成熟Ｂ細胞由来抗原に反応
してin situで通常誘発されるものよりも有効な構成成
分を有する抗体を産生すべくゲノムを操作することがで
きない。本発明の抗体は上記の欠点をもたず、更に優秀
な分子を提供する機会を与える。
ーナル抗体は、理論的には上記したように有効であり且
つその特異性によりポリクローナル抗体よりも明らかに
好適であるが、或る種の欠点を有する。第１に、これら
はハイブリドーマ(従って、哺乳動物)起源の他の蛋白質
及び細胞物質で汚染される傾向がある。これらの細胞は
更に、発癌性を高め、発生し又は媒介し得る物質、特に
核酸断片を含有し、更に蛋白質断片も含有する。第２
に、モノクローナル抗体を産生するハイブリドーマ系は
不安定な傾向があり、産生される抗体の構造が変化した
り、抗体産生が完全に停止したりする(Ｇ．Ｋohler et
al．,Ｐroc．Ｎatl．Ａcad．Ｓci．,ＵＳＡ,７７:２１
９７(１９８０);Ｓ．Ｌ．Ｍorrison,Ｊ．Ｉmmunol．１
２３:７９３(１９７９))。細胞系ゲノムは、現在その性
質が未知であるような刺激に反応してそれ自体で変化(a
lteration)すると思われ、その結果誤った配列を産生し
得る。第３に、ハイブリドーマ及びＢ細胞は共に或る種
の抗体をグリコシル化型で産生することが避けられず
(Ｆ．Ｍelchers, Ｂiochemistry,１０:６５３(１９７
１))、これは或る場合には望ましくないものである。第
４に、モノクローナル抗体及びポリクローナル抗体の産
生はいずれも比較的高価である。第５に、恐らく最も重
要なことであるが、現在の技術(ハイブリドーマ又はＢ
細胞反応)による産生では、成熟Ｂ細胞由来抗原に反応
してin situで通常誘発されるものよりも有効な構成成
分を有する抗体を産生すべくゲノムを操作することがで
きない。本発明の抗体は上記の欠点をもたず、更に優秀
な分子を提供する機会を与える。
【０００８】抗体特異性を欠如している免疫グロブリン
でさえ、抗体自身よりは小さい範囲の潜在的用途である
が有用である。現在まで理解されたこの種の免疫グロブ
リンの用途としては、グロブリン関連貧血に対する蛋白
質補充治療がある。この意味で、抗原に結合し得ないこ
とは実際に有益である。何故ならこれら蛋白質の治療価
値はこのような機能により阻害されるからである。現
在、この種の非特異性抗体は、適当に誘発された骨髄腫
細胞培養物からのみ少量で誘導することができる。本発
明は、それに代わる一層経済的な起源を提供する。更
に、本発明は四元体(tetramer)の４つの鎖を別々に処理
することにより特異性を消却する機会を与える。
でさえ、抗体自身よりは小さい範囲の潜在的用途である
が有用である。現在まで理解されたこの種の免疫グロブ
リンの用途としては、グロブリン関連貧血に対する蛋白
質補充治療がある。この意味で、抗原に結合し得ないこ
とは実際に有益である。何故ならこれら蛋白質の治療価
値はこのような機能により阻害されるからである。現
在、この種の非特異性抗体は、適当に誘発された骨髄腫
細胞培養物からのみ少量で誘導することができる。本発
明は、それに代わる一層経済的な起源を提供する。更
に、本発明は四元体(tetramer)の４つの鎖を別々に処理
することにより特異性を消却する機会を与える。
【０００９】Ａ．２．一般的構造特性 脊椎動物系に於ける基本的な免疫グロブリン構造単位は
現在充分に理解されている(Ｇ．Ｍ．Ｅdelman, Ａnn．
Ｎ．Ｙ．Ａcad．Ｓci．,１９０:５(１９７１))。これら
の単位は、分子量約２３,０００ダルトンの２つの同一
のＬポリペプチド鎖と分子量５３,０００〜７０,０００
の２つの同一なＨ鎖とから構成されている。これら４つ
の鎖はジスルフィド結合により「Ｙ」形状で結合され、こ
こでＬ鎖は、図１に示すように、Ｙの口部から出発し分
岐領域を通って連続するＨ鎖を包囲する。「枝」部分は、
図に示したようにＦab領域と呼ばれる。Ｈ鎖はγ,μ,
α,δ又はεとして更にこれらのいくつかのサブクラス
に分類され、この鎖の性質はこれが長い不変領域を有す
るためＩgＧ,ＩgＭ,ＩgＡ,ＩgＤ又はＩgＥとしての抗体
の「クラス」を決定する。Ｌ鎖はκ又はλとして分類され
る。各Ｈ鎖のクラスはκ又はλのいずれのＬ鎖とも組合
せて作成することができる。Ｌ鎖とＨ鎖とは互いに共有
結合され、免疫グロブリンがハイブリドーマ又はＢ細胞
により生成される際に２つのＨ鎖の「テイル(尾部)」部分
は共有ジスルフィド結合により互いに結合される。然し
ながら、正確な配置に於いて、鎖の非共有的会合が起こ
っても、集合体は抗原との反応が同様に可能であり、或
いは非特異的免疫グロブリンとして蛋白質補充に有用で
ある。
現在充分に理解されている(Ｇ．Ｍ．Ｅdelman, Ａnn．
Ｎ．Ｙ．Ａcad．Ｓci．,１９０:５(１９７１))。これら
の単位は、分子量約２３,０００ダルトンの２つの同一
のＬポリペプチド鎖と分子量５３,０００〜７０,０００
の２つの同一なＨ鎖とから構成されている。これら４つ
の鎖はジスルフィド結合により「Ｙ」形状で結合され、こ
こでＬ鎖は、図１に示すように、Ｙの口部から出発し分
岐領域を通って連続するＨ鎖を包囲する。「枝」部分は、
図に示したようにＦab領域と呼ばれる。Ｈ鎖はγ,μ,
α,δ又はεとして更にこれらのいくつかのサブクラス
に分類され、この鎖の性質はこれが長い不変領域を有す
るためＩgＧ,ＩgＭ,ＩgＡ,ＩgＤ又はＩgＥとしての抗体
の「クラス」を決定する。Ｌ鎖はκ又はλとして分類され
る。各Ｈ鎖のクラスはκ又はλのいずれのＬ鎖とも組合
せて作成することができる。Ｌ鎖とＨ鎖とは互いに共有
結合され、免疫グロブリンがハイブリドーマ又はＢ細胞
により生成される際に２つのＨ鎖の「テイル(尾部)」部分
は共有ジスルフィド結合により互いに結合される。然し
ながら、正確な配置に於いて、鎖の非共有的会合が起こ
っても、集合体は抗原との反応が同様に可能であり、或
いは非特異的免疫グロブリンとして蛋白質補充に有用で
ある。
【００１０】アミノ酸配列は、Ｙの頂部のＮ−末端から
各鎖の底部のＣ−末端まで延在する。Ｎ−末端は、抗体
を誘発した抗原に対し特異的で且つ長さ約１００個のア
ミノ酸から成る可変領域であり、この可変領域はＬ鎖と
Ｈ鎖との間及び抗体毎に僅かの変動がある。各鎖の可変
領域は、鎖の残余の長さに亘って延在する不変領域と結
合している。Ｌ鎖とＨ鎖の結合は、ゲノムレベルで見
て、約１２個のアミノ酸をコードするＬ鎖遺伝子内の
「Ｊ」領域として、並びに両方で約２５個のアミノ酸をコ
ードするＨ鎖遺伝子内の「Ｄ」領域と「Ｊ」領域との組合せ
として、現在知られている結合配列を介して生ずるもの
と思われる。
各鎖の底部のＣ−末端まで延在する。Ｎ−末端は、抗体
を誘発した抗原に対し特異的で且つ長さ約１００個のア
ミノ酸から成る可変領域であり、この可変領域はＬ鎖と
Ｈ鎖との間及び抗体毎に僅かの変動がある。各鎖の可変
領域は、鎖の残余の長さに亘って延在する不変領域と結
合している。Ｌ鎖とＨ鎖の結合は、ゲノムレベルで見
て、約１２個のアミノ酸をコードするＬ鎖遺伝子内の
「Ｊ」領域として、並びに両方で約２５個のアミノ酸をコ
ードするＨ鎖遺伝子内の「Ｄ」領域と「Ｊ」領域との組合せ
として、現在知られている結合配列を介して生ずるもの
と思われる。
【００１１】鎖の残余の部分は不変領域と呼ばれ、特定
のクラス内では、抗体の特異性(即ち、これを誘発する
抗原)と共に変化しない。上記したように、５種の主要
な公知クラスの不変領域が存在し、これらは免疫グロブ
リン分子のクラス(Ｈ鎖不変領域のγ,μ,α,δ及びεに
対応するＩgＧ,ＩgＭ,ＩgＡ,ＩgＤ及びＩgＥ)を決定す
る。不変領域もしくはクラスは、補体の活性化(Ｅ．
Ａ．Ｋabat,“Ｓtructural Ｃoncepts in Ｉmmunology
and Ｉmmunochemistry",第２版,p．４１３−４３６, Ｈ
olt, Ｒinehart, Ｗinston(１９７６))及びその他の細
胞反応(Ｄ．Ｗ．Ａndrews et al．,Ｃlinical Ｉmmunob
iology,p．１−１８,Ｗ．Ｂ．Ｓanders(１９８０);Ｓ．
Ｋohl et al．,Ｉmmunology,４８:１８７(１９８３))を
含め、抗体のその後のエフェクター機能を決定する一
方、可変領域はこれが反応する抗原を決定する。
のクラス内では、抗体の特異性(即ち、これを誘発する
抗原)と共に変化しない。上記したように、５種の主要
な公知クラスの不変領域が存在し、これらは免疫グロブ
リン分子のクラス(Ｈ鎖不変領域のγ,μ,α,δ及びεに
対応するＩgＧ,ＩgＭ,ＩgＡ,ＩgＤ及びＩgＥ)を決定す
る。不変領域もしくはクラスは、補体の活性化(Ｅ．
Ａ．Ｋabat,“Ｓtructural Ｃoncepts in Ｉmmunology
and Ｉmmunochemistry",第２版,p．４１３−４３６, Ｈ
olt, Ｒinehart, Ｗinston(１９７６))及びその他の細
胞反応(Ｄ．Ｗ．Ａndrews et al．,Ｃlinical Ｉmmunob
iology,p．１−１８,Ｗ．Ｂ．Ｓanders(１９８０);Ｓ．
Ｋohl et al．,Ｉmmunology,４８:１８７(１９８３))を
含め、抗体のその後のエフェクター機能を決定する一
方、可変領域はこれが反応する抗原を決定する。
【００１２】Ｂ．組換ＤＮＡ技術 組換ＤＮＡ技術は、遺伝子配列のクローニング及び発現
に関する技術が集積されて充分高度な状態に達してい
る。各種のＤＮＡ配列をかなり容易に組換えて、形質転
換微生物及び細胞培養物に於いて異種蛋白質産物を産生
し得る新規なＤＮＡ配列を創成することができる。ＤＮ
Ａの各種の平滑末端断片又は「粘着(付着性)」末端断片を
in vitroで結合して発現ベクターを産生させ且つ生物を
形質転換させる一般的手段及び方法が現在使用できる。
に関する技術が集積されて充分高度な状態に達してい
る。各種のＤＮＡ配列をかなり容易に組換えて、形質転
換微生物及び細胞培養物に於いて異種蛋白質産物を産生
し得る新規なＤＮＡ配列を創成することができる。ＤＮ
Ａの各種の平滑末端断片又は「粘着(付着性)」末端断片を
in vitroで結合して発現ベクターを産生させ且つ生物を
形質転換させる一般的手段及び方法が現在使用できる。
【００１３】必須要素(即ち、複製のオリジン、１種も
しくはそれ以上の表現型選択特性、発現制御配列、異種
遺伝子挿入物(インサート))及び残余のベクターのＤＮ
Ａ組換えは、一般に宿主細胞の外部で行なわれる。得ら
れる複製可能な組換発現ベクター即ちプラスミドを形質
転換により細胞中へ導入し、多量の組換ベヒクルを形質
転換体の増殖によって得る。コードされているＤＮＡメ
ッセージの転写及び翻訳を支配する部分に関し、遺伝子
が適正に挿入された場合、得られる発現ベクターは挿入
遺伝子がコードするポリプペチド配列を産生するのに有
用であり、この過程を「発現」と呼ぶ。得られる産物は、
必要に応じ、宿主細胞の溶菌及び適当な精製による他の
蛋白質からの産物の回収によって得ることができる。
しくはそれ以上の表現型選択特性、発現制御配列、異種
遺伝子挿入物(インサート))及び残余のベクターのＤＮ
Ａ組換えは、一般に宿主細胞の外部で行なわれる。得ら
れる複製可能な組換発現ベクター即ちプラスミドを形質
転換により細胞中へ導入し、多量の組換ベヒクルを形質
転換体の増殖によって得る。コードされているＤＮＡメ
ッセージの転写及び翻訳を支配する部分に関し、遺伝子
が適正に挿入された場合、得られる発現ベクターは挿入
遺伝子がコードするポリプペチド配列を産生するのに有
用であり、この過程を「発現」と呼ぶ。得られる産物は、
必要に応じ、宿主細胞の溶菌及び適当な精製による他の
蛋白質からの産物の回収によって得ることができる。
【００１４】実際上、組換ＤＮＡ技術の使用は、全く異
種のポリプペチドを発現することができ(所謂直接的発
現)、或いは同種(homologous)ポリプペチドのアミノ酸
配列の一部に融合した異種ポリプペチドを発現すること
もできる。後者の場合、目的とする生物活性産物は、し
ばしばそれが細胞外環境で開裂されるまで融合した同種
／異種ポリプペチド内で生物不活性にされている。
種のポリプペチドを発現することができ(所謂直接的発
現)、或いは同種(homologous)ポリプペチドのアミノ酸
配列の一部に融合した異種ポリプペチドを発現すること
もできる。後者の場合、目的とする生物活性産物は、し
ばしばそれが細胞外環境で開裂されるまで融合した同種
／異種ポリプペチド内で生物不活性にされている。
【００１５】遺伝学及び細胞生理学の研究のための細胞
もしくは組織培養物並びに微生物系を維持する技術は充
分確立されている。単離した細胞から順次トランスファ
ーすることにより作成された永久細胞系を維持するため
の手段及び方法が使用できる。研究に使用する目的に
は、この種の細胞系は液体媒体中の個体支持体上に維持
され、或いは支持栄養源を含有する懸濁物中での増殖に
より維持される。大量生産への規模拡大は、単に機械的
問題を提起するだけと思われる。
もしくは組織培養物並びに微生物系を維持する技術は充
分確立されている。単離した細胞から順次トランスファ
ーすることにより作成された永久細胞系を維持するため
の手段及び方法が使用できる。研究に使用する目的に
は、この種の細胞系は液体媒体中の個体支持体上に維持
され、或いは支持栄養源を含有する懸濁物中での増殖に
より維持される。大量生産への規模拡大は、単に機械的
問題を提起するだけと思われる。
【００１６】本発明は、適当な宿主細胞培養物を用いる
組換技術により生成される抗体及び非特異性免疫グロブ
リン(ＮＳＩ)に関するものである。これらの抗体及びＮ
ＳＩは、純粋な「モノクローナル」形態で容易に製造する
ことができる。これらをゲノムレベルで処理して互いに
異なる種からの相同性(homology)を引き出す変種のキメ
ラを生成することができる。更に、４つの鎖全部を同じ
細胞で生成する必要はないので、蛋白質レベルで処理す
ることもできる。従って、多くの「タイプ」の免疫グロブ
リンが本発明に包含される。
組換技術により生成される抗体及び非特異性免疫グロブ
リン(ＮＳＩ)に関するものである。これらの抗体及びＮ
ＳＩは、純粋な「モノクローナル」形態で容易に製造する
ことができる。これらをゲノムレベルで処理して互いに
異なる種からの相同性(homology)を引き出す変種のキメ
ラを生成することができる。更に、４つの鎖全部を同じ
細胞で生成する必要はないので、蛋白質レベルで処理す
ることもできる。従って、多くの「タイプ」の免疫グロブ
リンが本発明に包含される。
【００１７】第１に、哺乳動物Ｂ細胞によりin situで
又は適当な永続性腫瘍系と融合したＢ細胞、即ちハイブ
リドーマにより産生される天然に存在する抗体のアミノ
酸配列に類似する免疫グロブリン特に抗体は、組換技術
を用いて産生される。第２に、本発明方法により、従来
性質が互いに関連するとは思われていなかったポリプペ
チドから成る免疫グロブリンが産生され、本発明はこの
ような免疫グロブリンに係る。この種の再編成は、２種
以上の抗原を結合し得る「ハイブリッド」抗体を産生する
のに特に有用であり、且つ異なる起源のＨ鎖とＬ鎖とが
実質的に特異性を減弱化する「複合」免疫グロブリンを産
生するのに有用である。第３に、遺伝子操作によって、
例えば可変領域は１種の哺乳動物モデル系からのアミノ
酸配列に対応し、不変領域は他の哺乳動物モデル系のア
ミノ酸配列に類似するような「キメラ」抗体を生成するこ
とができる。更に、これら２種の類似配列は、異なる種
から誘導することができる。第４に、遺伝子操作によ
り、特異性及びその他の特性が向上した「改変」抗体を生
成することもできる。
又は適当な永続性腫瘍系と融合したＢ細胞、即ちハイブ
リドーマにより産生される天然に存在する抗体のアミノ
酸配列に類似する免疫グロブリン特に抗体は、組換技術
を用いて産生される。第２に、本発明方法により、従来
性質が互いに関連するとは思われていなかったポリプペ
チドから成る免疫グロブリンが産生され、本発明はこの
ような免疫グロブリンに係る。この種の再編成は、２種
以上の抗原を結合し得る「ハイブリッド」抗体を産生する
のに特に有用であり、且つ異なる起源のＨ鎖とＬ鎖とが
実質的に特異性を減弱化する「複合」免疫グロブリンを産
生するのに有用である。第３に、遺伝子操作によって、
例えば可変領域は１種の哺乳動物モデル系からのアミノ
酸配列に対応し、不変領域は他の哺乳動物モデル系のア
ミノ酸配列に類似するような「キメラ」抗体を生成するこ
とができる。更に、これら２種の類似配列は、異なる種
から誘導することができる。第４に、遺伝子操作によ
り、特異性及びその他の特性が向上した「改変」抗体を生
成することもできる。
【００１８】２つの他のタイプの免疫グロブリン様の部
分が産生され得る:即ち、標的組織に対するホーミング
キャリア(homing carrier)として有用な「単一価(unival
ent)」抗体及び免疫グロブリン分子の「Ｆab」領域、即ち
「Ｙ」の枝のみを含む「Ｆab蛋白質」である。これらの単一
価の抗体及びＦab断片も「哺乳動物性(哺乳動物由来)」と
することができ、即ち哺乳動物由来のアミノ酸配列に類
似する。例えば、不変配列パターン及び可変配列パター
ンが異なる起源であるような哺乳動物鎖もしくはキメラ
の新規な組立ても可能である。最後に、組換技術により
産生されるＬ鎖もしくはＨ鎖のみ、或いはその部分のい
ずれも本発明に包含され、哺乳動物性であってもキメラ
であってもよい。
分が産生され得る:即ち、標的組織に対するホーミング
キャリア(homing carrier)として有用な「単一価(unival
ent)」抗体及び免疫グロブリン分子の「Ｆab」領域、即ち
「Ｙ」の枝のみを含む「Ｆab蛋白質」である。これらの単一
価の抗体及びＦab断片も「哺乳動物性(哺乳動物由来)」と
することができ、即ち哺乳動物由来のアミノ酸配列に類
似する。例えば、不変配列パターン及び可変配列パター
ンが異なる起源であるような哺乳動物鎖もしくはキメラ
の新規な組立ても可能である。最後に、組換技術により
産生されるＬ鎖もしくはＨ鎖のみ、或いはその部分のい
ずれも本発明に包含され、哺乳動物性であってもキメラ
であってもよい。
【００１９】他の面に於いて、本発明は、上記のＮＳ
Ｉ,抗体及びその部分をコードするＤＮＡ並びに適当な
宿主細胞に於いてこの種の免疫グロブリンの産生を行な
い得る発現ベクター又はプラスミドに向けられる。本発
明は、これらベクターにより形質転換して得られる宿主
細胞及び細胞培養物も包含する。最後に本発明はこれら
ＮＳＩ及び抗体の製造方法並びにＤＮＡ配列、プラスミ
ド及びそれらによる形質転換細胞に向けられる。
Ｉ,抗体及びその部分をコードするＤＮＡ並びに適当な
宿主細胞に於いてこの種の免疫グロブリンの産生を行な
い得る発現ベクター又はプラスミドに向けられる。本発
明は、これらベクターにより形質転換して得られる宿主
細胞及び細胞培養物も包含する。最後に本発明はこれら
ＮＳＩ及び抗体の製造方法並びにＤＮＡ配列、プラスミ
ド及びそれらによる形質転換細胞に向けられる。
【００２０】詳細な説明 Ａ．定義 本明細書中に使用する「抗体」という用語は、特異的免疫
反応活性を有する四元体(tetramer)又はその集合体(agg
regate)を意味し、通常図１の「Ｙ」形状に合体されたＬ
鎖とＨ鎖とから成り、これら連鎖の間に共有結合を有し
又は持たない。「免疫グロブリン」という用語は、特異的
免疫反応活性があるかないかに拘らず、この種の集合体
(assembly)又はその一部を意味する。「非特異的免疫グ
ロブリン」(「ＮＳＩ」)という用語は、特異性を持たない
免疫グロブリン、即ち抗体でないものを意味する。
反応活性を有する四元体(tetramer)又はその集合体(agg
regate)を意味し、通常図１の「Ｙ」形状に合体されたＬ
鎖とＨ鎖とから成り、これら連鎖の間に共有結合を有し
又は持たない。「免疫グロブリン」という用語は、特異的
免疫反応活性があるかないかに拘らず、この種の集合体
(assembly)又はその一部を意味する。「非特異的免疫グ
ロブリン」(「ＮＳＩ」)という用語は、特異性を持たない
免疫グロブリン、即ち抗体でないものを意味する。
【００２１】「哺乳動物抗体」という用語は、鎖のアミノ
酸配列がin situで又はハイブリドーマに於いて哺乳動
物系により産生される抗体に見られるような配列と相同
(homologous)である抗体を意味する。これらの抗体は、
不純な形態であるが慣用の系においても生成され得るよ
うな抗体に類似する。
酸配列がin situで又はハイブリドーマに於いて哺乳動
物系により産生される抗体に見られるような配列と相同
(homologous)である抗体を意味する。これらの抗体は、
不純な形態であるが慣用の系においても生成され得るよ
うな抗体に類似する。
【００２２】「ハイブリッド抗体」という用語は、鎖が個
別に対応の哺乳動物抗体の鎖と相同である新規な集合体
を示し、従って２つの異なる抗原が四元体により沈澱し
得るような抗体を意味する。ハイブリッド抗体に於いて
一方のＨ鎖とＬ鎖との対は１つの抗原に対して生じた抗
体と相同であり、Ｈ鎖とＬ鎖との他方の対は他の抗原に
対して生じた抗体と相同である。この結果、「二価(deva
lence)」の性質が生じ、即ち２つの抗原に同時に結合す
る能力が生ずる。勿論、この種のハイブリッドは下記す
るようなキメラ鎖を用いて生成することもできる。
別に対応の哺乳動物抗体の鎖と相同である新規な集合体
を示し、従って２つの異なる抗原が四元体により沈澱し
得るような抗体を意味する。ハイブリッド抗体に於いて
一方のＨ鎖とＬ鎖との対は１つの抗原に対して生じた抗
体と相同であり、Ｈ鎖とＬ鎖との他方の対は他の抗原に
対して生じた抗体と相同である。この結果、「二価(deva
lence)」の性質が生じ、即ち２つの抗原に同時に結合す
る能力が生ずる。勿論、この種のハイブリッドは下記す
るようなキメラ鎖を用いて生成することもできる。
【００２３】「複合(composite)」免疫グロブリンという
用語は、Ｈ鎖とＬ鎖とが異なる種の起源又は特異性のも
のに類似し、従って得られたものが非特異的免疫グロブ
リン(ＮＳＩ)になると思われ、即ち抗体特性を欠如する
と思われるようなものを意味する。
用語は、Ｈ鎖とＬ鎖とが異なる種の起源又は特異性のも
のに類似し、従って得られたものが非特異的免疫グロブ
リン(ＮＳＩ)になると思われ、即ち抗体特性を欠如する
と思われるようなものを意味する。
【００２４】「キメラ抗体」という用語は、Ｈ鎖とＬ鎖と
の各アミノ酸配列の１部が特定種に由来する又は特定ク
ラスに属する抗体の対応配列と相同であり、且つ鎖の残
部が他の対応配列と相同であるような抗体を意味する。
典型的には、これらキメラ抗体に於いて、Ｌ鎖とＨ鎖と
の両者の可変領域は哺乳動物の１種に由来する抗体の可
変領域に類似し、不変部分は他の哺乳動物に由来する抗
体の配列と相同である。この種のキメラ型に対する１つ
の明らかな利点は、例えば容易に入手し得るハイブリド
ーマ又はヒト以外の宿主生物由来Ｂ細胞を、例えばヒト
細胞調製物に由来する不変領域と組合せて使用すること
により、現在公知の起源から可変領域を便利に誘導し得
ることである。可変領域は製造が容易であるという利点
を有し且つ特異性はその起源により影響されないが、不
変領域がヒト由来であるために、抗体を注射した場合、
ヒト以外の起源に由来する不変領域よりもヒト被験者に
対する免疫反応を誘発しにくいと思われる。
の各アミノ酸配列の１部が特定種に由来する又は特定ク
ラスに属する抗体の対応配列と相同であり、且つ鎖の残
部が他の対応配列と相同であるような抗体を意味する。
典型的には、これらキメラ抗体に於いて、Ｌ鎖とＨ鎖と
の両者の可変領域は哺乳動物の１種に由来する抗体の可
変領域に類似し、不変部分は他の哺乳動物に由来する抗
体の配列と相同である。この種のキメラ型に対する１つ
の明らかな利点は、例えば容易に入手し得るハイブリド
ーマ又はヒト以外の宿主生物由来Ｂ細胞を、例えばヒト
細胞調製物に由来する不変領域と組合せて使用すること
により、現在公知の起源から可変領域を便利に誘導し得
ることである。可変領域は製造が容易であるという利点
を有し且つ特異性はその起源により影響されないが、不
変領域がヒト由来であるために、抗体を注射した場合、
ヒト以外の起源に由来する不変領域よりもヒト被験者に
対する免疫反応を誘発しにくいと思われる。
【００２５】然しながら、この定義はこの特定例に限定
されない。即ち、Ｈ鎖もしくはＬ鎖の一方又は双方が異
なる起源の抗体の配列に類似した配列の組合せから成る
任意の抗体を包含し、これらの起源は異なるクラスであ
っても、異なる抗原反応であっても、或いは異なる種の
起源があってもよく、融合点(fusion point)が可変／不
変領域の境界に存在するかどうかに関係ない。従って、
不変領域も可変領域も公知の抗体配列に類似しないよう
な抗体を産生することができる。このようにして、例え
ば可変領域が特定抗原に対しより高度の特異親和性を有
するか、又は不変領域が向上した補体固定反応(complem
ent fixation)を誘発させ得るような抗体を作成するこ
とができ、或いは特定の不変領域が有する性質を更に改
善することができる。
されない。即ち、Ｈ鎖もしくはＬ鎖の一方又は双方が異
なる起源の抗体の配列に類似した配列の組合せから成る
任意の抗体を包含し、これらの起源は異なるクラスであ
っても、異なる抗原反応であっても、或いは異なる種の
起源があってもよく、融合点(fusion point)が可変／不
変領域の境界に存在するかどうかに関係ない。従って、
不変領域も可変領域も公知の抗体配列に類似しないよう
な抗体を産生することができる。このようにして、例え
ば可変領域が特定抗原に対しより高度の特異親和性を有
するか、又は不変領域が向上した補体固定反応(complem
ent fixation)を誘発させ得るような抗体を作成するこ
とができ、或いは特定の不変領域が有する性質を更に改
善することができる。
【００２６】「改変(変容)抗体(altered antibody)」とい
う用語は、アミノ酸配列が哺乳動物の抗体又はその他の
脊椎動物の抗体とは変化している抗体を意味する。本発
明に対して組換ＤＮＡ技術が適切であるため、天然抗体
に見られるアミノ酸の配列に制限する必要はない。抗体
を再設計して所望の特性を得ることができる。可能な変
化は数多く、僅か１個もしくは数個のアミノ酸の変化か
ら例えば不変領域の完全な再設計に至る範囲とすること
ができる。一般に、不変領域に於ける変化は例えば補体
固定、膜との相互作用及びその他の作用機能のような細
胞処理特性(cellular process characteristics)を改良
させるために行なわれる。可変領域に於ける変化は、抗
原結合特性を改良するために行なわれる。更に、抗体を
工学的に処理して「魔法玉(magic bullet)」概念に従って
毒性剤(toxic agent)を特異的に放出する役に立てるこ
ともできる。改変(alteration)は標準的組換技術により
行なうことができ、又オリゴヌクレオチド−指向突然変
異誘発技術(aligonucleotide−directed mutagenesis t
echniques)によっても行なうことができる(Ｄalbadie−
ＭcＦarland et al．,Ｐroc．Ｎatl．Ａcad．Ｓci．,Ｕ
ＳＡ,７９:６４０９(１９８２))。
う用語は、アミノ酸配列が哺乳動物の抗体又はその他の
脊椎動物の抗体とは変化している抗体を意味する。本発
明に対して組換ＤＮＡ技術が適切であるため、天然抗体
に見られるアミノ酸の配列に制限する必要はない。抗体
を再設計して所望の特性を得ることができる。可能な変
化は数多く、僅か１個もしくは数個のアミノ酸の変化か
ら例えば不変領域の完全な再設計に至る範囲とすること
ができる。一般に、不変領域に於ける変化は例えば補体
固定、膜との相互作用及びその他の作用機能のような細
胞処理特性(cellular process characteristics)を改良
させるために行なわれる。可変領域に於ける変化は、抗
原結合特性を改良するために行なわれる。更に、抗体を
工学的に処理して「魔法玉(magic bullet)」概念に従って
毒性剤(toxic agent)を特異的に放出する役に立てるこ
ともできる。改変(alteration)は標準的組換技術により
行なうことができ、又オリゴヌクレオチド−指向突然変
異誘発技術(aligonucleotide−directed mutagenesis t
echniques)によっても行なうことができる(Ｄalbadie−
ＭcＦarland et al．,Ｐroc．Ｎatl．Ａcad．Ｓci．,Ｕ
ＳＡ,７９:６４０９(１９８２))。
【００２７】「単一価の抗体(univalent antibody)」とい
う用語は、第２のＨ鎖のＦc(もしくはステム)領域に結
合したＨ鎖／Ｌ鎖ダイマーから成る集合体(aggregatio
n)を意味する。この種の抗体は抗原に対し特異的である
が、特異抗原表面を有する組織を標的とする所望の性質
を更に有し、その抗原有効性(antigenic effectivenes
s)を損うことがなく、即ち抗原変調(antigenic modulat
ion)がない。この点に関する単一価の抗体の現象及び性
質はＭ．Ｊ．Ｇlennie et al．,Ｎature,２９５:７１２
(１９８２)に示されている。従来、単一価の抗体は蛋白
質分解により形成されていた。
う用語は、第２のＨ鎖のＦc(もしくはステム)領域に結
合したＨ鎖／Ｌ鎖ダイマーから成る集合体(aggregatio
n)を意味する。この種の抗体は抗原に対し特異的である
が、特異抗原表面を有する組織を標的とする所望の性質
を更に有し、その抗原有効性(antigenic effectivenes
s)を損うことがなく、即ち抗原変調(antigenic modulat
ion)がない。この点に関する単一価の抗体の現象及び性
質はＭ．Ｊ．Ｇlennie et al．,Ｎature,２９５:７１２
(１９８２)に示されている。従来、単一価の抗体は蛋白
質分解により形成されていた。
【００２８】「Ｆab」領域とは、Ｈ鎖のＹ枝部分から成る
配列に対し、及び全体的にＬ鎖に対しほぼ均等又は同様
(analogous)であり且つ全体(集合体)として抗体活性を
有することが示されている鎖の部分を意味する。「Ｆab
蛋白質」(この蛋白質は本発明の一面を構成する)は、１
つのＨ鎖と１つのＬ鎖との集合体(aggregate)(一般にＦ
ab'として知られる)並びに抗体Ｙの２つの枝部分に対応
する四元体(一般にＦ(ab)2として知られる)を包含し、
これらはいずれも共有的に又は非共有的に集合される。
但し、この集合は特定抗原又は抗原群(antigen family)
と選択的に反応することができる。Ｆab抗体は単一価の
抗体と同様に、従来蛋白質分解により生成されており、
標的組織に対する抗原変調を誘発しないという性質を有
する。然しながら、これらは「エフェクター」Ｆc部分を
欠如するので例えばマクロファージによる標的細胞の溶
菌を行なうことができない。
配列に対し、及び全体的にＬ鎖に対しほぼ均等又は同様
(analogous)であり且つ全体(集合体)として抗体活性を
有することが示されている鎖の部分を意味する。「Ｆab
蛋白質」(この蛋白質は本発明の一面を構成する)は、１
つのＨ鎖と１つのＬ鎖との集合体(aggregate)(一般にＦ
ab'として知られる)並びに抗体Ｙの２つの枝部分に対応
する四元体(一般にＦ(ab)2として知られる)を包含し、
これらはいずれも共有的に又は非共有的に集合される。
但し、この集合は特定抗原又は抗原群(antigen family)
と選択的に反応することができる。Ｆab抗体は単一価の
抗体と同様に、従来蛋白質分解により生成されており、
標的組織に対する抗原変調を誘発しないという性質を有
する。然しながら、これらは「エフェクター」Ｆc部分を
欠如するので例えばマクロファージによる標的細胞の溶
菌を行なうことができない。
【００２９】「Ｆab蛋白質」は、一般的用語「抗体」もしく
は「免疫グロブリン」と同様に本発明の定義に従う同様な
サブセットを有する。即ち、「哺乳動物」Ｆab蛋白質、
「ハイブリッド」Ｆab蛋白質、「キメラ」Ｆab及び「改変(al
tered)」Ｆab蛋白質が種々のタイプの抗体につき上記に
示した対応の定義と同様に規定される。
は「免疫グロブリン」と同様に本発明の定義に従う同様な
サブセットを有する。即ち、「哺乳動物」Ｆab蛋白質、
「ハイブリッド」Ｆab蛋白質、「キメラ」Ｆab及び「改変(al
tered)」Ｆab蛋白質が種々のタイプの抗体につき上記に
示した対応の定義と同様に規定される。
【００３０】勿論、個々のＨ鎖もしくはＬ鎖は、上記に
従って「哺乳動物」、「キメラ」又は「改変」とすることがで
きる。発明の詳細な説明から明らかとなるように、開示
技術を使用して特定的に定義したもの以外に、例えば、
キメラＬ鎖及び哺乳動物Ｈ鎖を含有するハイブリッド抗
体、哺乳動物Ｌ鎖と共にＨ鎖のキメラＦab蛋白質を含有
するハイブリッドＦab蛋白質、等のような４ペプチド鎖
の集合体のその他の組合せを製造することができる。
従って「哺乳動物」、「キメラ」又は「改変」とすることがで
きる。発明の詳細な説明から明らかとなるように、開示
技術を使用して特定的に定義したもの以外に、例えば、
キメラＬ鎖及び哺乳動物Ｈ鎖を含有するハイブリッド抗
体、哺乳動物Ｌ鎖と共にＨ鎖のキメラＦab蛋白質を含有
するハイブリッドＦab蛋白質、等のような４ペプチド鎖
の集合体のその他の組合せを製造することができる。
【００３１】「発現ベクター」という用語は、そこに含有
されるＤＮＡ配列を発現し得るベクターを包含し、即ち
コード配列は発現を行ない得るその他の配列に有効に発
現するように結合される。これは必ずしも明確に規定さ
れないが、これらの発現ベクターは宿主生物に於いてエ
ピソームとして、又は染色体ＤＮＡの一体的部分として
複製し得るものでなければならないことを意味する。明
らかに、複製可能性が欠如することは、有効に機能し得
なくなる。有効な発現ベクターの有用であるが必ずしも
必要でない要素は、マーカーコード配列であり、即ち容
易に細胞を固定し得る蛋白質を含有する細胞の表現型特
性(たとえばテトラサイクリン耐性)をもたらすような蛋
白質をコードする配列である。要するに、「発現ベクタ
ー」には機能的定義が与えられ、特定の含有ＤＮＡコー
ドを発現し得る全てのＤＮＡ配列がこの用語に包含さ
れ、同様に特定の配列に適用される。現在この種のベク
ターはしばしばプラスミドの形態であるので、「プラス
ミド」と「発現ベクター」とはしばしば互換的に使用され
る。然しながら、本発明は均等な機能を有し且つ時と共
に当業界で公知となり得るような他の形態の発現ベクタ
ーをも包含することを意図する。
されるＤＮＡ配列を発現し得るベクターを包含し、即ち
コード配列は発現を行ない得るその他の配列に有効に発
現するように結合される。これは必ずしも明確に規定さ
れないが、これらの発現ベクターは宿主生物に於いてエ
ピソームとして、又は染色体ＤＮＡの一体的部分として
複製し得るものでなければならないことを意味する。明
らかに、複製可能性が欠如することは、有効に機能し得
なくなる。有効な発現ベクターの有用であるが必ずしも
必要でない要素は、マーカーコード配列であり、即ち容
易に細胞を固定し得る蛋白質を含有する細胞の表現型特
性(たとえばテトラサイクリン耐性)をもたらすような蛋
白質をコードする配列である。要するに、「発現ベクタ
ー」には機能的定義が与えられ、特定の含有ＤＮＡコー
ドを発現し得る全てのＤＮＡ配列がこの用語に包含さ
れ、同様に特定の配列に適用される。現在この種のベク
ターはしばしばプラスミドの形態であるので、「プラス
ミド」と「発現ベクター」とはしばしば互換的に使用され
る。然しながら、本発明は均等な機能を有し且つ時と共
に当業界で公知となり得るような他の形態の発現ベクタ
ーをも包含することを意図する。
【００３２】「組換宿主細胞」という用語は、組換ＤＮＡ
技術を用いて作成されたベクターにより形質転換された
細胞を意味する。本明細書に定義したように、組換宿主
細胞により産生される抗体又はその改変物(modificatio
n)は、この形態転換のため未形質転換宿主で産生される
ような少量でなく、より一般的には検出量以下のもので
ない。
技術を用いて作成されたベクターにより形質転換された
細胞を意味する。本明細書に定義したように、組換宿主
細胞により産生される抗体又はその改変物(modificatio
n)は、この形態転換のため未形質転換宿主で産生される
ような少量でなく、より一般的には検出量以下のもので
ない。
【００３３】組換宿主から抗体を単離する方法の説明に
於いて、「細胞」及び「細胞培養物」という用語は、特記し
ない限り抗体の起源を示すために互換的に使用される。
換言すれば、「細胞」からの抗体の回収は、遠心分離され
た全細胞からの回収又は培地と懸濁細胞との両者を含有
する細胞培養物からの回収のいずれをも意味する。
於いて、「細胞」及び「細胞培養物」という用語は、特記し
ない限り抗体の起源を示すために互換的に使用される。
換言すれば、「細胞」からの抗体の回収は、遠心分離され
た全細胞からの回収又は培地と懸濁細胞との両者を含有
する細胞培養物からの回収のいずれをも意味する。
【００３４】Ｂ．宿主細胞培養物及びベクター 本明細書中に開示したベクター及び方法は、広範囲の原
核生物及び真核生物に亘る宿主細胞に使用するのに適し
ている。
核生物及び真核生物に亘る宿主細胞に使用するのに適し
ている。
【００３５】一般的には勿論、本発明に有用なベクター
を作成する際、ＤＮＡ配列をクローン化(クローニング)
するには原核生物が好適である。例えばＥ．coli Ｋ１
２菌株２９４(ＡＴＣＣ Ｎo．３１４４６)が特に有用
である。使用し得るその他の微生物菌株はＥ．coli菌
株、例えばＥ．coliＢ及びＥ．coliＸ１７７６(ＡＴＣ
Ｃ Ｎo．３１５３７)を包含する。これらの例は、勿論
例示であって限定を意味するものでない。
を作成する際、ＤＮＡ配列をクローン化(クローニング)
するには原核生物が好適である。例えばＥ．coli Ｋ１
２菌株２９４(ＡＴＣＣ Ｎo．３１４４６)が特に有用
である。使用し得るその他の微生物菌株はＥ．coli菌
株、例えばＥ．coliＢ及びＥ．coliＸ１７７６(ＡＴＣ
Ｃ Ｎo．３１５３７)を包含する。これらの例は、勿論
例示であって限定を意味するものでない。
【００３６】発現用にも原核生物を使用することができ
る。上記の菌株並びにＥ．coli Ｗ３１１０(Ｆ-,λ-,
原始栄養性(prototrophic)、ＡＴＣＣ Ｎo．２７３２
５)、桿菌例えばＢacillus subtilus、及び他の腸内細
菌例えばＳalmonella typhimurium又はＳerratia marce
sans及び各種のＰscudomonas種を使用することができ
る。
る。上記の菌株並びにＥ．coli Ｗ３１１０(Ｆ-,λ-,
原始栄養性(prototrophic)、ＡＴＣＣ Ｎo．２７３２
５)、桿菌例えばＢacillus subtilus、及び他の腸内細
菌例えばＳalmonella typhimurium又はＳerratia marce
sans及び各種のＰscudomonas種を使用することができ
る。
【００３７】一般に、レプリコン及び制御配列を含有し
宿主細胞に適合性の種由来のプラスミドベクターを、こ
れら宿主と関連して使用する。通常、ベクターは複製部
位並びに形質転換細胞に表現型選択を与え得るマーカー
配列を有する。例えばＥ．coliは、典型的にはpＢＲ３
２２即ちＥ．coli種から得られるプラスミド(Ｂolivare
t al．,Ｇene２:９５(１９７７))を用いて形質転換され
る。pＢＲ３２２はアンピシリン耐性及びテトラサイク
リン耐性遺伝子を有し、従って形質転換細胞を同定する
ための便利な手段を与える。pＢＲ３２２プラスミド又
はその他の微生物プラスミドは、又、微生物がそれ自身
の蛋白質を発現するように使用し得るプロモーターを含
有し又は含有するよう改変されなければならない。組換
ＤＮＡの作成に最も一般的に使用されるプロモーター
は、β−ラクタマーゼ(ペニシリナーゼ)及び乳糖プロモ
ーター系(Ｃhang et al．,Ｎature．２７５:６１５(１
９７８);Ｉtakura et al．,Ｓcience,１９８:１０５６
(１９７７);Ｇoeddel et al．,Ｎature,２８１:５４４
(１９７９))並びにトリプトファン(trp)プロモーター系
(Ｇoeddel et al．,Ｎucleic Ａcids Ｒes．,８:４０５
７(１９８０);ＥＰＯ出願公開第００３６７７６号)を包
含する。これらが特に一般的に使用されるが、他の微生
物プロモーターも見出され且つ利用されており、これら
ヌクレオチド配列に関する詳細が公開されており、当業
者はこれらをプラスミドベクターと機能的に結合させる
ことができる(Ｓiebenlist et al．,Ｃell,２０:２６９
(１９８０))。
宿主細胞に適合性の種由来のプラスミドベクターを、こ
れら宿主と関連して使用する。通常、ベクターは複製部
位並びに形質転換細胞に表現型選択を与え得るマーカー
配列を有する。例えばＥ．coliは、典型的にはpＢＲ３
２２即ちＥ．coli種から得られるプラスミド(Ｂolivare
t al．,Ｇene２:９５(１９７７))を用いて形質転換され
る。pＢＲ３２２はアンピシリン耐性及びテトラサイク
リン耐性遺伝子を有し、従って形質転換細胞を同定する
ための便利な手段を与える。pＢＲ３２２プラスミド又
はその他の微生物プラスミドは、又、微生物がそれ自身
の蛋白質を発現するように使用し得るプロモーターを含
有し又は含有するよう改変されなければならない。組換
ＤＮＡの作成に最も一般的に使用されるプロモーター
は、β−ラクタマーゼ(ペニシリナーゼ)及び乳糖プロモ
ーター系(Ｃhang et al．,Ｎature．２７５:６１５(１
９７８);Ｉtakura et al．,Ｓcience,１９８:１０５６
(１９７７);Ｇoeddel et al．,Ｎature,２８１:５４４
(１９７９))並びにトリプトファン(trp)プロモーター系
(Ｇoeddel et al．,Ｎucleic Ａcids Ｒes．,８:４０５
７(１９８０);ＥＰＯ出願公開第００３６７７６号)を包
含する。これらが特に一般的に使用されるが、他の微生
物プロモーターも見出され且つ利用されており、これら
ヌクレオチド配列に関する詳細が公開されており、当業
者はこれらをプラスミドベクターと機能的に結合させる
ことができる(Ｓiebenlist et al．,Ｃell,２０:２６９
(１９８０))。
【００３８】原核生物の他に、酵母培養物のような真核
微生物も使用することができる。Ｓaccharomyces cerev
isiae即ち一般的なパン酵母が真核微生物として最も一
般的に使用されるが、他の多くの菌株も一般的に使用し
得る。Ｓaccharomycesに於ける発現については例えばプ
ラスミドＹＲp７(Ｓtinchcomb et al．,Ｎature,２８
２:３９(１９７９);Ｋingsman et al．,Ｇene,７:１４
１(１９７９);Ｔschemperet al．, Ｇene,１０:１５７
(１９８０))が一般的に使用される。このプラスミドは
既にトリプトファン中で増殖する能力を欠如した酵母の
突然変異菌株、例えばＡＴＣＣ Ｎo．４４０７６即ち
ＰＥＰ４−１(Ｊones,Ｇenetics,８５:１２(１９７７))
に対し選択マーカーを与えるtrp１遺伝子を含有する。
酵母宿主細胞ゲノムの特性としてtrp１欠陥(lesion)が
存在するため、トリプトファンの不在下での増殖による
形質転換の検出用に有効な環境が得られる。
微生物も使用することができる。Ｓaccharomyces cerev
isiae即ち一般的なパン酵母が真核微生物として最も一
般的に使用されるが、他の多くの菌株も一般的に使用し
得る。Ｓaccharomycesに於ける発現については例えばプ
ラスミドＹＲp７(Ｓtinchcomb et al．,Ｎature,２８
２:３９(１９７９);Ｋingsman et al．,Ｇene,７:１４
１(１９７９);Ｔschemperet al．, Ｇene,１０:１５７
(１９８０))が一般的に使用される。このプラスミドは
既にトリプトファン中で増殖する能力を欠如した酵母の
突然変異菌株、例えばＡＴＣＣ Ｎo．４４０７６即ち
ＰＥＰ４−１(Ｊones,Ｇenetics,８５:１２(１９７７))
に対し選択マーカーを与えるtrp１遺伝子を含有する。
酵母宿主細胞ゲノムの特性としてtrp１欠陥(lesion)が
存在するため、トリプトファンの不在下での増殖による
形質転換の検出用に有効な環境が得られる。
【００３９】酵母ベクターに於ける適当なプロモーター
配列は３−ホスホグリセレートキナーゼ(Ｈitzeman et
al．,Ｊ．Ｂiol．Ｃhem．,２５５:２０７３(１９８０))
又はその他の糖分解酵素(Ｈess et al．,Ｊ．Ａdv．Ｅn
zymc Ｒeg．,７:１４９(１９６８);Ｈolland et al．,
Ｂiochemistry,１７:４９００(１９７８))例えばエノラ
ーゼ、グリセルアルデヒド−３−ホスフェートデヒドロ
ゲナーゼ、ヘキソキナーゼ、ピルベートデカルボキシラ
ーゼ、ホスホフルクトキナーゼ、グルコース−６−ホス
フェートイソメラーゼ、３−ホスホグリセレートムター
ゼ、ピルベートキナーゼ、トリオースホスフェートイソ
メラーゼ、ホスホグルコースイソメラーゼ及びグルコキ
ナーゼに対するプロモーターを包含する。適する発現プ
ラスミドを作成する際、これら遺伝子に関連する停止配
列も、mＲＮＡのポリアデニル化及び停止を行なうよう
に発現させたり配列の発現ベクター３'中へ結合させ
る。増殖条件により制御される転写の付加的利点を更に
有する他のプロモーターは、アルコールデヒドロゲナー
ゼ２、イソチトクロームＣ、酸ホスファターゼ、窒素代
謝に関連する分解酵素並びに上記のグリセルアルデヒド
−３−ホスフェートデヒドロゲナーゼ及びマルトースと
ガラクトースとの利用に関する酵素(Ｈolland,上記)に
対するプロモーター領域である。酵母適合性のプロモー
ターと複製のオリジンと停止配列とを有するプラスミド
ベクターが適している。
配列は３−ホスホグリセレートキナーゼ(Ｈitzeman et
al．,Ｊ．Ｂiol．Ｃhem．,２５５:２０７３(１９８０))
又はその他の糖分解酵素(Ｈess et al．,Ｊ．Ａdv．Ｅn
zymc Ｒeg．,７:１４９(１９６８);Ｈolland et al．,
Ｂiochemistry,１７:４９００(１９７８))例えばエノラ
ーゼ、グリセルアルデヒド−３−ホスフェートデヒドロ
ゲナーゼ、ヘキソキナーゼ、ピルベートデカルボキシラ
ーゼ、ホスホフルクトキナーゼ、グルコース−６−ホス
フェートイソメラーゼ、３−ホスホグリセレートムター
ゼ、ピルベートキナーゼ、トリオースホスフェートイソ
メラーゼ、ホスホグルコースイソメラーゼ及びグルコキ
ナーゼに対するプロモーターを包含する。適する発現プ
ラスミドを作成する際、これら遺伝子に関連する停止配
列も、mＲＮＡのポリアデニル化及び停止を行なうよう
に発現させたり配列の発現ベクター３'中へ結合させ
る。増殖条件により制御される転写の付加的利点を更に
有する他のプロモーターは、アルコールデヒドロゲナー
ゼ２、イソチトクロームＣ、酸ホスファターゼ、窒素代
謝に関連する分解酵素並びに上記のグリセルアルデヒド
−３−ホスフェートデヒドロゲナーゼ及びマルトースと
ガラクトースとの利用に関する酵素(Ｈolland,上記)に
対するプロモーター領域である。酵母適合性のプロモー
ターと複製のオリジンと停止配列とを有するプラスミド
ベクターが適している。
【００４０】微生物の他に、多細胞生物由来細胞の培養
物も宿主として使用することができる。原則として、任
意のこの種の細胞培養物は、脊椎動物由来であっても、
或いは無脊椎動物の培養物であっても使用可能である。
然しながら、最も興味があるものは脊椎動物細胞であ
り、脊椎動物細胞の培養(組織培養)による増殖が、近年
日常の手法となった(Ｔissue Ｃulture, Ａcademic Ｐr
ess, Ｋruse and Ｐatterson編(１９７３))。この種の
有用な宿主細胞系の例は、ＶＥＲＯ細胞及びＨeＬa細
胞、チャイニーズハムスター卵巣(ＣＨＯ)細胞系並びに
Ｗ１３８,ＢＨＫ,ＣＯＳ−７及びＭＤＣＫ細胞系であ
る。この種の細胞に対する発現ベクターは一般に、(必
要に応じ)複製のオリジン、発現すべき遺伝子の前方に
位置するプロモーター並びに任意の必要なリポソーム結
合部位、ＲＮＡスプライス部位、ポリアデニル化部位及
び転写停止配列を含む。
物も宿主として使用することができる。原則として、任
意のこの種の細胞培養物は、脊椎動物由来であっても、
或いは無脊椎動物の培養物であっても使用可能である。
然しながら、最も興味があるものは脊椎動物細胞であ
り、脊椎動物細胞の培養(組織培養)による増殖が、近年
日常の手法となった(Ｔissue Ｃulture, Ａcademic Ｐr
ess, Ｋruse and Ｐatterson編(１９７３))。この種の
有用な宿主細胞系の例は、ＶＥＲＯ細胞及びＨeＬa細
胞、チャイニーズハムスター卵巣(ＣＨＯ)細胞系並びに
Ｗ１３８,ＢＨＫ,ＣＯＳ−７及びＭＤＣＫ細胞系であ
る。この種の細胞に対する発現ベクターは一般に、(必
要に応じ)複製のオリジン、発現すべき遺伝子の前方に
位置するプロモーター並びに任意の必要なリポソーム結
合部位、ＲＮＡスプライス部位、ポリアデニル化部位及
び転写停止配列を含む。
【００４１】哺乳動物細胞に於いて使用するには、発現
ベクターに対する制御機能がしばしばウィルス性材料に
より与えられる。例えば一般的に使用されるプロモータ
ーはポリオーマ、アデノウィルス２及び特にしばしばサ
ルウィルス４０(ＳＶ４０)から得られる。ＳＶ４０ウィ
ルスの初期及び後期プロモーターが特に有用である。何
故なら、これら両者は複製のＳＶ４０ウィルスオリジン
をも含有する断片としてウィルスから容易に得られるか
らである。(Ｆiers et al．,Ｎature,２７３:１１３(１
９７８),これを引用して本明細書に包含する)。より小
さい又はより大きいＳＶ４０断片も使用し得るが、但し
ＨindＩＩＩから複製のウィルスオリジン内に存在する
ＢglＩ部位まで延びる約２５０bp配列が含まれることが
必要である。更に一般に所望の遺伝子配列に関連するプ
ロモーター又は制御配列を使用することもでき、且つ使
用するのがしばしば望ましい。但し、この種の制御配列
は、宿主細胞系に対し適合性であるものとする。
ベクターに対する制御機能がしばしばウィルス性材料に
より与えられる。例えば一般的に使用されるプロモータ
ーはポリオーマ、アデノウィルス２及び特にしばしばサ
ルウィルス４０(ＳＶ４０)から得られる。ＳＶ４０ウィ
ルスの初期及び後期プロモーターが特に有用である。何
故なら、これら両者は複製のＳＶ４０ウィルスオリジン
をも含有する断片としてウィルスから容易に得られるか
らである。(Ｆiers et al．,Ｎature,２７３:１１３(１
９７８),これを引用して本明細書に包含する)。より小
さい又はより大きいＳＶ４０断片も使用し得るが、但し
ＨindＩＩＩから複製のウィルスオリジン内に存在する
ＢglＩ部位まで延びる約２５０bp配列が含まれることが
必要である。更に一般に所望の遺伝子配列に関連するプ
ロモーター又は制御配列を使用することもでき、且つ使
用するのがしばしば望ましい。但し、この種の制御配列
は、宿主細胞系に対し適合性であるものとする。
【００４２】複製のオリジンは、例えばＳＶ４０又はそ
の他のウィルス(例えばポリオーマ、アデノ、ＶＳＶ、
ＢＰＶ等)源から得られるような外来オリジンを含むよ
うにベクターを作成して供給するか、或いは宿主細胞の
染色体複製メカニズムにより供給することができる。ベ
クターが宿主細胞の染色体中に組み込まれれば、これで
しばしば充分である。
の他のウィルス(例えばポリオーマ、アデノ、ＶＳＶ、
ＢＰＶ等)源から得られるような外来オリジンを含むよ
うにベクターを作成して供給するか、或いは宿主細胞の
染色体複製メカニズムにより供給することができる。ベ
クターが宿主細胞の染色体中に組み込まれれば、これで
しばしば充分である。
【００４３】本発明を好適具体例につき本明細書中に説
明するが、ここに記載したような宿主細胞、ベクター及
び発現系のみに限定されるものでないことが了解されよ
う。
明するが、ここに記載したような宿主細胞、ベクター及
び発現系のみに限定されるものでないことが了解されよ
う。
【００４４】Ｃ．使用方法 Ｃ．１．形質転換: 強固な細胞壁バリヤーを持たない細胞を宿主細胞として
使用する場合、トリンスフェクションはＧraham及びＶa
n der ＥbによりＶirology,５２:５４６(１９７８)に記
載された燐酸カルシウム沈澱法により行なわれる。然し
ながら、例えば核注入又はプロトプラスト融合によるよ
うな細胞中へのＤＮＡの他の導入法も使用することがで
きる。
使用する場合、トリンスフェクションはＧraham及びＶa
n der ＥbによりＶirology,５２:５４６(１９７８)に記
載された燐酸カルシウム沈澱法により行なわれる。然し
ながら、例えば核注入又はプロトプラスト融合によるよ
うな細胞中へのＤＮＡの他の導入法も使用することがで
きる。
【００４５】原核細胞又は実質の細胞壁構造を含有する
細胞を使用する場合、好適なトランスフェクション方法
はＦ．Ｎ．Ｃohen et al．,によりＰroc．Ｎatl．Ａca
d．Ｓci．,ＵＳＡ,６９:２１１０(１９７２)に記載され
たように塩化カルシウムを使用するカルシウム処理であ
る。
細胞を使用する場合、好適なトランスフェクション方法
はＦ．Ｎ．Ｃohen et al．,によりＰroc．Ｎatl．Ａca
d．Ｓci．,ＵＳＡ,６９:２１１０(１９７２)に記載され
たように塩化カルシウムを使用するカルシウム処理であ
る。
【００４６】Ｃ．２．ベクターの作成 所望のコード配列と制御配列とを含有する適するベクタ
ーの作成は、標準的結合技術を使用する。単離されたプ
ラスミド又はＤＮＡ断片を開裂し、適当に処理し且つ所
望の形態に再結合して、所要のプラスミドを生成する。
使用する方法は、ＤＮＡ源又は使用する宿主に依存しな
い。
ーの作成は、標準的結合技術を使用する。単離されたプ
ラスミド又はＤＮＡ断片を開裂し、適当に処理し且つ所
望の形態に再結合して、所要のプラスミドを生成する。
使用する方法は、ＤＮＡ源又は使用する宿主に依存しな
い。
【００４７】開裂は、適当な緩衝液中で１種又はそれ以
上の制限酵素により処理して行なわれる。一般に、約１
μgのプラスミド又はＤＮＡ断片を約２０μlの緩衝溶液
中で約１ユニットの酵素と共に使用する(特定制限酵素
に対する適当な緩衝液及び基質の量は製造業者により特
定されている)。３７℃にて約１時間インキュベーショ
ンする。培養後、フェノール及びクロロホルムでの抽出
により蛋白質を除去し、且つ核酸をエタノールでの沈澱
により水性フラクションから回収する。
上の制限酵素により処理して行なわれる。一般に、約１
μgのプラスミド又はＤＮＡ断片を約２０μlの緩衝溶液
中で約１ユニットの酵素と共に使用する(特定制限酵素
に対する適当な緩衝液及び基質の量は製造業者により特
定されている)。３７℃にて約１時間インキュベーショ
ンする。培養後、フェノール及びクロロホルムでの抽出
により蛋白質を除去し、且つ核酸をエタノールでの沈澱
により水性フラクションから回収する。
【００４８】平滑末端が必要ならば、この調製物を１０
ユニットのＥ．coliＤＮＡポリメラーゼＩ(Ｋlenow)と
共に１５℃にて１５分間処理し、フェノール−クロロホ
ルム抽出し、エタノール沈澱する。
ユニットのＥ．coliＤＮＡポリメラーゼＩ(Ｋlenow)と
共に１５℃にて１５分間処理し、フェノール−クロロホ
ルム抽出し、エタノール沈澱する。
【００４９】開裂した断片のサイズ分画はＤ．Ｇoeddel
et al．によりＮucleic Ａcids Ｒes．,８:４０５７
(１９８０)(引用して本明細書に包含する)に記載された
６％ポリアクリルアミドゲルを用いて行なわれる。
et al．によりＮucleic Ａcids Ｒes．,８:４０５７
(１９８０)(引用して本明細書に包含する)に記載された
６％ポリアクリルアミドゲルを用いて行なわれる。
【００５０】結合には、正確な整合性を与えるために適
当に末端処理した所望の成分のほぼ等モル量を０．５μ
gのＤＮＡ当り約１０ユニットのＴ４ＤＮＡリガーゼで
処理する。(開裂したベクターを成分として使用する場
合、細菌のアルカリ性ホスファターゼで予備処理するこ
とにより開裂ベクターの再結合を防止するのが有用であ
る。)
当に末端処理した所望の成分のほぼ等モル量を０．５μ
gのＤＮＡ当り約１０ユニットのＴ４ＤＮＡリガーゼで
処理する。(開裂したベクターを成分として使用する場
合、細菌のアルカリ性ホスファターゼで予備処理するこ
とにより開裂ベクターの再結合を防止するのが有用であ
る。)
【００５１】下記の実施例に於いて、プラスミド作成に
対する正確な結合は、Ｅ．coli Ｋ１２菌株２９４(Ａ
ＴＣＣ Ｎo．３１４４６)を結合混合物で形質転換する
ことにより確認される。成功した形質転換体は、プラス
ミドの作成様式に応じてアンピシリン耐性又はテトラサ
イクリン耐性により選択した。次いで、形質転換体から
のプラスミドを調製し、制限分析し及び／又はＭessing
等の方法(Ｎucleic Ａcids Ｒes．,９:３０９(１９８
１))又はＭaxam et al．の方法(Ｍethods in Ｅnzymolo
gy,６５:４９９(１９８０))によって配列決定した。
対する正確な結合は、Ｅ．coli Ｋ１２菌株２９４(Ａ
ＴＣＣ Ｎo．３１４４６)を結合混合物で形質転換する
ことにより確認される。成功した形質転換体は、プラス
ミドの作成様式に応じてアンピシリン耐性又はテトラサ
イクリン耐性により選択した。次いで、形質転換体から
のプラスミドを調製し、制限分析し及び／又はＭessing
等の方法(Ｎucleic Ａcids Ｒes．,９:３０９(１９８
１))又はＭaxam et al．の方法(Ｍethods in Ｅnzymolo
gy,６５:４９９(１９８０))によって配列決定した。
【００５２】Ｄ．方法の概略 Ｄ．１．哺乳動物抗体 本発明の一部を構成し且つその方法により製造される第
１のタイプの抗体は、「哺乳動物抗体」であり、Ｈ鎖とＬ
鎖とが成熟哺乳動物Ｂリンパ球によりin situで、或い
はハイブリドーマ培養物の部分として永久株化細胞と融
合した場合に産生される抗体のアミノ酸配列に類似する
ものである。要するに、これらの抗体は次のようにして
産生される。
１のタイプの抗体は、「哺乳動物抗体」であり、Ｈ鎖とＬ
鎖とが成熟哺乳動物Ｂリンパ球によりin situで、或い
はハイブリドーマ培養物の部分として永久株化細胞と融
合した場合に産生される抗体のアミノ酸配列に類似する
ものである。要するに、これらの抗体は次のようにして
産生される。
【００５３】Ｈ鎖もしくはＬ鎖をコードするメッセンジ
ャーＲＮＡを適当な起源、即ち成熟Ｂ細胞又はハイブリ
ドーマ培養物から単離する。その際ＲＮＡ単離の標準技
術及びポリ−Ａ mＲＮＡを分離するためのオリゴ−dＴ
セルロースクロマトグラフィーを使用する。更にポリ−
Ａ mＲＮＡを分画して、場合により所望抗体のＬ鎖も
しくはＨ鎖に於けるアミノ酸配列をコードするのに充分
なサイズの配列を得る。
ャーＲＮＡを適当な起源、即ち成熟Ｂ細胞又はハイブリ
ドーマ培養物から単離する。その際ＲＮＡ単離の標準技
術及びポリ−Ａ mＲＮＡを分離するためのオリゴ−dＴ
セルロースクロマトグラフィーを使用する。更にポリ−
Ａ mＲＮＡを分画して、場合により所望抗体のＬ鎖も
しくはＨ鎖に於けるアミノ酸配列をコードするのに充分
なサイズの配列を得る。
【００５４】次いで、所望のcＤＮＡに特徴的である適
当なプライマー好ましくは核酸配列を用いて、mＲＮＡ
の混合物からcＤＮＡライブラリーを作成する。配列が
公知であれば、この種のプライマーを抗体のアミノ酸配
列に基いて推定し且つ合成することができる。或いは、
所望の抗体を産生する細胞系からの未分画ポリ−Ａ m
ＲＮＡのcＤＮＡ又はポリ−dＴを使用することもでき
る。得られたcＤＮＡを必要に応じポリアクリルアミド
ゲルでサイズ分画し、次いで適当な制限酵素(例えばＰs
tＩ)により開裂し且つdＧ残部で延長したpＢＲ３２２又
はその他の適当なクローニングベクターとアニールする
ために例えばdＣ残基で延長する。勿論、他のテイル及
び他のクローニングベクター残部を用いてcＤＮＡ含有
クローニングベクターを形成するその他の手段も使用し
得るが、前記のものが標準的且つ好適な選択である。適
する宿主細胞菌株、典型的にはＥ．coliをアニールした
クローニングベクターで形質転換し、得られた形質転換
体を例えばテトラサイクリン耐性により、或いはクロー
ニングベクタープラスミド上に存在する他の表現型特性
により同定する。
当なプライマー好ましくは核酸配列を用いて、mＲＮＡ
の混合物からcＤＮＡライブラリーを作成する。配列が
公知であれば、この種のプライマーを抗体のアミノ酸配
列に基いて推定し且つ合成することができる。或いは、
所望の抗体を産生する細胞系からの未分画ポリ−Ａ m
ＲＮＡのcＤＮＡ又はポリ−dＴを使用することもでき
る。得られたcＤＮＡを必要に応じポリアクリルアミド
ゲルでサイズ分画し、次いで適当な制限酵素(例えばＰs
tＩ)により開裂し且つdＧ残部で延長したpＢＲ３２２又
はその他の適当なクローニングベクターとアニールする
ために例えばdＣ残基で延長する。勿論、他のテイル及
び他のクローニングベクター残部を用いてcＤＮＡ含有
クローニングベクターを形成するその他の手段も使用し
得るが、前記のものが標準的且つ好適な選択である。適
する宿主細胞菌株、典型的にはＥ．coliをアニールした
クローニングベクターで形質転換し、得られた形質転換
体を例えばテトラサイクリン耐性により、或いはクロー
ニングベクタープラスミド上に存在する他の表現型特性
により同定する。
【００５５】成功した形質転換体を釣り上げて、マイク
ロタイター皿又はその他の支持体に移し、更に増殖及び
保存する。次いで、これら増殖する培養物のニトロセル
ロースフィルターのプリント物(imprint)をcＤＮＡ中の
所望配列に相補的であることが知られた塩基を含有する
適当なヌクレオチド配列でプローブする。数種のプロー
ブを使用することができ、好ましくはＡＴＰ32でキナー
ゼ処理することにより標識した合成単一鎖ＤＮＡ配列を
使用する。ニトロセルロースフィルターに固定された細
胞を溶菌し、ＤＮＡを変性し、固定した後にキナーゼ処
理したプローブと反応させる。うまくハイブリダイズす
るクローンをフォトプレートへ接触させて検出し、プラ
スミドを増殖するコロニーから単離し、遺伝子の所望部
分が存在することを証明するために当業界で知られた手
段により配列決定する。
ロタイター皿又はその他の支持体に移し、更に増殖及び
保存する。次いで、これら増殖する培養物のニトロセル
ロースフィルターのプリント物(imprint)をcＤＮＡ中の
所望配列に相補的であることが知られた塩基を含有する
適当なヌクレオチド配列でプローブする。数種のプロー
ブを使用することができ、好ましくはＡＴＰ32でキナー
ゼ処理することにより標識した合成単一鎖ＤＮＡ配列を
使用する。ニトロセルロースフィルターに固定された細
胞を溶菌し、ＤＮＡを変性し、固定した後にキナーゼ処
理したプローブと反応させる。うまくハイブリダイズす
るクローンをフォトプレートへ接触させて検出し、プラ
スミドを増殖するコロニーから単離し、遺伝子の所望部
分が存在することを証明するために当業界で知られた手
段により配列決定する。
【００５６】所望の遺伝子断片を切断処理して、適当な
発現ベクター中へ挿入した場合の制御セグメントとの適
当な解読枠を確保する。典型的には、ヌクレオチドを
５'末端へ付加して開始信号と適当に位置する制限エン
ドヌクレアーゼ部位とを含むようにする。
発現ベクター中へ挿入した場合の制御セグメントとの適
当な解読枠を確保する。典型的には、ヌクレオチドを
５'末端へ付加して開始信号と適当に位置する制限エン
ドヌクレアーゼ部位とを含むようにする。
【００５７】次いで、適当に処理した遺伝子配列を、遺
伝子と共に解読枠にあるプロモーターを含有し且つ使用
する宿主に対し適合性であるベクター中に配置する。例
えば米国特許出願第３０７４７３号、第２９１８９２号
及び第３０５６５７号(ＥＰＯ特許公開第００３６７７
６号、第００４８９７０号及び第００５１８７３号)明
細書に記載されたような多数のプラスミドは、適当なプ
ロモーターと制御配列とリボソーム結合部位と転写停止
部位と便利なマーカーとを既に含有する。
伝子と共に解読枠にあるプロモーターを含有し且つ使用
する宿主に対し適合性であるベクター中に配置する。例
えば米国特許出願第３０７４７３号、第２９１８９２号
及び第３０５６５７号(ＥＰＯ特許公開第００３６７７
６号、第００４８９７０号及び第００５１８７３号)明
細書に記載されたような多数のプラスミドは、適当なプ
ロモーターと制御配列とリボソーム結合部位と転写停止
部位と便利なマーカーとを既に含有する。
【００５８】本発明に於いては、Ｌ鎖をコードする遺伝
子及びＨ鎖をコードする遺伝子を上記の手法により別々
に回収する。即ち、これらは、それぞれ適当なプロモー
ター及び翻訳制御の下にある限り、別々の発現プラスミ
ド中へ挿入することができ、或いは一緒に同じプラスミ
ドに挿入することができる。
子及びＨ鎖をコードする遺伝子を上記の手法により別々
に回収する。即ち、これらは、それぞれ適当なプロモー
ター及び翻訳制御の下にある限り、別々の発現プラスミ
ド中へ挿入することができ、或いは一緒に同じプラスミ
ドに挿入することができる。
【００５９】次いで、上記のように作成した発現ベクタ
ーを使用して適当な細胞を形質転換する。Ｌ鎖及びＨ鎖
を同一種又は異なる種の別々の細胞培養物中に形質転換
することができ、Ｌ鎖及びＨ鎖に対する別々のプラスミ
ドを使用して単一の細胞培養物を同時形質転換すること
ができ、或いは両遺伝子を含有し且つＬ鎖とＨ鎖との両
者に対する遺伝子を発現し得る単一の発現プラスミドを
単一の細胞培養物に形質転換することができる。
ーを使用して適当な細胞を形質転換する。Ｌ鎖及びＨ鎖
を同一種又は異なる種の別々の細胞培養物中に形質転換
することができ、Ｌ鎖及びＨ鎖に対する別々のプラスミ
ドを使用して単一の細胞培養物を同時形質転換すること
ができ、或いは両遺伝子を含有し且つＬ鎖とＨ鎖との両
者に対する遺伝子を発現し得る単一の発現プラスミドを
単一の細胞培養物に形質転換することができる。
【００６０】上記３つの選択のどれを選択するかに関係
なく、細胞を所望蛋白質の産生に適する条件下で増殖さ
せる。この種の条件は、主として所望蛋白質の性質では
なく、発現ベクター中に使用されるプロモーター及び制
御系のタイプにより支配される。次いで、このように産
生された蛋白質を当業界で公知の方法により細胞培養物
から回収するが、方法の選択は必然的に蛋白質の発現さ
れた形態に依存する。例えばＥ．coliで発現された成熟
異種蛋白質を不溶性粒子として細胞内に沈着させるのが
一般的であり、これは回収を可能にするための細胞の溶
菌と変性剤(denaturant)中への可溶化とを必要とする。
他方、酵母及び細菌の菌株中の適切な合成条件下の蛋白
質は培地中(酵母及びク゛ラム陽性菌)又はペリプラズム空
間(グラム陰性菌)へ分泌することができ、それほど激し
くない方法により回収することができる。一般に、宿主
としての組織培養細胞は異種蛋白質の便利な回収を可能
にすると思われる。
なく、細胞を所望蛋白質の産生に適する条件下で増殖さ
せる。この種の条件は、主として所望蛋白質の性質では
なく、発現ベクター中に使用されるプロモーター及び制
御系のタイプにより支配される。次いで、このように産
生された蛋白質を当業界で公知の方法により細胞培養物
から回収するが、方法の選択は必然的に蛋白質の発現さ
れた形態に依存する。例えばＥ．coliで発現された成熟
異種蛋白質を不溶性粒子として細胞内に沈着させるのが
一般的であり、これは回収を可能にするための細胞の溶
菌と変性剤(denaturant)中への可溶化とを必要とする。
他方、酵母及び細菌の菌株中の適切な合成条件下の蛋白
質は培地中(酵母及びク゛ラム陽性菌)又はペリプラズム空
間(グラム陰性菌)へ分泌することができ、それほど激し
くない方法により回収することができる。一般に、宿主
としての組織培養細胞は異種蛋白質の便利な回収を可能
にすると思われる。
【００６１】Ｈ鎖とＬ鎖とを同一宿主中で同時発現させ
る場合、単離法は再編成抗体を回収するように設計され
る。これは下記するようにin vitroで行なうことがで
き、或いは細胞質の還元環境からＩgＧ鎖を分泌する微
生物中in vivoで行なうことも可能である。より詳細な
説明は下記Ｄ．２．に示す。
る場合、単離法は再編成抗体を回収するように設計され
る。これは下記するようにin vitroで行なうことがで
き、或いは細胞質の還元環境からＩgＧ鎖を分泌する微
生物中in vivoで行なうことも可能である。より詳細な
説明は下記Ｄ．２．に示す。
【００６２】Ｄ．２．鎖組換技術 Ｈ鎖及びＬ鎖又はその部分を互いに分離して産生する本
発明の方法の能力は、独特且つ先例のない免疫グロブリ
ン、Ｆab領域及び単一価の抗体の集合体を得る機会を与
える。このような製造は、単離した鎖を再組立てする技
術の使用を必要とする。この種の手段は当業界で公知で
あり、従ってこれらにつきここで再検討するのが適当で
ある。
発明の方法の能力は、独特且つ先例のない免疫グロブリ
ン、Ｆab領域及び単一価の抗体の集合体を得る機会を与
える。このような製造は、単離した鎖を再組立てする技
術の使用を必要とする。この種の手段は当業界で公知で
あり、従ってこれらにつきここで再検討するのが適当で
ある。
【００６３】単一鎖のジスルフィド結合を含有する蛋白
質を還元し且つ再酸化して天然構造及び活性を高収率で
再生させているが(Ｒ．Ｂ．Ｆreedman et al．,Ｅnzymo
logyof Ｐost Ｔranslational Ｍodification of Ｐrot
eins,１:１５７−２１２(１９８０)Ａcademic Ｐress
社、ＮＹ．)、ジスルフィド結合により結合されている
不連続ポリペプチド鎖より成る蛋白質は還元開裂の後に
in vitroで再編成するのが困難である。精巧な場合であ
るインシュリンは永年に亘り多くの実験的注目を集めて
おり、現在ではこれに関し工業的方法が確立されている
ほど効率的に再編成することができる(Ｒ．Ｅ．Ｃhance
et al．,Ｐeptides:第７回米国ペプチドシンポジウム
のＰroceedings(Ｄ．Ｈ．Ｒich及びＥ．Ｇross編)７２
１−７２８．Ｐierce Ｃhemical Ｃo．,Ｒockford,Ｉ
Ｌ．(１９８１))。
質を還元し且つ再酸化して天然構造及び活性を高収率で
再生させているが(Ｒ．Ｂ．Ｆreedman et al．,Ｅnzymo
logyof Ｐost Ｔranslational Ｍodification of Ｐrot
eins,１:１５７−２１２(１９８０)Ａcademic Ｐress
社、ＮＹ．)、ジスルフィド結合により結合されている
不連続ポリペプチド鎖より成る蛋白質は還元開裂の後に
in vitroで再編成するのが困難である。精巧な場合であ
るインシュリンは永年に亘り多くの実験的注目を集めて
おり、現在ではこれに関し工業的方法が確立されている
ほど効率的に再編成することができる(Ｒ．Ｅ．Ｃhance
et al．,Ｐeptides:第７回米国ペプチドシンポジウム
のＰroceedings(Ｄ．Ｈ．Ｒich及びＥ．Ｇross編)７２
１−７２８．Ｐierce Ｃhemical Ｃo．,Ｒockford,Ｉ
Ｌ．(１９８１))。
【００６４】免疫グロブリンは、インシュリンよりも困
難な問題を含むことが判明している。四元体は１５個も
しくはそれ以上のジスルフィド結合により分子内及び分
子間で安定化されている。鎖間ジスルフィドのみの開裂
により分解されたＨ鎖とＬ鎖とを再結合して、鎖間ジス
ルフィドを復帰させなくても抗体活性を再取することが
可能であった(Ｇ．Ｍ．Ｅdelman et al．,Ｐroc．Ｎat
l．Ａcad．Ｓci．,ＵＳＡ,５０:７５３(１９６３)）。
更に、蛋白質分解により生成される活性なＩgＧの断片
(約５０,０００ＭＷのＦab断片)をそれらの完全に還元
したＨ鎖成分とＬ鎖成分とに開裂させ、これらをかなり
効率的に再編成して活性抗体を与えることができる
(Ｅ．Ｈaber,Ｐroc．Ｎatl．Ａcad．Ｓci．,ＵＳＡ,５
２:１０９９(１９６４);Ｐ．Ｌ．Ｗhitney et al．,Ｐr
oc．Ｎatl．Ａcad．Ｓci．,ＵＳＡ,５３:５２４(１９６
５))。完全還元された天然ＩgＧから活性抗体を再編成
する試みは、恐らく還元鎖及び副産物又は中間物が再編
成過程に於いて不溶解性であるため、完全に不成功であ
った(Ｍ．Ｈ．Ｆreedman et al．,Ｊ．Ｂiol．Ｃhem．,
２４１:５２２５(１９６６))。然しながら、免疫グロブ
リンを完全還元の前にリジンのポリアデニル化によりラ
ンダムに改変すれば、分離される鎖は再酸化の際に抗原
結合性の活性を回収する能力を有する(上記)。
難な問題を含むことが判明している。四元体は１５個も
しくはそれ以上のジスルフィド結合により分子内及び分
子間で安定化されている。鎖間ジスルフィドのみの開裂
により分解されたＨ鎖とＬ鎖とを再結合して、鎖間ジス
ルフィドを復帰させなくても抗体活性を再取することが
可能であった(Ｇ．Ｍ．Ｅdelman et al．,Ｐroc．Ｎat
l．Ａcad．Ｓci．,ＵＳＡ,５０:７５３(１９６３)）。
更に、蛋白質分解により生成される活性なＩgＧの断片
(約５０,０００ＭＷのＦab断片)をそれらの完全に還元
したＨ鎖成分とＬ鎖成分とに開裂させ、これらをかなり
効率的に再編成して活性抗体を与えることができる
(Ｅ．Ｈaber,Ｐroc．Ｎatl．Ａcad．Ｓci．,ＵＳＡ,５
２:１０９９(１９６４);Ｐ．Ｌ．Ｗhitney et al．,Ｐr
oc．Ｎatl．Ａcad．Ｓci．,ＵＳＡ,５３:５２４(１９６
５))。完全還元された天然ＩgＧから活性抗体を再編成
する試みは、恐らく還元鎖及び副産物又は中間物が再編
成過程に於いて不溶解性であるため、完全に不成功であ
った(Ｍ．Ｈ．Ｆreedman et al．,Ｊ．Ｂiol．Ｃhem．,
２４１:５２２５(１９６６))。然しながら、免疫グロブ
リンを完全還元の前にリジンのポリアデニル化によりラ
ンダムに改変すれば、分離される鎖は再酸化の際に抗原
結合性の活性を回収する能力を有する(上記)。
【００６５】免疫グロブリンの再編成に対して特に適し
た方法は、現在では古典的となったインシュリン組換技
術から得られるものであり、ここでは出発物質を酸化ス
ルフィトリシス(Ｏxidative sulfitolysis)により調製
し、蛋白質に於ける全てのシステインのチオール不安定
性Ｓ−スルホン酸基を発生させ、ジスルフィドを非還元
的に破壊する(Ｃhance et al．,上記)。酸化スルフィ
トリシスは緩和なジスルフィド開裂反応であり(Ｇ．
Ｅ．Ｍeans et al．,Ｃhemical Ｍodificationof
Ｐroteins,Ｈolden−Ｄay,Ｓan Ｆrancisco(１９７
１))、これはしばしば還元より緩和であり、且つジスル
フィド再生成がチオール−ジスルフィド相互交換を介し
て生じ得る緩和な還元剤に露呈されるまで安定であるよ
うな誘導体を生成する。本発明に於いて、酸化スルフィ
トリシスにより生成されるＨ鎖及びＬ鎖のＳ−スルホネ
ートは、ジスルフィド結合生成を行なうために空気酸化
とチオール−ジスルフィド相互交換との両者を用いて再
編成された。一般的手順は、１９８２年１２月２２日付
で出願された米国特許出願第４５２１８７号(ＥＰＯ出
願第８３．３０７８４０．５号)明細書に詳細に示され
ており、これを参考のためここに引用して本明細書に包
含する。
た方法は、現在では古典的となったインシュリン組換技
術から得られるものであり、ここでは出発物質を酸化ス
ルフィトリシス(Ｏxidative sulfitolysis)により調製
し、蛋白質に於ける全てのシステインのチオール不安定
性Ｓ−スルホン酸基を発生させ、ジスルフィドを非還元
的に破壊する(Ｃhance et al．,上記)。酸化スルフィ
トリシスは緩和なジスルフィド開裂反応であり(Ｇ．
Ｅ．Ｍeans et al．,Ｃhemical Ｍodificationof
Ｐroteins,Ｈolden−Ｄay,Ｓan Ｆrancisco(１９７
１))、これはしばしば還元より緩和であり、且つジスル
フィド再生成がチオール−ジスルフィド相互交換を介し
て生じ得る緩和な還元剤に露呈されるまで安定であるよ
うな誘導体を生成する。本発明に於いて、酸化スルフィ
トリシスにより生成されるＨ鎖及びＬ鎖のＳ−スルホネ
ートは、ジスルフィド結合生成を行なうために空気酸化
とチオール−ジスルフィド相互交換との両者を用いて再
編成された。一般的手順は、１９８２年１２月２２日付
で出願された米国特許出願第４５２１８７号(ＥＰＯ出
願第８３．３０７８４０．５号)明細書に詳細に示され
ており、これを参考のためここに引用して本明細書に包
含する。
【００６６】Ｄ．３．組換技術により可能な変種 上記Ｄ．１及びＤ．２に記載した技術を用いて、哺乳動
物抗体の効率的産生を得るために用いた他の操作を全く
簡潔に変化させて、この基本的抗体型の多くの変種を産
生させることができる。これらの変種は組換技術の使用
に本質的であり、通常見られる哺乳動物免疫グロブリン
鎖に於けるアミノ酸配列の遺伝子レベルでの改変を可能
にし、この方法の真価はこれら変種を得る能力を有する
こと並びに所望の珍しく、しばしば汚染された分子を経
済的且つ特異的に産生する能力を有することにある。更
に、これらの変種は個々の鎖を単離する能力を特徴と
し、従って新規な集合体をもたらす。
物抗体の効率的産生を得るために用いた他の操作を全く
簡潔に変化させて、この基本的抗体型の多くの変種を産
生させることができる。これらの変種は組換技術の使用
に本質的であり、通常見られる哺乳動物免疫グロブリン
鎖に於けるアミノ酸配列の遺伝子レベルでの改変を可能
にし、この方法の真価はこれら変種を得る能力を有する
こと並びに所望の珍しく、しばしば汚染された分子を経
済的且つ特異的に産生する能力を有することにある。更
に、これらの変種は個々の鎖を単離する能力を特徴と
し、従って新規な集合体をもたらす。
【００６７】要するに、遺伝子操作は発現ベクターの作
成過程でゲノム材料の再編成を可能にするので、この種
の再編成を行なって「天然」抗体、もしくは免疫グロブリ
ンの成分に対し新規なコード配列を産生することができ
る。下記に詳細に説明するように、哺乳動物Ｈ鎖に対す
るコード配列は、単一起源又は単一クラスからは完全に
は得ることができず、配列の部分を例えばネズミ−ネズ
ミハイブリドーマ、ヒト−ネズミハイブリドーマ或いは
一連の抗原処理に呼応して分化させたＢ細胞のような種
々異なるmＲＮＡプールからＤ．１に記載した技術によ
り回収することができる。各々の場合に於ける配列の所
望の部分は、Ｄ．１に記載したプローブ及び分析技術を
用いて回収され且つ同じモデル配列の部分について使用
されると同じ結合法を用いて発現ベクターに組換えるこ
とができる。この種のキメラ鎖は任意所望の長さで作成
することができ、例えば完全なＨ鎖を作成することがで
き、そのＦab領域に対する配列のみを作成することもで
きる。
成過程でゲノム材料の再編成を可能にするので、この種
の再編成を行なって「天然」抗体、もしくは免疫グロブリ
ンの成分に対し新規なコード配列を産生することができ
る。下記に詳細に説明するように、哺乳動物Ｈ鎖に対す
るコード配列は、単一起源又は単一クラスからは完全に
は得ることができず、配列の部分を例えばネズミ−ネズ
ミハイブリドーマ、ヒト−ネズミハイブリドーマ或いは
一連の抗原処理に呼応して分化させたＢ細胞のような種
々異なるmＲＮＡプールからＤ．１に記載した技術によ
り回収することができる。各々の場合に於ける配列の所
望の部分は、Ｄ．１に記載したプローブ及び分析技術を
用いて回収され且つ同じモデル配列の部分について使用
されると同じ結合法を用いて発現ベクターに組換えるこ
とができる。この種のキメラ鎖は任意所望の長さで作成
することができ、例えば完全なＨ鎖を作成することがで
き、そのＦab領域に対する配列のみを作成することもで
きる。
【００６８】組換技術の使用により生ずる付加的な融通
性は、別々の培養物に於いてＨ鎖とＬ鎖もしくはその断
片或いは同じ培養物に於けるＨ鎖とＬ鎖との独特な組合
せを産生し、且つ適当な成分が組立てられるまで抗体又
は免疫グロブリン集合体の再編成を防止する能力から生
ずる。例えば、通常の抗体産生はＬ鎖及びＨ鎖の部分が
同じ細胞に於ける特定の決定子に呼応して作成されるの
で、自動的に「哺乳動物の交代」の生成をもたらすが、本
発明の方法は完全に新規な混合物を組立てる機会を提供
する。若干制限された量の「ハイブリッド」抗体が「クワ
ドローマ(quadroma)」、即ちこのように産生されたＨ鎖
とＬ鎖とのランダム集合を可能にする２種のハイブリド
ーマ細胞培養物の融合体により産生されている。
性は、別々の培養物に於いてＨ鎖とＬ鎖もしくはその断
片或いは同じ培養物に於けるＨ鎖とＬ鎖との独特な組合
せを産生し、且つ適当な成分が組立てられるまで抗体又
は免疫グロブリン集合体の再編成を防止する能力から生
ずる。例えば、通常の抗体産生はＬ鎖及びＨ鎖の部分が
同じ細胞に於ける特定の決定子に呼応して作成されるの
で、自動的に「哺乳動物の交代」の生成をもたらすが、本
発明の方法は完全に新規な混合物を組立てる機会を提供
する。若干制限された量の「ハイブリッド」抗体が「クワ
ドローマ(quadroma)」、即ちこのように産生されたＨ鎖
とＬ鎖とのランダム集合を可能にする２種のハイブリド
ーマ細胞培養物の融合体により産生されている。
【００６９】本発明は、所望鎖をin vitroで混合するこ
とにより、或いは同じ培養物を所望鎖に対するコード配
列で形質転換させることにより一層制御された所望鎖の
組立てを可能にする。
とにより、或いは同じ培養物を所望鎖に対するコード配
列で形質転換させることにより一層制御された所望鎖の
組立てを可能にする。
【００７０】Ｄ．４．複合免疫グロブリン 哺乳動物抗体の組換体産生につき詳細に説明した上記の
方法を若干改変して使用することにより、本発明に包含
される他の種類の抗体又はＮＳＩを作成することができ
る。鎖の相同性が種々異なる特異性の免疫グロブリン配
列に対応するような特定具体例の非特異性複合免疫グロ
ブリンを作成するには勿論、Ｈ鎖とＬ鎖とを別々の培養
物で作成し、これらを所望に応じて再組立てすることの
みを必要とする。
方法を若干改変して使用することにより、本発明に包含
される他の種類の抗体又はＮＳＩを作成することができ
る。鎖の相同性が種々異なる特異性の免疫グロブリン配
列に対応するような特定具体例の非特異性複合免疫グロ
ブリンを作成するには勿論、Ｈ鎖とＬ鎖とを別々の培養
物で作成し、これらを所望に応じて再組立てすることの
みを必要とする。
【００７１】例えば、抗−ＣＥＡＬ鎖／抗−肝炎Ｈ鎖の
複合抗体を作成するには、Ｌ鎖クローンのための鋳型と
して使用するmＲＮＡの適する原料は、例えばＥ．１に
記載する抗−ＣＥＡ産生細胞系である。Ｈ鎖に対応する
mＲＮＡは肝炎感染に反応して生じたＢ細胞から、或い
はＢ細胞がこの種の起源であるようなハイブリドーマか
ら得られるであろう。この種の複合体は本発明の方法を
用いて殆んど任意に組立てることができ、且つ各鎖に対
する鋳型として使用するのに適したmＲＮＡの入手し得
る起源によってのみ制約されることが明らかである。こ
の方法の他の特徴は、全て上記のものと同様である。
複合抗体を作成するには、Ｌ鎖クローンのための鋳型と
して使用するmＲＮＡの適する原料は、例えばＥ．１に
記載する抗−ＣＥＡ産生細胞系である。Ｈ鎖に対応する
mＲＮＡは肝炎感染に反応して生じたＢ細胞から、或い
はＢ細胞がこの種の起源であるようなハイブリドーマか
ら得られるであろう。この種の複合体は本発明の方法を
用いて殆んど任意に組立てることができ、且つ各鎖に対
する鋳型として使用するのに適したmＲＮＡの入手し得
る起源によってのみ制約されることが明らかである。こ
の方法の他の特徴は、全て上記のものと同様である。
【００７２】Ｄ．５．ハイブリッド抗体 ハイブリッド抗体は、２種以上の抗原と同時に反応し得
るので特に有用である。例えば上記Ｄ．４に示したよう
な種々異なる抗原に対する抗体の鎖に対応するＨ鎖とＬ
鎖との対は、４つの別々の培養物で作成され、四元体の
時期尚早な組立てを防止する。この後、別々に作成され
た４種のペプチドを混合することにより、所望の四元体
まで組立てることができる。ランダムな集合は極めて望
ましくない産生物の生成をもたらし得るが、同質(相同)
のＬ鎖及びＨ鎖が互いに結合されて他の対とは一致しな
いような産生物のその部分は所望のハイブリッド抗体を
与える。
るので特に有用である。例えば上記Ｄ．４に示したよう
な種々異なる抗原に対する抗体の鎖に対応するＨ鎖とＬ
鎖との対は、４つの別々の培養物で作成され、四元体の
時期尚早な組立てを防止する。この後、別々に作成され
た４種のペプチドを混合することにより、所望の四元体
まで組立てることができる。ランダムな集合は極めて望
ましくない産生物の生成をもたらし得るが、同質(相同)
のＬ鎖及びＨ鎖が互いに結合されて他の対とは一致しな
いような産生物のその部分は所望のハイブリッド抗体を
与える。
【００７３】Ｄ．６．キメラ抗体 キメラ抗体(例えば可変配列が不変配列とは別に誘導さ
れる)を作成するには、上記Ｄ．１及びＤ．２の手順を
適当に改変及び付加して応用することができる。好適手
順は、Ｈ鎖及びＬ鎖の部分をコードする遺伝子の所望部
分を適当な種々異なる起源から回収し、これら断片を制
限エンドヌクレアーゼにより再結合して各鎖をコードす
る遺伝子を再編成することである。
れる)を作成するには、上記Ｄ．１及びＤ．２の手順を
適当に改変及び付加して応用することができる。好適手
順は、Ｈ鎖及びＬ鎖の部分をコードする遺伝子の所望部
分を適当な種々異なる起源から回収し、これら断片を制
限エンドヌクレアーゼにより再結合して各鎖をコードす
る遺伝子を再編成することである。
【００７４】例えば、特に好適なキメラ構造に於いて、
ネズミハイブリドーマ培養物により産生される抗体の可
変配列をコードするＨ鎖遺伝子及びＬ鎖遺伝子の部分を
この培養物から回収し且つクローニングし、そしてヒト
抗体に対するＨ鎖及びＬ鎖の不変領域をコードする遺伝
子断片を例えばヒト骨髄腫細胞から回収しクローニング
する。次いで適する制限酵素を使用して、ネズミ遺伝子
の可変部分をヒト遺伝子の不変領域へ２つの鎖のそれぞ
れにつき結合させることができる。キメラ鎖はＤ．１に
示したように産生し、Ｄ．２に示したように合体させ、
非キメラ型と同様に使用する。勿論、鎖に於ける任意の
接合点を選択することができる。
ネズミハイブリドーマ培養物により産生される抗体の可
変配列をコードするＨ鎖遺伝子及びＬ鎖遺伝子の部分を
この培養物から回収し且つクローニングし、そしてヒト
抗体に対するＨ鎖及びＬ鎖の不変領域をコードする遺伝
子断片を例えばヒト骨髄腫細胞から回収しクローニング
する。次いで適する制限酵素を使用して、ネズミ遺伝子
の可変部分をヒト遺伝子の不変領域へ２つの鎖のそれぞ
れにつき結合させることができる。キメラ鎖はＤ．１に
示したように産生し、Ｄ．２に示したように合体させ、
非キメラ型と同様に使用する。勿論、鎖に於ける任意の
接合点を選択することができる。
【００７５】Ｄ．７．改変抗体 改変抗体は、本質的にキメラ抗体の範囲内にある。ここ
でも、Ｄ．１及びＤ．２の技術を応用することができ
る。然しながら鎖の接合部分ではなく適するアミノ酸の
改変、欠失又は付加を例えば突然変異のような可能な技
術により作成する(上記)。例えば、減少した補体固定
(結合)性を有する抗体をコードする遺伝子、或いは向上
した金属結合能力を有する遺伝子をこの種の技術を用い
て作成する。例えば、後者のクラスはメタロチオネイン
ＩＩをコードする公知の遺伝子配列を利用することがで
きる(Ｍ．Ｋarin et al．,Ｎature．２９９:７９７(１
９８２))。この分子断片のキレート化特性は、重金属を
腫瘍部位まで運ぶ際、腫瘍造影に於ける助剤として有用
である(Ｄ．Ａ．Ｓcheinberg et al．,Ｓcience,２１
５:１９(１９８２))。
でも、Ｄ．１及びＤ．２の技術を応用することができ
る。然しながら鎖の接合部分ではなく適するアミノ酸の
改変、欠失又は付加を例えば突然変異のような可能な技
術により作成する(上記)。例えば、減少した補体固定
(結合)性を有する抗体をコードする遺伝子、或いは向上
した金属結合能力を有する遺伝子をこの種の技術を用い
て作成する。例えば、後者のクラスはメタロチオネイン
ＩＩをコードする公知の遺伝子配列を利用することがで
きる(Ｍ．Ｋarin et al．,Ｎature．２９９:７９７(１
９８２))。この分子断片のキレート化特性は、重金属を
腫瘍部位まで運ぶ際、腫瘍造影に於ける助剤として有用
である(Ｄ．Ａ．Ｓcheinberg et al．,Ｓcience,２１
５:１９(１９８２))。
【００７６】Ｄ．８．単一価の抗体 他の好適具体例に於いて、第３の(Ｈ)鎖のＦc領域と結
合した一対のＨ鎖及びＬ鎖から成る抗体を生成させる。
これらの抗体は特に有用な性質を有する。これらは、通
常の抗体と同様に、例えば腫瘍のような組織の抗原表面
を標的として使用することができるが、通常の抗体とは
異なり、これらは標的組織の抗原表面を後退させて非受
容性とはならない。通常の抗体の使用は、数時間でこの
種の表面抗原の集合及びその後の失活をもたらす。
合した一対のＨ鎖及びＬ鎖から成る抗体を生成させる。
これらの抗体は特に有用な性質を有する。これらは、通
常の抗体と同様に、例えば腫瘍のような組織の抗原表面
を標的として使用することができるが、通常の抗体とは
異なり、これらは標的組織の抗原表面を後退させて非受
容性とはならない。通常の抗体の使用は、数時間でこの
種の表面抗原の集合及びその後の失活をもたらす。
【００７７】単一価の抗体の作成方法は、本発明の簡潔
な応用である。所望のＦc領域のＨ鎖に対する遺伝子を
制限酵素により開裂させ、所望のＦc領域をコードする
その部分のみを発現する。次いで、この部分をＤ．２の
技術を用いて別々に作成したＨ鎖に結合し、所望対をＨ
／Ｈ及びＦc／Ｆc組合せ物から分離し、別々に産生した
Ｌ鎖を付加する。このようにして、２つのＨ鎖部分の予
備結合は、通常の抗体が生成される可能性を減少させ
る。
な応用である。所望のＦc領域のＨ鎖に対する遺伝子を
制限酵素により開裂させ、所望のＦc領域をコードする
その部分のみを発現する。次いで、この部分をＤ．２の
技術を用いて別々に作成したＨ鎖に結合し、所望対をＨ
／Ｈ及びＦc／Ｆc組合せ物から分離し、別々に産生した
Ｌ鎖を付加する。このようにして、２つのＨ鎖部分の予
備結合は、通常の抗体が生成される可能性を減少させ
る。
【００７８】Ｄ．９．Ｆab蛋白質 同様にして、Ｈ鎖部分に対する完全遺伝子を含む必要は
ない。上記の変種を全てＦab蛋白質の産生に対する方法
に積み重ねることができ、全体的手順はアミノ末端２２
０個のアミノ酸をコードするＨ鎖の部分を適当な発現ベ
クターで使用する点のみ相違する。
ない。上記の変種を全てＦab蛋白質の産生に対する方法
に積み重ねることができ、全体的手順はアミノ末端２２
０個のアミノ酸をコードするＨ鎖の部分を適当な発現ベ
クターで使用する点のみ相違する。
【００７９】Ｅ．好適具体例の特定例 上記に本発明を一般的意味に於いて記載したが、所望抗
体を産生させる実験手順の詳細を説明するために以下い
くつかの特定具体例を示す。
体を産生させる実験手順の詳細を説明するために以下い
くつかの特定具体例を示す。
【００８０】例Ｅ．１は抗ＣＥＡ抗体成分を作成するた
めの即ち「哺乳動物抗体」を作成するための一般的手順を
示している。
めの即ち「哺乳動物抗体」を作成するための一般的手順を
示している。
【００８１】例Ｅ．３は再編成方法を示しており、従っ
て哺乳動物性複合ハイブリッド及びキメラ免疫グロブリ
ン並びにＦab蛋白質及び単一価の抗体を製造するために
応用できる。
て哺乳動物性複合ハイブリッド及びキメラ免疫グロブリ
ン並びにＦab蛋白質及び単一価の抗体を製造するために
応用できる。
【００８２】例Ｅ．４は、可変領域と不変領域とが種々
異なる起源から得られるようにＨ鎖もしくはＬ鎖を処理
するための手順を示している。
異なる起源から得られるようにＨ鎖もしくはＬ鎖を処理
するための手順を示している。
【００８３】例Ｅ．５は短くしたＨ鎖ゲノムを得る方法
を示しており、これはＦab領域の産生を可能にし且つ同
様にしてＦc領域の産生も可能にする。
を示しており、これはＦab領域の産生を可能にし且つ同
様にしてＦc領域の産生も可能にする。
【００８４】以下、実施例により本発明を説明するが、
これらのみに限定されない。
これらのみに限定されない。
【００８５】Ｅ．１．ネズミ抗−ＣＥＡ抗体鎖に対する
発現ベクターの作成及びペプチド合成 胎生期癌の抗原(ＣＥＡ)は、ヒトオリジンの或る種の腫
瘍細胞の表面に関連する(Ｐ．Ｇold et al．,Ｊ．Ｅx
p．Ｍed．,１２２:４６７(１９６５))。ＣＥＡに結合す
る抗体(抗−ＣＥＡ抗体)は、これら腫瘍の早期発見に有
用であり(Ｔ．Ｒ．Ｖan Ｎagell et al．,Ｃancer Ｒe
s．,４０:５０２(１９８０))、表面にＣＥＡを支持する
と思われるヒト腫瘍の処置に使用できる能力を有する。
Ｉgγ1型(クラス)の抗−ＣＥＡ抗体を分泌するネズミハ
イブリドーマ細胞系(ＣＥＡ．６６−Ｅ３)がＣ．Ｗagen
er et al．,Ｊ．Ｉmmunol．,１３０:２３０８(１９８
３)(この文献を引用して本明細書に包含する)に記載さ
れているように調製されて、mＲＮＡ源として使用され
た。この細胞系による抗ＣＥＡ抗体の産生を決定した。
これら細胞により産生された抗体のＮ−末端配列を次の
ようにしてモノクローナル抗−ＣＥＡのそれと比較し
た。精製したＩgＧをＰＣＡ酵素で処理し(Ｄ．Ｎ．Ｐod
ell et al．,Ｂiochem．Ｂiophys．Ｒes．Ｃommun．,８
１:１７６(１９７８)、次いで６Ｍグアニジン塩酸塩と
１０mＭ２−メルカプトエタノールに於いて解離させた
(１．０mgの免疫グロブリン、５分間、１００℃の水
浴)。解離した鎖をアルキルフェニルカラム(Ｗaters Ａ
ssociates社製)に於いて１００％Ａ(０．１％、ＴＦＡ
−水)〜９０％Ｂ(ＴＦＡ／Ｈ2Ｏ／ＭeＣＮ:０．１／
９．９／９０)の直線勾配を用いて０．８ml／min．の流
速で分離した。３つの主たるピークを溶出させ、銀染色
によってＳＤＳゲルで分析した。最初の２つのピークは
純粋なＬ鎖(ＭＷ２５,０００ダルトン)であり、第３の
ピークはＨ鎖とＬ鎖との７:３混合物であった。１．２n
Ｍ(ナノモル)のＬ鎖をＪ．Ｅ．Ｓhively, Ｍethods in
Ｅnzymology,７９:３１(１９８１)の方法により０．４n
ＭのＮＨ2末端収率にて配列決定した。Ｈ鎖とＬ鎖との
混合物(３nＭ)も配列決定し、Ｌ鎖の配列を二重配列か
ら推定してＨ鎖の配列を得た。
発現ベクターの作成及びペプチド合成 胎生期癌の抗原(ＣＥＡ)は、ヒトオリジンの或る種の腫
瘍細胞の表面に関連する(Ｐ．Ｇold et al．,Ｊ．Ｅx
p．Ｍed．,１２２:４６７(１９６５))。ＣＥＡに結合す
る抗体(抗−ＣＥＡ抗体)は、これら腫瘍の早期発見に有
用であり(Ｔ．Ｒ．Ｖan Ｎagell et al．,Ｃancer Ｒe
s．,４０:５０２(１９８０))、表面にＣＥＡを支持する
と思われるヒト腫瘍の処置に使用できる能力を有する。
Ｉgγ1型(クラス)の抗−ＣＥＡ抗体を分泌するネズミハ
イブリドーマ細胞系(ＣＥＡ．６６−Ｅ３)がＣ．Ｗagen
er et al．,Ｊ．Ｉmmunol．,１３０:２３０８(１９８
３)(この文献を引用して本明細書に包含する)に記載さ
れているように調製されて、mＲＮＡ源として使用され
た。この細胞系による抗ＣＥＡ抗体の産生を決定した。
これら細胞により産生された抗体のＮ−末端配列を次の
ようにしてモノクローナル抗−ＣＥＡのそれと比較し
た。精製したＩgＧをＰＣＡ酵素で処理し(Ｄ．Ｎ．Ｐod
ell et al．,Ｂiochem．Ｂiophys．Ｒes．Ｃommun．,８
１:１７６(１９７８)、次いで６Ｍグアニジン塩酸塩と
１０mＭ２−メルカプトエタノールに於いて解離させた
(１．０mgの免疫グロブリン、５分間、１００℃の水
浴)。解離した鎖をアルキルフェニルカラム(Ｗaters Ａ
ssociates社製)に於いて１００％Ａ(０．１％、ＴＦＡ
−水)〜９０％Ｂ(ＴＦＡ／Ｈ2Ｏ／ＭeＣＮ:０．１／
９．９／９０)の直線勾配を用いて０．８ml／min．の流
速で分離した。３つの主たるピークを溶出させ、銀染色
によってＳＤＳゲルで分析した。最初の２つのピークは
純粋なＬ鎖(ＭＷ２５,０００ダルトン)であり、第３の
ピークはＨ鎖とＬ鎖との７:３混合物であった。１．２n
Ｍ(ナノモル)のＬ鎖をＪ．Ｅ．Ｓhively, Ｍethods in
Ｅnzymology,７９:３１(１９８１)の方法により０．４n
ＭのＮＨ2末端収率にて配列決定した。Ｈ鎖とＬ鎖との
混合物(３nＭ)も配列決定し、Ｌ鎖の配列を二重配列か
ら推定してＨ鎖の配列を得た。
【００８６】以下の説明に於いて、ＣＥＡ．６６−Ｅ３
により産生された抗ＣＥＡ抗体に対するＨ鎖及びＬ鎖の
遺伝子の単離及び発現につき記載する。これら鎖の不変
領域はそれぞれγ及びκ型(family)に属するので、「Ｌ
鎖」と「κ鎖」及び「Ｈ鎖」と「γ鎖」とをそれぞれ以下では
互換的に使用する。
により産生された抗ＣＥＡ抗体に対するＨ鎖及びＬ鎖の
遺伝子の単離及び発現につき記載する。これら鎖の不変
領域はそれぞれγ及びκ型(family)に属するので、「Ｌ
鎖」と「κ鎖」及び「Ｈ鎖」と「γ鎖」とをそれぞれ以下では
互換的に使用する。
【００８７】Ｅ．１．１．抗ＣＥＡのＬ鎖及びＨ鎖(κ
及びγ鎖)に対するメッセンジャーＲＮＡの単離 ＣＥＡ．６６−Ｅ３細胞から全ＲＮＡをＬynch et a
l．,Ｖirology,９８:２５１(１９７９)により報告され
たように抽出した。これら細胞を遠心分離によりペレッ
ト化し、約１g部分のペレットを１０mＭ ＮaＣl,１０m
ＭトリスＨＣl(pＨ７．４)、１．５mＭ ＭgＣl2の１０
ml中に再懸濁した。この再懸濁した細胞を最終濃度１％
まで非イオン性表面活性剤ＮＰ−４０を添加して溶菌
し、核を遠心分離により除去した。１％最終濃度までＳ
ＤＳ(pＨ７．４)を添加した後、上清を３mlずつのフェ
ノール(再蒸溜)／クロロホルム:イソアミルアルコール
２５:１にて４℃で２回抽出した。水相をＮaＣl中で
０．２Ｍとし、２倍容量の１００％エタノールを添加
し、−２０℃で１晩貯蔵することにより全ＲＮＡを沈澱
した。遠心分離後、ポリ−Ａ mＲＮＡをＡviv及びＬed
er,Ｐroc．Ｎatl．Ａcad．Ｓci．,ＵＳＡ,６９:１４０
８(１９７２)により記載されたオリゴ−dＴセルロース
クロマトグラフィーにより全ＲＮＡから精製した。１g
の細胞から１４２μgのポリ−Ａ mＲＮＡが得られた。
及びγ鎖)に対するメッセンジャーＲＮＡの単離 ＣＥＡ．６６−Ｅ３細胞から全ＲＮＡをＬynch et a
l．,Ｖirology,９８:２５１(１９７９)により報告され
たように抽出した。これら細胞を遠心分離によりペレッ
ト化し、約１g部分のペレットを１０mＭ ＮaＣl,１０m
ＭトリスＨＣl(pＨ７．４)、１．５mＭ ＭgＣl2の１０
ml中に再懸濁した。この再懸濁した細胞を最終濃度１％
まで非イオン性表面活性剤ＮＰ−４０を添加して溶菌
し、核を遠心分離により除去した。１％最終濃度までＳ
ＤＳ(pＨ７．４)を添加した後、上清を３mlずつのフェ
ノール(再蒸溜)／クロロホルム:イソアミルアルコール
２５:１にて４℃で２回抽出した。水相をＮaＣl中で
０．２Ｍとし、２倍容量の１００％エタノールを添加
し、−２０℃で１晩貯蔵することにより全ＲＮＡを沈澱
した。遠心分離後、ポリ−Ａ mＲＮＡをＡviv及びＬed
er,Ｐroc．Ｎatl．Ａcad．Ｓci．,ＵＳＡ,６９:１４０
８(１９７２)により記載されたオリゴ−dＴセルロース
クロマトグラフィーにより全ＲＮＡから精製した。１g
の細胞から１４２μgのポリ−Ａ mＲＮＡが得られた。
【００８８】Ｅ．１．２．Ｈ鎖及びＬ鎖のＤＮＡ配列挿
入物を有するプラスミドを含有したＥ．coliコロニーラ
イブラリーの作成 上記Ｅ．１．１で調製した未分画ポリ−Ａ mＲＮＡの
５μgをＧoeddel et al．,Ｎature,２８１:５４４(１
９７９)及びＷickens et al．,Ｊ．Ｂiol．Ｃhem．,２
５３:２４８３(１９７８)(この文献を引用して本明細書
に包含する)により、二重鎖(ds)cＤＮＡのオリゴ−dＴ
プライム処理調製物に対する鋳型として使用した。この
cＤＮＡを６％ポリアクリルアミドゲル電気泳動によっ
て寸法(サイズ)分画し、長さ６００塩基対より大きいds
cＤＮＡの１２４ngを電気溶出によって回収した。２０
ngのds cＤＮＡをＣhang et al．,Ｎature,２７５:６１
７(１９７８)(この文献を引用して本明細書に包含する)
に記載された末端(ターミナル)デオキシヌクレオチジル
トランスフェラーゼを用いてデオキシＣ残基で延長さ
せ、予めＰstＩにより開裂させ、デオキシＧで処理した
２００ngのプラスミドpＢＲ３２２(Ｂolivar et al．,
Ｇene,２:９５(１９７７))と共にアニールした。それぞ
れアニールした混合物をＥ．coli Ｋ１２菌株２９４
(ＡＴＣＣ Ｎo．３１４４６)に形質転換した。約８,５
００種のアンピシリン感受性且つテトラサイクリン耐性
の形質転換体が得られた。
入物を有するプラスミドを含有したＥ．coliコロニーラ
イブラリーの作成 上記Ｅ．１．１で調製した未分画ポリ−Ａ mＲＮＡの
５μgをＧoeddel et al．,Ｎature,２８１:５４４(１
９７９)及びＷickens et al．,Ｊ．Ｂiol．Ｃhem．,２
５３:２４８３(１９７８)(この文献を引用して本明細書
に包含する)により、二重鎖(ds)cＤＮＡのオリゴ−dＴ
プライム処理調製物に対する鋳型として使用した。この
cＤＮＡを６％ポリアクリルアミドゲル電気泳動によっ
て寸法(サイズ)分画し、長さ６００塩基対より大きいds
cＤＮＡの１２４ngを電気溶出によって回収した。２０
ngのds cＤＮＡをＣhang et al．,Ｎature,２７５:６１
７(１９７８)(この文献を引用して本明細書に包含する)
に記載された末端(ターミナル)デオキシヌクレオチジル
トランスフェラーゼを用いてデオキシＣ残基で延長さ
せ、予めＰstＩにより開裂させ、デオキシＧで処理した
２００ngのプラスミドpＢＲ３２２(Ｂolivar et al．,
Ｇene,２:９５(１９７７))と共にアニールした。それぞ
れアニールした混合物をＥ．coli Ｋ１２菌株２９４
(ＡＴＣＣ Ｎo．３１４４６)に形質転換した。約８,５
００種のアンピシリン感受性且つテトラサイクリン耐性
の形質転換体が得られた。
【００８９】Ｅ．１．３．合成プローブの作成 可変領域ＤＮＡ配列の２５塩基対３'で始まるネズミＭ
ＯＰＣ２１κ鎖に対する不変領域のコード配列に補完
(相補)的な１４元体、即ち５'ＧＧＴＧＧＧＡＡＧＡＴ
ＧＧＡ３'をκ鎖プローブとして使用した。ネズミＭＯ
ＰＣ２１γ鎖に対する可変領域ＤＮＡ配列の７２塩基対
３'に位置するコード配列に補完的な１５元体、即ち５'
ＧＡＣＣＡＧＧＣＡＴＣＣＣＡＧ３'をγ鎖遺伝子プロ
ーブとして使用した。
ＯＰＣ２１κ鎖に対する不変領域のコード配列に補完
(相補)的な１４元体、即ち５'ＧＧＴＧＧＧＡＡＧＡＴ
ＧＧＡ３'をκ鎖プローブとして使用した。ネズミＭＯ
ＰＣ２１γ鎖に対する可変領域ＤＮＡ配列の７２塩基対
３'に位置するコード配列に補完的な１５元体、即ち５'
ＧＡＣＣＡＧＧＣＡＴＣＣＣＡＧ３'をγ鎖遺伝子プロ
ーブとして使用した。
【００９０】両プローブは、ドイツ公開公報第２６４４
４３２号(この文献を引用して本明細書に包含する)に記
載されたホスホトリエステル法により合成し、次のよう
にキナーゼ処理して放射能活性にした。２５０ngのデオ
キシオリゴヌクレオチドを６０mＭトリスＨＣl(pＨ
８)、１０mＭ ＭgＣl2、１５mＭ β−メルカプトエタ
ノール及び１００μＣi(γ−Ｐ32)ＡＴＰ(Ａmersham,
５,０００Ｃi／mＭ)の２５μl中に入れた。５ユニット
のＴ４ポリヌクレオチドキナーゼを加え、反応を３７℃
にて３０分間進行させ、ＥＤＴＡを２０mＭまで加える
ことにより停止させた。
４３２号(この文献を引用して本明細書に包含する)に記
載されたホスホトリエステル法により合成し、次のよう
にキナーゼ処理して放射能活性にした。２５０ngのデオ
キシオリゴヌクレオチドを６０mＭトリスＨＣl(pＨ
８)、１０mＭ ＭgＣl2、１５mＭ β−メルカプトエタ
ノール及び１００μＣi(γ−Ｐ32)ＡＴＰ(Ａmersham,
５,０００Ｃi／mＭ)の２５μl中に入れた。５ユニット
のＴ４ポリヌクレオチドキナーゼを加え、反応を３７℃
にて３０分間進行させ、ＥＤＴＡを２０mＭまで加える
ことにより停止させた。
【００９１】Ｅ．１．４．κ鎖又はγ鎖配列に対するコ
ロニーライブラリーの選別 上記Ｅ．１．２に記載したように、調製した約２,００
０個のコロニーをＬＢ(Ｍiller, Ｅxperiments in Ｍol
ecular Ｇenetics,p．４３１−３,Ｃold Ｓpring Ｈar
bor Ｌab．,Ｃold Ｓpring Ｈarbor, Ｎew Ｙork(１９
７２)＋５μg／mlのテトラサイクリンを含有するマイク
ロタイター皿の穴に個々に接種し、ＤＭＳＯを７％まで
添加した後に−２０℃で貯蔵した。このライブラリーか
らの個々のコロニーを２組のＳchleicher及びＳchuell
ＢＡ８５／２０のニトロセルロースフィルターに移
し、ＬＢ＋５μg／mlテトラサイクリンを含有する寒天
板で増殖した。３７℃にて約１０時間増殖した後、これ
らのコロニーフィルターをＬＢ＋５μg／mlテトラサイ
クリンと１２．５μg／mlのクロラムフェニコールとを
含有する寒天板に移し、３７℃にて１晩再培養した。次
いで、各コロニーからのＤＮＡを変性させ、Ｇrunstein
et al．,Ｐroc．Ｎatl．Ａcad．Ｓci．,ＵＳＡ,７２:
３９６１(１９７５)(この文献を引用して本明細書に包
含する)に記載されたＧrunstein−Ｈogness法の変法に
よってフィルターに固定した。各フィルターを０．５Ｎ
ＮaＯＨと１．５Ｍ ＮaＣlとの上に３分間浮遊させ
てコロニーを溶菌し、ＤＮＡを変性させ、次いで３Ｍ
ＮaＣlと０．５ＭトリスＨＣl(pＨ７．５)の上に１５分
間浮遊させて中和した。次いでこれらフィルターを２×
ＳＳＣ上に更に１５分間浮遊させ、８０℃の減圧オーブ
ン内で２時間焼成した。これらフィルターを０．９Ｍ
ＮaＣl、１×Ｄenhardts,１００mＭトリスＨＣl(pＨ
７．５)、５mＭ Ｎa−ＥＤＴＡ、１mＭ ＡＴＰ、１Ｍ
燐酸ナトリウム(二塩基性)、１mＭピロ燐酸ナトリウ
ム、０．５％ＮＰ−４０及び２００μg／mlＥ．colit−
ＲＮＡに於いて室温で２時間予備ハイブリゼーションし
た後、同じ溶液で１晩ハイブリゼーションし(実質的に
Ｗellace et al．,Ｎucleic Ａcids Ｒesearch,９:８７
９(１９８１)に記載されている)、この場合、上記のキ
ナーゼ処理したκプローブ又はγプローブの約４０×１
０6cpmを使用した。６×ＳＳＣ、０．１％ＳＤＳ中に於
いて、３７℃で激しく洗浄した後、これらフィルターを
ＤupontＬightning−Ｐlusg強化スクリーンを用いてＫo
dak ＸＲ−５ Ｘ線フィルムに−８０℃で１６〜２４時
間露出した。κ鎖プローブとハイブリダイズした約２０
種のコロニー及びγ鎖プローブとハイブリダイズした２
０種のコロニーを特性化した。
ロニーライブラリーの選別 上記Ｅ．１．２に記載したように、調製した約２,００
０個のコロニーをＬＢ(Ｍiller, Ｅxperiments in Ｍol
ecular Ｇenetics,p．４３１−３,Ｃold Ｓpring Ｈar
bor Ｌab．,Ｃold Ｓpring Ｈarbor, Ｎew Ｙork(１９
７２)＋５μg／mlのテトラサイクリンを含有するマイク
ロタイター皿の穴に個々に接種し、ＤＭＳＯを７％まで
添加した後に−２０℃で貯蔵した。このライブラリーか
らの個々のコロニーを２組のＳchleicher及びＳchuell
ＢＡ８５／２０のニトロセルロースフィルターに移
し、ＬＢ＋５μg／mlテトラサイクリンを含有する寒天
板で増殖した。３７℃にて約１０時間増殖した後、これ
らのコロニーフィルターをＬＢ＋５μg／mlテトラサイ
クリンと１２．５μg／mlのクロラムフェニコールとを
含有する寒天板に移し、３７℃にて１晩再培養した。次
いで、各コロニーからのＤＮＡを変性させ、Ｇrunstein
et al．,Ｐroc．Ｎatl．Ａcad．Ｓci．,ＵＳＡ,７２:
３９６１(１９７５)(この文献を引用して本明細書に包
含する)に記載されたＧrunstein−Ｈogness法の変法に
よってフィルターに固定した。各フィルターを０．５Ｎ
ＮaＯＨと１．５Ｍ ＮaＣlとの上に３分間浮遊させ
てコロニーを溶菌し、ＤＮＡを変性させ、次いで３Ｍ
ＮaＣlと０．５ＭトリスＨＣl(pＨ７．５)の上に１５分
間浮遊させて中和した。次いでこれらフィルターを２×
ＳＳＣ上に更に１５分間浮遊させ、８０℃の減圧オーブ
ン内で２時間焼成した。これらフィルターを０．９Ｍ
ＮaＣl、１×Ｄenhardts,１００mＭトリスＨＣl(pＨ
７．５)、５mＭ Ｎa−ＥＤＴＡ、１mＭ ＡＴＰ、１Ｍ
燐酸ナトリウム(二塩基性)、１mＭピロ燐酸ナトリウ
ム、０．５％ＮＰ−４０及び２００μg／mlＥ．colit−
ＲＮＡに於いて室温で２時間予備ハイブリゼーションし
た後、同じ溶液で１晩ハイブリゼーションし(実質的に
Ｗellace et al．,Ｎucleic Ａcids Ｒesearch,９:８７
９(１９８１)に記載されている)、この場合、上記のキ
ナーゼ処理したκプローブ又はγプローブの約４０×１
０6cpmを使用した。６×ＳＳＣ、０．１％ＳＤＳ中に於
いて、３７℃で激しく洗浄した後、これらフィルターを
ＤupontＬightning−Ｐlusg強化スクリーンを用いてＫo
dak ＸＲ−５ Ｘ線フィルムに−８０℃で１６〜２４時
間露出した。κ鎖プローブとハイブリダイズした約２０
種のコロニー及びγ鎖プローブとハイブリダイズした２
０種のコロニーを特性化した。
【００９２】Ｅ．１．５．κＤＮＡ配列プローブにハイ
ブリダイズしたコロニーの特性化 κ鎖プローブにハイブリダイズした数種の異なる形質転
換体から単離したプラスミドＤＮＡをＰstＩにより開裂
し、ポリアクリルアミドゲル電気泳動(ＰＡＧＥ)により
分画した。この分析により、多数のプラスミドＤＮＡが
充分な長さのκ鎖をコード化するのに充分な大きさのc
ＤＮＡ挿入物を含有することが示された。これらプラス
ミドの１種に於けるcＤＮＡ挿入物の完全ヌクレオチド
配列をＳmith, Ｍethods Ｅnzymol．,６５:５６０(１９
８０)(この文献を引用して本明細書に包含する)に記載
されたジデオキシヌクレオチド鎖停止法により、制限エ
ンドヌクレアーゼ開裂断片をＭ１３ベクター中へサブク
ローニングした後に決定した(Ｍessing et al．,Ｎucle
ic Ａcids Ｒesearch,９:３０９(１９８１))。図２、図
３、図４および図５はpＫ１７Ｇ４のcＤＮＡ挿入物のヌ
クレオチド配列を示し、図６、図７および図８は対応す
るアミノ酸配列を有する遺伝子配列を示している。ネズ
ミ抗−ＣＥＡκ鎖の全コード領域を、この１種の大型Ｄ
ＮＡ断片につき単離した。κ鎖のアミノ酸配列は、pＫ
１７Ｇ４ cＤＮＡ挿入物のヌクレオチド配列から推定
して、成熟ネズミ抗−ＣＥＡκ鎖の最初の２３個のＮ−
末端アミノ酸と完全に一致し、これは精製したネズミ抗
−ＣＥＡκ鎖のアミノ酸配列分析により決定された。p
Ｋ１７Ｇ４のコード領域は、予備配列の２７塩基対もし
くは９個のアミノ酸と成熟蛋白質の６４２塩基対もしく
は２１４個のアミノ酸を含有する。グリコシル化してい
ない成熟蛋白質(ＭＷ２４,５５３)は、１２個のアミノ
酸のＪ１結合領域を含め１１９個のアミノ酸から成る可
変領域と１０７個のアミノ酸から成る不変領域とを有す
る。アミノ酸２１５の後の停止コドンの後にポリ−Ａ付
加に至るまで３'未翻訳配列の２１２塩基対が始まる。p
Ｋ１７Ｇ４を同定するために使用したκ鎖プローブは、
ヌクレオチド３７４−３８８にハイブリダイズする
(図、図３、図４および図５)。
ブリダイズしたコロニーの特性化 κ鎖プローブにハイブリダイズした数種の異なる形質転
換体から単離したプラスミドＤＮＡをＰstＩにより開裂
し、ポリアクリルアミドゲル電気泳動(ＰＡＧＥ)により
分画した。この分析により、多数のプラスミドＤＮＡが
充分な長さのκ鎖をコード化するのに充分な大きさのc
ＤＮＡ挿入物を含有することが示された。これらプラス
ミドの１種に於けるcＤＮＡ挿入物の完全ヌクレオチド
配列をＳmith, Ｍethods Ｅnzymol．,６５:５６０(１９
８０)(この文献を引用して本明細書に包含する)に記載
されたジデオキシヌクレオチド鎖停止法により、制限エ
ンドヌクレアーゼ開裂断片をＭ１３ベクター中へサブク
ローニングした後に決定した(Ｍessing et al．,Ｎucle
ic Ａcids Ｒesearch,９:３０９(１９８１))。図２、図
３、図４および図５はpＫ１７Ｇ４のcＤＮＡ挿入物のヌ
クレオチド配列を示し、図６、図７および図８は対応す
るアミノ酸配列を有する遺伝子配列を示している。ネズ
ミ抗−ＣＥＡκ鎖の全コード領域を、この１種の大型Ｄ
ＮＡ断片につき単離した。κ鎖のアミノ酸配列は、pＫ
１７Ｇ４ cＤＮＡ挿入物のヌクレオチド配列から推定
して、成熟ネズミ抗−ＣＥＡκ鎖の最初の２３個のＮ−
末端アミノ酸と完全に一致し、これは精製したネズミ抗
−ＣＥＡκ鎖のアミノ酸配列分析により決定された。p
Ｋ１７Ｇ４のコード領域は、予備配列の２７塩基対もし
くは９個のアミノ酸と成熟蛋白質の６４２塩基対もしく
は２１４個のアミノ酸を含有する。グリコシル化してい
ない成熟蛋白質(ＭＷ２４,５５３)は、１２個のアミノ
酸のＪ１結合領域を含め１１９個のアミノ酸から成る可
変領域と１０７個のアミノ酸から成る不変領域とを有す
る。アミノ酸２１５の後の停止コドンの後にポリ−Ａ付
加に至るまで３'未翻訳配列の２１２塩基対が始まる。p
Ｋ１７Ｇ４を同定するために使用したκ鎖プローブは、
ヌクレオチド３７４−３８８にハイブリダイズする
(図、図３、図４および図５)。
【００９３】Ｅ．１．６．γ１ＤＮＡプローブにハイブ
リダイズしたコロニーの特性化 Ｈ鎖γ１プローブとのハイブリダイズに対し陽性である
数種の形質転換体から単離されたプラスミドＤＮＡを、
上記Ｅ．１．５．に記載したようにＰstＩ制限エンドヌ
クレアーゼ分析にかけた。最も大きいcＤＮＡ挿入物断
片を示すプラスミドＤＮＡを後の試験用に選択した。ネ
ズミＨ鎖(γ−１鎖)をコード化するヌクレオチド配列
は、可変領域と不変領域との間の接合部近くにＮcoＩ制
限エンドヌクレアーゼ開裂部位を有する。選択したプラ
スミドＤＮＡをＰstＩとＮcoＩとの両者により消化し、
ポリアクリルアミドで寸法分画した。この分析はＮcoＩ
制限エンドヌクレアーゼ部位を有する多数のプラスミド
ＤＮＡの同定を可能にするが、このいずれもネズミ抗−
ＣＥＡＨ鎖の全コード化領域をコードするのに充分大き
いcＤＮＡ挿入物断片を示さない。
リダイズしたコロニーの特性化 Ｈ鎖γ１プローブとのハイブリダイズに対し陽性である
数種の形質転換体から単離されたプラスミドＤＮＡを、
上記Ｅ．１．５．に記載したようにＰstＩ制限エンドヌ
クレアーゼ分析にかけた。最も大きいcＤＮＡ挿入物断
片を示すプラスミドＤＮＡを後の試験用に選択した。ネ
ズミＨ鎖(γ−１鎖)をコード化するヌクレオチド配列
は、可変領域と不変領域との間の接合部近くにＮcoＩ制
限エンドヌクレアーゼ開裂部位を有する。選択したプラ
スミドＤＮＡをＰstＩとＮcoＩとの両者により消化し、
ポリアクリルアミドで寸法分画した。この分析はＮcoＩ
制限エンドヌクレアーゼ部位を有する多数のプラスミド
ＤＮＡの同定を可能にするが、このいずれもネズミ抗−
ＣＥＡＨ鎖の全コード化領域をコードするのに充分大き
いcＤＮＡ挿入物断片を示さない。
【００９４】単離した１種のプラスミド(即ちpγ２９
８)に於いて、約１３００bpのcＤＮＡ挿入物は５'未翻
訳領域、信号配列及びＨ鎖のＮ−末端部分に対する配列
情報を有する。pγ２９８はネズミ抗−ＣＥＡγ１鎖に
対するＣ−末端配列をコードしなかったので、プラスミ
ドＤＮＡを他のコロニーから単離してＰstＩ及びＮcoＩ
で選別した。pγ１１のcＤＮＡ挿入物に於けるＣ−末端
領域を配列決定して、停止コドンと３'未翻訳配列とpγ
２９８から喪失されたコード配列の部分とを含有するこ
とが示された。
８)に於いて、約１３００bpのcＤＮＡ挿入物は５'未翻
訳領域、信号配列及びＨ鎖のＮ−末端部分に対する配列
情報を有する。pγ２９８はネズミ抗−ＣＥＡγ１鎖に
対するＣ−末端配列をコードしなかったので、プラスミ
ドＤＮＡを他のコロニーから単離してＰstＩ及びＮcoＩ
で選別した。pγ１１のcＤＮＡ挿入物に於けるＣ−末端
領域を配列決定して、停止コドンと３'未翻訳配列とpγ
２９８から喪失されたコード配列の部分とを含有するこ
とが示された。
【００９５】図９、図１０、図１１、図１２、図１３及
び図１４はネズミ抗−ＣＥＡＨ鎖の全ヌクレオチド配列
を示し(Ｓmith, Ｍethods Ｅnzymol．,６５:５６０(１
９８０)のジデオキシヌクレオチド鎖停止法により決定
する)、図１５、図１６、図１７、図１８および図１９
は翻訳配列を含んでいる。
び図１４はネズミ抗−ＣＥＡＨ鎖の全ヌクレオチド配列
を示し(Ｓmith, Ｍethods Ｅnzymol．,６５:５６０(１
９８０)のジデオキシヌクレオチド鎖停止法により決定
する)、図１５、図１６、図１７、図１８および図１９
は翻訳配列を含んでいる。
【００９６】pγ２９８ cＤＮＡ挿入物のヌクレオチド
配列から推定したγ１(Ｈ鎖)のアミノ酸配列は、精製ネ
ズミ抗−ＣＥＡγ１鎖のアミノ酸配列分析により決定し
て成熟ネズミ抗−ＣＥＡγ１鎖の最初の２３個のＮ−末
端アミノ酸に完全に一致する。コード領域は予備配列の
５７塩基対もしくは１９個のアミノ酸と、成熟蛋白質の
１３４６塩基対もしくは４４７個のアミノ酸とより成っ
ている。グリコシル化されていない成熟蛋白質(ＭＷ５
２,２５８)は、１２個のアミノ酸のＤ領域を含め１３５
個のアミノ酸より成る可変領域と、１３個のアミノ酸よ
り成るＪ４結合領域とを有する。不変領域は３２４個の
アミノ酸である。アミノ酸４４７の後の停止コドンに続
いて、ポリ−Ａ付加まで９６bpの３未翻訳配列が開始す
る。pγ２９８及びpγ１１を同定するために使用したプ
ローブは、ヌクレオチド５２８−５４２にハイブリダイ
ズした(図９、図１０、図１１、図１２、図１３及び図
１４)。
配列から推定したγ１(Ｈ鎖)のアミノ酸配列は、精製ネ
ズミ抗−ＣＥＡγ１鎖のアミノ酸配列分析により決定し
て成熟ネズミ抗−ＣＥＡγ１鎖の最初の２３個のＮ−末
端アミノ酸に完全に一致する。コード領域は予備配列の
５７塩基対もしくは１９個のアミノ酸と、成熟蛋白質の
１３４６塩基対もしくは４４７個のアミノ酸とより成っ
ている。グリコシル化されていない成熟蛋白質(ＭＷ５
２,２５８)は、１２個のアミノ酸のＤ領域を含め１３５
個のアミノ酸より成る可変領域と、１３個のアミノ酸よ
り成るＪ４結合領域とを有する。不変領域は３２４個の
アミノ酸である。アミノ酸４４７の後の停止コドンに続
いて、ポリ−Ａ付加まで９６bpの３未翻訳配列が開始す
る。pγ２９８及びpγ１１を同定するために使用したプ
ローブは、ヌクレオチド５２８−５４２にハイブリダイ
ズした(図９、図１０、図１１、図１２、図１３及び図
１４)。
【００９７】Ｅ．１．７．ネズミ成熟抗−ＣＥＡ κ鎖
遺伝子を直接発現させるためのプラスミドの作成、pＫ
ＣＥＡtrp２０７−１＊ 図２０、図２１および図２２はpＫＣＥＡtrp２０７−１
＊の作成を示している。
遺伝子を直接発現させるためのプラスミドの作成、pＫ
ＣＥＡtrp２０７−１＊ 図２０、図２１および図２２はpＫＣＥＡtrp２０７−１
＊の作成を示している。
【００９８】まず、単一のtrpプロモーターを有する中
間プラスミドpＨＧＨ２０７−１＊を次のように作成し
た:プラスミドpＨＧＨ２０７(１９８１年１０月１日付
出願の米国特許出願第３０７,４７３号(ＥＰＯ公開第０
０３６７７６号)に記載)は、二重lacプロモーターに続
いてＥcoＲＩ部位に整列(フランキング)するtrpプロモ
ーターを有し、これを使用してpＨＣＨ２０７−１を作
成した。pＨＧＨ２０７をＢamＨＩで消化し、ＥcoＲＩ
で部分消化した。完全trpプロモーターを含有する最も
大きい断片を単離し、これをpＢＲ３２２からの最も大
きいＥcoＲＩ−ＢamＨＩ断片に結合し、この結合混合物
を使用してＥ．coli２９４を形質転換した。ＴetR Ａmp
Rのコロニーを単離し、これらの殆んどはpＨＧＨ２０７
−１を含有した。ampR遺伝子とtrpプロモーターの間に
ＥcoＲＩ部位を欠如するpＨＧＨ２０７−１＊をＥcoＲ
ＩでのpＨＧＨ２０７−１の部分消化、末端に於けるＫl
enow及びdＮＴＰの充填及び再結合によって得た。
間プラスミドpＨＧＨ２０７−１＊を次のように作成し
た:プラスミドpＨＧＨ２０７(１９８１年１０月１日付
出願の米国特許出願第３０７,４７３号(ＥＰＯ公開第０
０３６７７６号)に記載)は、二重lacプロモーターに続
いてＥcoＲＩ部位に整列(フランキング)するtrpプロモ
ーターを有し、これを使用してpＨＣＨ２０７−１を作
成した。pＨＧＨ２０７をＢamＨＩで消化し、ＥcoＲＩ
で部分消化した。完全trpプロモーターを含有する最も
大きい断片を単離し、これをpＢＲ３２２からの最も大
きいＥcoＲＩ−ＢamＨＩ断片に結合し、この結合混合物
を使用してＥ．coli２９４を形質転換した。ＴetR Ａmp
Rのコロニーを単離し、これらの殆んどはpＨＧＨ２０７
−１を含有した。ampR遺伝子とtrpプロモーターの間に
ＥcoＲＩ部位を欠如するpＨＧＨ２０７−１＊をＥcoＲ
ＩでのpＨＧＨ２０７−１の部分消化、末端に於けるＫl
enow及びdＮＴＰの充填及び再結合によって得た。
【００９９】５μgのpＨＧＨ２０７−１＊をＥcoＲＩで
消化し、これら末端を６０mＭ ＮaＣl,７mＭ ＭgＣ
l2,７mＭトリスＨＣl(pＨ７．４)及び１mＭの各dＮＴＰ
を含有する５０μlの反応液中で１２ユニットのＤＮＡ
ポリメラーゼを用いて３７℃にて１時間延長し、次いで
フェノール／ＣＨＣl3で抽出しエタノールで沈澱させ
た。沈澱したＤＮＡをＢamＨＩで消化し、大ベクター断
片(断片１)を５％ポリアクリルアミドゲル電気泳動、電
気溶出、フェノール／ＣＨＣl3抽出及びエタノール沈澱
によって精製した。
消化し、これら末端を６０mＭ ＮaＣl,７mＭ ＭgＣ
l2,７mＭトリスＨＣl(pＨ７．４)及び１mＭの各dＮＴＰ
を含有する５０μlの反応液中で１２ユニットのＤＮＡ
ポリメラーゼを用いて３７℃にて１時間延長し、次いで
フェノール／ＣＨＣl3で抽出しエタノールで沈澱させ
た。沈澱したＤＮＡをＢamＨＩで消化し、大ベクター断
片(断片１)を５％ポリアクリルアミドゲル電気泳動、電
気溶出、フェノール／ＣＨＣl3抽出及びエタノール沈澱
によって精製した。
【０１００】このＤＮＡを１０mＭトリス(pＨ８)、１m
Ｍ ＥＤＴＡの５０μl中に再懸濁し、５００ユニット
の細菌性アルカリホスファターゼ(ＢＡＰ)で６５℃にて
３０秒間処理し、フェノールＣＨＣl3抽出し、エタノー
ル沈澱させた。
Ｍ ＥＤＴＡの５０μl中に再懸濁し、５００ユニット
の細菌性アルカリホスファターゼ(ＢＡＰ)で６５℃にて
３０秒間処理し、フェノールＣＨＣl3抽出し、エタノー
ル沈澱させた。
【０１０１】Ｌ鎖配列１部を含有するＤＮＡ断片を次の
ように作成した:７μgのpＫ１７ＫＧ４ＤＮＡをＰstＩ
で消化しcＤＮＡ挿入物を含有するκ鎖を６％ゲル電気
泳動及び電気溶出によって単離した。フェノール／ＣＨ
Ｃl3抽出、エタノール沈澱及び水中への再懸濁の後、こ
の断片をＡvaＩＩによって消化した。３３３bpのＰstＩ
−ＡvaＩＩ ＤＮＡ断片を単離し、６％ポリアクリルア
ミドゲルから精製した。
ように作成した:７μgのpＫ１７ＫＧ４ＤＮＡをＰstＩ
で消化しcＤＮＡ挿入物を含有するκ鎖を６％ゲル電気
泳動及び電気溶出によって単離した。フェノール／ＣＨ
Ｃl3抽出、エタノール沈澱及び水中への再懸濁の後、こ
の断片をＡvaＩＩによって消化した。３３３bpのＰstＩ
−ＡvaＩＩ ＤＮＡ断片を単離し、６％ポリアクリルア
ミドゲルから精製した。
【０１０２】１５ヌクレオチドＤＮＡプライマーをホス
ホトリエステル法(Ｇ．Ｏ．２,６４４,４３２(上記))に
より合成し、次の配列を有した:
ホトリエステル法(Ｇ．Ｏ．２,６４４,４３２(上記))に
より合成し、次の配列を有した:
【０１０３】５'メチオニンは開始コドンとして作用す
る。５００ngのこのプライマーを０．５mＭ ＡＴＰを
含有する２０μlの反応液中で１０ユニットのＴ４ＤＮ
Ａキナーゼにより５'末端で燐酸化した。約２００ngの
ＰstＩ−ＡvaＩＩ ＤＮＡ断片を２０μlの燐酸化した
プライマーと混合し、９５℃まで３分間加熱し、ドライ
アイスエタノール浴中で急速に凍結させた。変性したＤ
ＮＡ溶液を６０mＭ ＮaＣl,７mＭ ＭgＣl2,７mＭトリ
スＨＣl(pＨ７．４),１２mＭの各dＮＴＰと成し、１２
ユニットのＤＮＡポリメラーゼＩ−大断片を加えた。３
７℃にて２時間培養した後、このプライマー修復反応物
をフェノール／ＣＨＣl3で抽出し、エタノール沈澱させ
てＳau３Ａで完全に消化した。次いで、反応混合物を６
％ポリアクリルアミドゲルで電気泳動にかけ、電気溶出
の後にＳau３Ａに対し平滑末端の１８２塩基対アミノ末
端断片(断片２)の約５０ngを得た。
る。５００ngのこのプライマーを０．５mＭ ＡＴＰを
含有する２０μlの反応液中で１０ユニットのＴ４ＤＮ
Ａキナーゼにより５'末端で燐酸化した。約２００ngの
ＰstＩ−ＡvaＩＩ ＤＮＡ断片を２０μlの燐酸化した
プライマーと混合し、９５℃まで３分間加熱し、ドライ
アイスエタノール浴中で急速に凍結させた。変性したＤ
ＮＡ溶液を６０mＭ ＮaＣl,７mＭ ＭgＣl2,７mＭトリ
スＨＣl(pＨ７．４),１２mＭの各dＮＴＰと成し、１２
ユニットのＤＮＡポリメラーゼＩ−大断片を加えた。３
７℃にて２時間培養した後、このプライマー修復反応物
をフェノール／ＣＨＣl3で抽出し、エタノール沈澱させ
てＳau３Ａで完全に消化した。次いで、反応混合物を６
％ポリアクリルアミドゲルで電気泳動にかけ、電気溶出
の後にＳau３Ａに対し平滑末端の１８２塩基対アミノ末
端断片(断片２)の約５０ngを得た。
【０１０４】１００ngの断片１(上記)と５０ngの断片２
とを２０mＭトリスＨＣl(pＨ７．５),１０mＭ ＭgＣ
l2,１０mＭ ＤＴＴ,２．５mＭ ＡＴＰ及び１ユニット
のＴ４ＤＮＡリガーゼの２０μlに於いて合せた。１４
℃にて１晩結合させた後、この反応物をＥ．coli Ｋ１
２菌株２９４で形質転換した。多数のアンピシリン耐性
形質転換体からのプラスミドＤＮＡの制限エンドヌクレ
アーゼ消化は適正な作成を示し、ＤＮＡ配列分析はこの
新規なプラスミドpＫＣＥＡＩnt１の開始コドンを介し
て所望のヌクレオチド配列を証明した(図２０、図２１
および図２２)。
とを２０mＭトリスＨＣl(pＨ７．５),１０mＭ ＭgＣ
l2,１０mＭ ＤＴＴ,２．５mＭ ＡＴＰ及び１ユニット
のＴ４ＤＮＡリガーゼの２０μlに於いて合せた。１４
℃にて１晩結合させた後、この反応物をＥ．coli Ｋ１
２菌株２９４で形質転換した。多数のアンピシリン耐性
形質転換体からのプラスミドＤＮＡの制限エンドヌクレ
アーゼ消化は適正な作成を示し、ＤＮＡ配列分析はこの
新規なプラスミドpＫＣＥＡＩnt１の開始コドンを介し
て所望のヌクレオチド配列を証明した(図２０、図２１
および図２２)。
【０１０５】κＬ鎖遺伝子のコード化配列の残部は次の
ように作成した:７μgのＫ１７Ｇ７ＤＮＡからのＰstＩ
cＤＮＡ挿入物断片をＡvaＩＩで部分消化させ、ＡvaＩ
Ｉ付着末端をＤＮＡポリメラーゼＩ大断片反応に於いて
平滑末端部まで延長させた。６％ポリアクリルアミドゲ
ル電気泳動に続き、６８６塩基対のＰstＩ−平滑末端Ａ
vaＩＩＤＮＡ断片を単離し、精製し、ＨpaＩＩ制限エン
ドヌクレアーゼ消化にかけた。４９７塩基対のＨpaＩＩ
−平滑末端ＡvaＩＩ ＤＮＡ断片(断片３)を単離し、ゲ
ル電気泳動の後に精製した。
ように作成した:７μgのＫ１７Ｇ７ＤＮＡからのＰstＩ
cＤＮＡ挿入物断片をＡvaＩＩで部分消化させ、ＡvaＩ
Ｉ付着末端をＤＮＡポリメラーゼＩ大断片反応に於いて
平滑末端部まで延長させた。６％ポリアクリルアミドゲ
ル電気泳動に続き、６８６塩基対のＰstＩ−平滑末端Ａ
vaＩＩＤＮＡ断片を単離し、精製し、ＨpaＩＩ制限エン
ドヌクレアーゼ消化にかけた。４９７塩基対のＨpaＩＩ
−平滑末端ＡvaＩＩ ＤＮＡ断片(断片３)を単離し、ゲ
ル電気泳動の後に精製した。
【０１０６】１０μgのpＫＣＥＡＩnt１ＤＮＡをＡvaＩ
で消化し、ＤＮＡポリメラーゼＩ大断片で延長化し、Ｘ
baＩで消化した。大平滑末端ＡvaＩ−ＸbaＩベクター断
片と、小平滑末端ＡvaＩ−ＸbaＩ断片とを単離し、６％
ポリアクリルアミドゲルから電気泳動の後に精製した。
大ベクター断片(断片４)を細菌性アルカリホスファター
ゼ(ＢＡＰ)で処理し、小断片をＨpaＩＩで消化させ、６
％ポリアクリルアミドゲルで電気泳動にかけ、１６９塩
基対のＸbaＩ−ＨpaＩＩＤＮＡ断片(断片５)を精製し
た。約７５ngの断片４と約５０ngの断片３と約５０ngの
断片５とをＴ４ＤＮＡリガーゼ反応物中であわせ、１４
℃にて１晩培養し、反応混合物をＥ．coliＫ１２菌株２
９４で形質転換した。６種のアンピシリン耐性形質転換
体からのプラスミドＤＮＡを制限エンドヌクレアーゼ消
化により分析した１種のプラスミドＤＮＡは適正な作成
を示し、これをpＫＣＥＡＩnt２と命名した。
で消化し、ＤＮＡポリメラーゼＩ大断片で延長化し、Ｘ
baＩで消化した。大平滑末端ＡvaＩ−ＸbaＩベクター断
片と、小平滑末端ＡvaＩ−ＸbaＩ断片とを単離し、６％
ポリアクリルアミドゲルから電気泳動の後に精製した。
大ベクター断片(断片４)を細菌性アルカリホスファター
ゼ(ＢＡＰ)で処理し、小断片をＨpaＩＩで消化させ、６
％ポリアクリルアミドゲルで電気泳動にかけ、１６９塩
基対のＸbaＩ−ＨpaＩＩＤＮＡ断片(断片５)を精製し
た。約７５ngの断片４と約５０ngの断片３と約５０ngの
断片５とをＴ４ＤＮＡリガーゼ反応物中であわせ、１４
℃にて１晩培養し、反応混合物をＥ．coliＫ１２菌株２
９４で形質転換した。６種のアンピシリン耐性形質転換
体からのプラスミドＤＮＡを制限エンドヌクレアーゼ消
化により分析した１種のプラスミドＤＮＡは適正な作成
を示し、これをpＫＣＥＡＩnt２と命名した。
【０１０７】最終的な作成は、pＫＣＥＡＩnt２からのt
rpプロモーターを含むＫ−ＣＥＡ断片をpＢＲ３２２(Ｘ
ＡＰ)中へ結合することにより行なった(pＢＲ３２２(Ｘ
ＡＰ)は１９８２年１２月２２日付出願の米国特許出願
第４５２,２２７号明細書に記載されたように、pＢＲ３
２２からＡvaＩ−ＰvaＩＩ断片の削除(欠失)に続く結合
によって作成した)。
rpプロモーターを含むＫ−ＣＥＡ断片をpＢＲ３２２(Ｘ
ＡＰ)中へ結合することにより行なった(pＢＲ３２２(Ｘ
ＡＰ)は１９８２年１２月２２日付出願の米国特許出願
第４５２,２２７号明細書に記載されたように、pＢＲ３
２２からＡvaＩ−ＰvaＩＩ断片の削除(欠失)に続く結合
によって作成した)。
【０１０８】Ｋ−ＣＥＡ断片は、pＫＣＥＡＩnt２をＡv
aＩで処理し、ＤＮＡポリメラーゼＩ(Ｋlenow断片)によ
りdＮＴＰの存在下で平滑末端化させ、ＰstＩで消化
し、ゲル電気泳動と電気溶出とにより所望断片を単離し
て作成した。
aＩで処理し、ＤＮＡポリメラーゼＩ(Ｋlenow断片)によ
りdＮＴＰの存在下で平滑末端化させ、ＰstＩで消化
し、ゲル電気泳動と電気溶出とにより所望断片を単離し
て作成した。
【０１０９】pＢＲ３２２(ＸＡＰ)からの大型ベクター
断片は、ＥcoＲＩによる処理、ポリメラーゼによる平滑
末端化及びＰstＩによる再消化に続いて、電気泳動と電
気溶出とによる大型ベクター断片の単離という順序の処
理によって作成した。
断片は、ＥcoＲＩによる処理、ポリメラーゼによる平滑
末端化及びＰstＩによる再消化に続いて、電気泳動と電
気溶出とによる大型ベクター断片の単離という順序の処
理によって作成した。
【０１１０】上記のように作成したＫ−ＣＥＡ断片とを
Ｔ４ＤＮＡリガーゼにより結合させ、結合混合物をＥ．
coliに上記のように形質転換させた。数種のアンピシリ
ン耐性形質転換体からのプラスミドＤＮＡを分析用に選
択し、１種のプラスミドＤＮＡが適正な作成を示し、こ
れをpＫＣＥＡtrp２０７−１＊と命名した。
Ｔ４ＤＮＡリガーゼにより結合させ、結合混合物をＥ．
coliに上記のように形質転換させた。数種のアンピシリ
ン耐性形質転換体からのプラスミドＤＮＡを分析用に選
択し、１種のプラスミドＤＮＡが適正な作成を示し、こ
れをpＫＣＥＡtrp２０７−１＊と命名した。
【０１１１】Ｅ．１．８．ネズミ成熟抗体−ＣＥＡＨ鎖
(γＩ鎖)遺伝子を直接発現するためのプラスミドベクタ
ーの作成、pγＣＥＡtrp２０７−１＊ 図２３、図２４および図２５はpγＣＥＡtrp２０７−１
＊の作成を示している。このプラスミドは、γ１遺伝子
のＣ−末端領域の作成で始まる２つの部分に於いて作成
した。
(γＩ鎖)遺伝子を直接発現するためのプラスミドベクタ
ーの作成、pγＣＥＡtrp２０７−１＊ 図２３、図２４および図２５はpγＣＥＡtrp２０７−１
＊の作成を示している。このプラスミドは、γ１遺伝子
のＣ−末端領域の作成で始まる２つの部分に於いて作成
した。
【０１１２】５μgのプラスミドpＨＧＨ２０７−１＊を
ＡvaＩで消化し、ＤＮＡポリメラーゼＩ大型断片(Ｋlen
ow断片)で平滑末端まで延長化し、フェノール／ＣＨＣl
3で抽出し、エタノール沈澱させた。ＤＮＡをＢamＨＩ
で消化し、ＢＡＰで処理し大型断片(断片Ａ)を６％ポリ
アクリルアミドゲル電気泳動及び電気溶出により精製し
た。
ＡvaＩで消化し、ＤＮＡポリメラーゼＩ大型断片(Ｋlen
ow断片)で平滑末端まで延長化し、フェノール／ＣＨＣl
3で抽出し、エタノール沈澱させた。ＤＮＡをＢamＨＩ
で消化し、ＢＡＰで処理し大型断片(断片Ａ)を６％ポリ
アクリルアミドゲル電気泳動及び電気溶出により精製し
た。
【０１１３】約５μgのpγ１１をＰstＩにより消化し、
そして遺伝子のＣ末端部分を有するγ鎖cＤＮＡ挿入物
切断片を精製し、ＡvaＩＩで消化し、次いでＡvaＩＩ付
着端部をクノールで延長化し、次いでＴaqＩの消化を行
なった。３７５塩基対の平滑端ＡvaＩＩ−ＴaqＩ断片
(断片Ｂ)を単離し、そしてゲル電気泳動および電気溶出
により精製した。
そして遺伝子のＣ末端部分を有するγ鎖cＤＮＡ挿入物
切断片を精製し、ＡvaＩＩで消化し、次いでＡvaＩＩ付
着端部をクノールで延長化し、次いでＴaqＩの消化を行
なった。３７５塩基対の平滑端ＡvaＩＩ−ＴaqＩ断片
(断片Ｂ)を単離し、そしてゲル電気泳動および電気溶出
により精製した。
【０１１４】９μgのpγ２９８をＴaqＩ及びＢamＨＩで
消化して４９６塩基対断片(断片Ｃ)を単離した。
消化して４９６塩基対断片(断片Ｃ)を単離した。
【０１１５】ほぼ等モル量の断片Ａ,Ｂ及びＣを２０μl
の反応混合物中で１４℃にて１晩結合させ、Ｅ．coli菌
株２９４に形質転換させた。６種のアンピシリン耐性形
質転換体からのプラスミドＤＮＡを制限エンドヌクレア
ーゼ分析にかけ、pγＣＥＡＩntと命名した１種のプラ
スミドＤＮＡはγ１のＣ−末端部分の正確な作成を示し
た(図１５、図１６、図１７、図１８および図１９)。
の反応混合物中で１４℃にて１晩結合させ、Ｅ．coli菌
株２９４に形質転換させた。６種のアンピシリン耐性形
質転換体からのプラスミドＤＮＡを制限エンドヌクレア
ーゼ分析にかけ、pγＣＥＡＩntと命名した１種のプラ
スミドＤＮＡはγ１のＣ−末端部分の正確な作成を示し
た(図１５、図１６、図１７、図１８および図１９)。
【０１１６】Ｎ−末端配列を得るため、３０μgのpγ２
９８をＰstＩで消化し、ネズミ抗−ＣＥＡγ鎖のＮ−末
端領域をコード化する６２８塩基対のＤＮＡ断片を単離
し、精製した。この断片を更にＡluＩ及びＲsaＩで消化
して２８０塩基対断片を単離した。１５ヌクレオチドＤ
ＮＡプライマー、即ち met glu val met leu ５' ＡＴＧ ＧＡＡ ＧＴＧ ＡＴＧ ＣＴＧ ３' をホスホトリエステル法(上記)により合成した。
９８をＰstＩで消化し、ネズミ抗−ＣＥＡγ鎖のＮ−末
端領域をコード化する６２８塩基対のＤＮＡ断片を単離
し、精製した。この断片を更にＡluＩ及びＲsaＩで消化
して２８０塩基対断片を単離した。１５ヌクレオチドＤ
ＮＡプライマー、即ち met glu val met leu ５' ＡＴＧ ＧＡＡ ＧＴＧ ＡＴＧ ＣＴＧ ３' をホスホトリエステル法(上記)により合成した。
【０１１７】５メチオニンは開始コドンとして作用す
る。５００ngのこの合成オリゴマーであるプライマーを
０．５mＭ ＡＴＰを２０μlの反応混合物中に含有する
１０ユニットのＴ４ＤＮＡキナーゼと反応させて５末端
で燐酸化した。５００ngの２８０塩基対ＡluＩ−ＲsaＩ
ＤＮＡ断片を燐酸化したプライマーと混合した。この
混合物を９５℃で３分間熱変性させ、ドライアイスエタ
ノール中で急冷した。変性したＤＮＡ溶液を６０mＭ
ＮaＣl,７mＭ ＭgＣl2,７mＭトリスＨＣl(pＨ７．４),
１２mＭの各dＮＴＰとなし、１２ユニットのＤＮＡポリ
メラーゼＩ−大型断片を加えた。３７℃で２時間培養し
た後、このプライマー修復反応物をフェノール／ＣＨＣ
l3で抽出し、エタノール沈澱させ、ＨpaＩＩで完全消化
させた。予想された１２５塩基対の平滑末端−ＨpaＩＩ
ＤＮＡ断片(断片Ｄ)５０ngをゲルから精製した。
る。５００ngのこの合成オリゴマーであるプライマーを
０．５mＭ ＡＴＰを２０μlの反応混合物中に含有する
１０ユニットのＴ４ＤＮＡキナーゼと反応させて５末端
で燐酸化した。５００ngの２８０塩基対ＡluＩ−ＲsaＩ
ＤＮＡ断片を燐酸化したプライマーと混合した。この
混合物を９５℃で３分間熱変性させ、ドライアイスエタ
ノール中で急冷した。変性したＤＮＡ溶液を６０mＭ
ＮaＣl,７mＭ ＭgＣl2,７mＭトリスＨＣl(pＨ７．４),
１２mＭの各dＮＴＰとなし、１２ユニットのＤＮＡポリ
メラーゼＩ−大型断片を加えた。３７℃で２時間培養し
た後、このプライマー修復反応物をフェノール／ＣＨＣ
l3で抽出し、エタノール沈澱させ、ＨpaＩＩで完全消化
させた。予想された１２５塩基対の平滑末端−ＨpaＩＩ
ＤＮＡ断片(断片Ｄ)５０ngをゲルから精製した。
【０１１８】第２の部分のpγ２９８ＤＮＡをＰstＩで
消化し、６２８塩基対のＤＮＡ断片をポリアクリルアミ
ドゲル電気泳動で精製し、更にＢamＨＩ及びＨpaＩＩで
消化した。得られた３８０塩基対断片(断片Ｅ)をゲル電
気泳動により精製した。
消化し、６２８塩基対のＤＮＡ断片をポリアクリルアミ
ドゲル電気泳動で精製し、更にＢamＨＩ及びＨpaＩＩで
消化した。得られた３８０塩基対断片(断片Ｅ)をゲル電
気泳動により精製した。
【０１１９】５μgのpγＣＥＡＩnt１をＥcoＲＩで消化
し、付着末端をＤＮＡポリメラーゼＩ(Ｋlenow)と整列
させ、ＢamＨＩで消化し、ＢＡＰで処理し、６％ポリア
クリルアミドゲル電気泳動にかけた。大型ベクター断片
(断片Ｆ)を単離し、精製した。
し、付着末端をＤＮＡポリメラーゼＩ(Ｋlenow)と整列
させ、ＢamＨＩで消化し、ＢＡＰで処理し、６％ポリア
クリルアミドゲル電気泳動にかけた。大型ベクター断片
(断片Ｆ)を単離し、精製した。
【０１２０】３つの断片の結合に於いて、５０ngの断片
Ｄと１００ngの断片Ｅと１００ngの断片Ｆとを４℃にて
２０μlの反応混合物中で１晩結合させ、これを使用し
てＥ．coli Ｋ１２菌株２９４を形質転換させた。１２
種のアンピシリン耐性形質転換体からのプラスミドＤＮ
Ａを正確な作成につき分析し、開始コドンを包囲するヌ
クレオチド配列がpγＣＥＡＩnt２と命名したプラスミ
ドにつき正確であることが証明された。
Ｄと１００ngの断片Ｅと１００ngの断片Ｆとを４℃にて
２０μlの反応混合物中で１晩結合させ、これを使用し
てＥ．coli Ｋ１２菌株２９４を形質転換させた。１２
種のアンピシリン耐性形質転換体からのプラスミドＤＮ
Ａを正確な作成につき分析し、開始コドンを包囲するヌ
クレオチド配列がpγＣＥＡＩnt２と命名したプラスミ
ドにつき正確であることが証明された。
【０１２１】Ｈ鎖遺伝子の発現に使用した発現プラスミ
ドpγＣＥＡtrp２０７−１は、pＢＲ３２２(ＸＡＰ)(上
記)からの大型ベクター断片と、pγＣＥＡＩnt２から作
成した２種の断片とを用いて３つの結合により作成す
る。
ドpγＣＥＡtrp２０７−１は、pＢＲ３２２(ＸＡＰ)(上
記)からの大型ベクター断片と、pγＣＥＡＩnt２から作
成した２種の断片とを用いて３つの結合により作成す
る。
【０１２２】pＢＲ３２２(ＸＡＰ)を上記のようにＥco
ＲＩで消化し、ＤＮＡポリメラーゼ(Ｋlenow)によりdＮ
ＴＰの存在下で平滑末端化させ、次いでＰstＩにより処
理し、ゲル電気泳動で大型ベクター断片を単離すること
により処理した。Ｈ鎖遺伝子のＮ−末端コード化領域と
結合したtrpプロモーターを含有するpγＣＥＡＩnt２か
らの１５４３塩基対断片を単離し、その際pγＣＥＡＩn
t２をＰstＩに続き、ＢamＨＩで処理し、所望の断片を
ＰＡＧＥにより単離した。遺伝子のＣ−末端コード化部
分を含有する８６９塩基対断片をＡvaＩによるpγＣＥ
ＡＩnt２の部分消化、Ｋlenowによる平滑末端化及びＢa
mＨＩによる消化、次いでゲル電気泳動による所望断片
の精製によって作成した。
ＲＩで消化し、ＤＮＡポリメラーゼ(Ｋlenow)によりdＮ
ＴＰの存在下で平滑末端化させ、次いでＰstＩにより処
理し、ゲル電気泳動で大型ベクター断片を単離すること
により処理した。Ｈ鎖遺伝子のＮ−末端コード化領域と
結合したtrpプロモーターを含有するpγＣＥＡＩnt２か
らの１５４３塩基対断片を単離し、その際pγＣＥＡＩn
t２をＰstＩに続き、ＢamＨＩで処理し、所望の断片を
ＰＡＧＥにより単離した。遺伝子のＣ−末端コード化部
分を含有する８６９塩基対断片をＡvaＩによるpγＣＥ
ＡＩnt２の部分消化、Ｋlenowによる平滑末端化及びＢa
mＨＩによる消化、次いでゲル電気泳動による所望断片
の精製によって作成した。
【０１２３】上記３種の断片を標準条件下でＴ４ＤＮＡ
リガーゼを用いて結合させ、結合混合物を使用してＥ．
coli菌株２９４を形質転換させた。数種のテトラサイク
リン耐性形質転換体からのプラスミドＤＮＡを分析し、
そのうち１種のプラスミドＤＮＡが適正な作成を示し、
これをpγＣＥＡtrp２０７−１と命名した。
リガーゼを用いて結合させ、結合混合物を使用してＥ．
coli菌株２９４を形質転換させた。数種のテトラサイク
リン耐性形質転換体からのプラスミドＤＮＡを分析し、
そのうち１種のプラスミドＤＮＡが適正な作成を示し、
これをpγＣＥＡtrp２０７−１と命名した。
【０１２４】Ｅ．１．９．Ｅ．coliによる免疫グロブリ
ンの鎖の産生 Ｅ．coli 菌株(Ｗ３１１０−ＡＴＣＣ Ｎo．２７３２
５)を標準技術によりpγＣＥＡtrp２０７−１又はpＫＣ
ＥＡtrp２０７−１で形質転換させた。
ンの鎖の産生 Ｅ．coli 菌株(Ｗ３１１０−ＡＴＣＣ Ｎo．２７３２
５)を標準技術によりpγＣＥＡtrp２０７−１又はpＫＣ
ＥＡtrp２０７−１で形質転換させた。
【０１２５】二重形質転換体を得るため、Ｅ．coli菌株
Ｗ３１１０細胞を予めamp遺伝子からのＰstＩ−ＰvuＩ
断片の開裂及び再結合によって改変させた改変pＫＣＥ
Ａtrp２０７−１及びpＫＣＥＡtrp２０７−１△で形質
転換させた。pＫＣＥＡtrp２０７−１△で形質転換させ
た細胞はアンピシリンに対し感受性であるが、テトラサ
イクリンに対し耐性である。成功した形質転換体をアン
ピシリンに対する耐性を付与するがテトラサイクリンに
対する耐性を付与しないpγＣＥＡＩnt２を用いて再び
形質転換させた。pＫＣＥＡtrp２０７−１△及びpγＣ
ＥＡＩnt２の両者を含有する細胞は、アンピシリンとテ
トラサイクリンとの両者を含有する培地中での増殖によ
り同定した。
Ｗ３１１０細胞を予めamp遺伝子からのＰstＩ−ＰvuＩ
断片の開裂及び再結合によって改変させた改変pＫＣＥ
Ａtrp２０７−１及びpＫＣＥＡtrp２０７−１△で形質
転換させた。pＫＣＥＡtrp２０７−１△で形質転換させ
た細胞はアンピシリンに対し感受性であるが、テトラサ
イクリンに対し耐性である。成功した形質転換体をアン
ピシリンに対する耐性を付与するがテトラサイクリンに
対する耐性を付与しないpγＣＥＡＩnt２を用いて再び
形質転換させた。pＫＣＥＡtrp２０７−１△及びpγＣ
ＥＡＩnt２の両者を含有する細胞は、アンピシリンとテ
トラサイクリンとの両者を含有する培地中での増殖によ
り同定した。
【０１２６】形質転換細胞に於けるＨ鎖及び／又はＬ鎖
の産生を確認するため、細胞試料を１０μg／mlのテト
ラサイクリンを含有し、トリプトファンを含有しないＭ
９培地に接種し、ＯＤ５５０が０．５の読みとなるまで
インドールアクリル酸(ＩＡＡ)で誘発させた。誘発細胞
を種々の時間に亘り、３７℃で増殖させ、次いで遠心分
離し、２％ＳＤＳと０．１Ｍ β−メルカプトエタノー
ルとを含有するＴＥ緩衝液中に懸濁させ、５分間煮沸し
た。１０倍容量のアセトンを加え、細胞を２２℃に１０
分間保ち、次いで１２,０００rpmにて遠心分離した。沈
澱物をＰ．Ｈ．ＯＦarrell,Ｊ．Ｂiol．Ｃhem．,２５
０:４００７(１９７５)によるＳＤＳ試料緩衝液に懸濁
させた。３分間煮沸し、再び遠心分離し、ＳＤＳのＰＡ
ＧＥ(１０％)を用いて分画し、銀染色剤により染色し
(Ｄ．Ｇoldman et al．,Ｓcience,２１１:１４３７(１
９８１)）、又はＬ鎖とＨ鎖とを同定するため、ウサギ
抗−ネズミＩgＧを用いてウェスタンプロット(Ｗestern
blot)にかけた(Ｗ．Ｎ．Ｂurnett et al．,Ａnal．Ｂi
ochem．,１１２:１９５(１９８１))。
の産生を確認するため、細胞試料を１０μg／mlのテト
ラサイクリンを含有し、トリプトファンを含有しないＭ
９培地に接種し、ＯＤ５５０が０．５の読みとなるまで
インドールアクリル酸(ＩＡＡ)で誘発させた。誘発細胞
を種々の時間に亘り、３７℃で増殖させ、次いで遠心分
離し、２％ＳＤＳと０．１Ｍ β−メルカプトエタノー
ルとを含有するＴＥ緩衝液中に懸濁させ、５分間煮沸し
た。１０倍容量のアセトンを加え、細胞を２２℃に１０
分間保ち、次いで１２,０００rpmにて遠心分離した。沈
澱物をＰ．Ｈ．ＯＦarrell,Ｊ．Ｂiol．Ｃhem．,２５
０:４００７(１９７５)によるＳＤＳ試料緩衝液に懸濁
させた。３分間煮沸し、再び遠心分離し、ＳＤＳのＰＡ
ＧＥ(１０％)を用いて分画し、銀染色剤により染色し
(Ｄ．Ｇoldman et al．,Ｓcience,２１１:１４３７(１
９８１)）、又はＬ鎖とＨ鎖とを同定するため、ウサギ
抗−ネズミＩgＧを用いてウェスタンプロット(Ｗestern
blot)にかけた(Ｗ．Ｎ．Ｂurnett et al．,Ａnal．Ｂi
ochem．,１１２:１９５(１９８１))。
【０１２７】pγＣＥＡtrp２０７−１で形質転換させた
細胞は、ＳＤＳ ＰＡＧＥに於いてＨ鎖の分子量に相当
するバンドを示し、これは銀染色により展開された。p
ＫＣＥＡtrp２０７−１で形質転換させた細胞はＬ鎖に
対する適正な分子量バンドを示し、ウェスタンブロット
により同定された。二重形質転換細胞は、ウェスタンブ
ロットによりウサギ抗−ネズミＩgＧを用いて展開した
場合、Ｈ鎖とＬ鎖との両者の分子量蛋白質に対するバン
ドを示した。これらを図２６、図２７及び図２８に示
す。
細胞は、ＳＤＳ ＰＡＧＥに於いてＨ鎖の分子量に相当
するバンドを示し、これは銀染色により展開された。p
ＫＣＥＡtrp２０７−１で形質転換させた細胞はＬ鎖に
対する適正な分子量バンドを示し、ウェスタンブロット
により同定された。二重形質転換細胞は、ウェスタンブ
ロットによりウサギ抗−ネズミＩgＧを用いて展開した
場合、Ｈ鎖とＬ鎖との両者の分子量蛋白質に対するバン
ドを示した。これらを図２６、図２７及び図２８に示
す。
【０１２８】図２６は、pγＣＥＡtrp２０７−１で形質
転換させた細胞から銀染色により展開した結果を示して
いる。レーン１はＣＥＡ．６６−Ｅ３からのモノクロー
ナル抗−ＣＥＡＨ鎖(標準)である。レーン２b−５bはＩ
ＡＡ添加後２時間、４時間、６時間及び２４時間の経時
試料である。レーン２a−５aは対応する未形質転換比較
であり、レーン２c−５cは対応する未誘発形質転換体で
ある。
転換させた細胞から銀染色により展開した結果を示して
いる。レーン１はＣＥＡ．６６−Ｅ３からのモノクロー
ナル抗−ＣＥＡＨ鎖(標準)である。レーン２b−５bはＩ
ＡＡ添加後２時間、４時間、６時間及び２４時間の経時
試料である。レーン２a−５aは対応する未形質転換比較
であり、レーン２c−５cは対応する未誘発形質転換体で
ある。
【０１２９】図２７は、pＫＣＥＡtrp２０７−１で形質
転換させた細胞からウェスタンブロットにより展開した
結果を示している。レーン１b−６bはＩＡＡ添加直後、
１時間、３．５時間、５時間、８時間及び２４時間後の
誘発細胞からの抽出物であり、１a−６aは対応する未誘
発比較であり、レーン７はpγＣＥＡtrp２０７−１比較
からの抽出物であり、レーン８、９及び１０はＣＥＡ．
６６−Ｅ３細胞からの種々な量の抗ＣＥＡ−κ鎖であ
る。
転換させた細胞からウェスタンブロットにより展開した
結果を示している。レーン１b−６bはＩＡＡ添加直後、
１時間、３．５時間、５時間、８時間及び２４時間後の
誘発細胞からの抽出物であり、１a−６aは対応する未誘
発比較であり、レーン７はpγＣＥＡtrp２０７−１比較
からの抽出物であり、レーン８、９及び１０はＣＥＡ．
６６−Ｅ３細胞からの種々な量の抗ＣＥＡ−κ鎖であ
る。
【０１３０】図２８は、ＩＡＡ添加後２４時間の二重形
質転換細胞の４種のコロニーからウェスタンブロットに
より展開した結果を示している(レーン４−７)。レーン
１−３は種々の量のモノクローナルγ鎖比較であり、レ
ーン８及び９はそれぞれ未形質転換細胞抽出物及びpγ
ＣＥＡtrp２０７−１形質転換細胞抽出物である。他の
定量分析に於いて、Ｅ．１．１０(下記)に従って増殖さ
せた凍結形質転換Ｅ．coli細胞をドデシル硫酸ナトリウ
ム(ＳＤＳ)／β−メルカプトエタノール細胞溶菌緩衝液
中で１００℃にて加熱することにより溶菌させた。１部
を種々の量のハイブリドーマ抗−ＣＥＡを加えたレーン
に隣接するＳＤＳポリアクリルアミドゲルに加えた。こ
のゲルをＮew Ｅngland Ｎuclear社からのＩ125−標識
したヒツジ抗−ネズミＩgＧ抗体を用いてウェスタンブ
ロット(Ｂurnett,上記)により展開させた。これら結果
を図２９に示す。この図は、Ｅ．coli産生物が標準ハイ
ブリドーマ鎖と共に移動することを示し、Ｅ．coliに於
ける検出し得る蛋白質分解を示さない。哺乳動物細胞か
らのＨ鎖はＥ．coli材料よりも前者がグリコシル化され
ているため僅かに重いと予想される。ハイブリドーマレ
ーンを標準として使用し、Ｈ鎖及びＬ鎖の産生につき次
の推定を行なった:
質転換細胞の４種のコロニーからウェスタンブロットに
より展開した結果を示している(レーン４−７)。レーン
１−３は種々の量のモノクローナルγ鎖比較であり、レ
ーン８及び９はそれぞれ未形質転換細胞抽出物及びpγ
ＣＥＡtrp２０７−１形質転換細胞抽出物である。他の
定量分析に於いて、Ｅ．１．１０(下記)に従って増殖さ
せた凍結形質転換Ｅ．coli細胞をドデシル硫酸ナトリウ
ム(ＳＤＳ)／β−メルカプトエタノール細胞溶菌緩衝液
中で１００℃にて加熱することにより溶菌させた。１部
を種々の量のハイブリドーマ抗−ＣＥＡを加えたレーン
に隣接するＳＤＳポリアクリルアミドゲルに加えた。こ
のゲルをＮew Ｅngland Ｎuclear社からのＩ125−標識
したヒツジ抗−ネズミＩgＧ抗体を用いてウェスタンブ
ロット(Ｂurnett,上記)により展開させた。これら結果
を図２９に示す。この図は、Ｅ．coli産生物が標準ハイ
ブリドーマ鎖と共に移動することを示し、Ｅ．coliに於
ける検出し得る蛋白質分解を示さない。哺乳動物細胞か
らのＨ鎖はＥ．coli材料よりも前者がグリコシル化され
ているため僅かに重いと予想される。ハイブリドーマレ
ーンを標準として使用し、Ｈ鎖及びＬ鎖の産生につき次
の推定を行なった:
【０１３１】 (細胞１g当り)Ｅ．coli (Ｗ３１１０／pγＣＥＡtrp２０７−１＊) ５mgγＥ．coli (Ｗ３１１０／pＫＣＥＡtrp２０７−１＊) １．５mgκＥ．coli (Ｗ３１１０／pＫＣＥＡtrp２０７−１＊△, pγＣＥＡＩnt２) ０．５mgκ,１．０mgγ
【０１３２】Ｅ．１．１０．組換κ鎖及びγ鎖からの抗
体の再編成 再編成用のＨ鎖及びＬ鎖調製物を得るため、形質転換細
胞を大型バッチで増殖させ、収穫し、凍結させた。種々
形質転換させた細胞の増殖条件は次の通りとした:
体の再編成 再編成用のＨ鎖及びＬ鎖調製物を得るため、形質転換細
胞を大型バッチで増殖させ、収穫し、凍結させた。種々
形質転換させた細胞の増殖条件は次の通りとした:
【０１３３】Ｅ．coli(Ｗ３１１０／pγＣＥＡtrp２０
７−１＊)を５μg／mlのテトラサイクリンを含有する５
００mlのＬＢ培地に接種し、回転振盪器で８時間増殖さ
せた。次いで、培養物を酵母栄養分、塩、グルコース及
び２μg／mlのテトラサイクリンを含有する１０lの発酵
培地に移した。増殖の際にグルコースを追加し、ＯＤ５
５０＝２０にてインドールアクリル酸(ＩＡＡ)、即ち、
trpデプレッサーを５０μg／mlの濃度まで加えた。細胞
に追加グルコースを最終ＯＤ５５０＝４０まで供給し、
これはＩＡＡを加えてから約６時間で達成された。
７−１＊)を５μg／mlのテトラサイクリンを含有する５
００mlのＬＢ培地に接種し、回転振盪器で８時間増殖さ
せた。次いで、培養物を酵母栄養分、塩、グルコース及
び２μg／mlのテトラサイクリンを含有する１０lの発酵
培地に移した。増殖の際にグルコースを追加し、ＯＤ５
５０＝２０にてインドールアクリル酸(ＩＡＡ)、即ち、
trpデプレッサーを５０μg／mlの濃度まで加えた。細胞
に追加グルコースを最終ＯＤ５５０＝４０まで供給し、
これはＩＡＡを加えてから約６時間で達成された。
【０１３４】pＫＣＥＡtrp２０７−１＊で形質転換させ
たＥ．coli(Ｗ３１１０)細胞とpＫＣＥＡtrp２０７−１
＊△及びpγＣＥＡＩnt２で二重形質転換させたものと
を上記と同様に増殖させた。但し、ＩＡＡ添加後６時間
に於ける収穫時のＯＤ５５０は２５−３０であった。次
いで、これらの細胞を遠心分離により収穫し凍結した。
たＥ．coli(Ｗ３１１０)細胞とpＫＣＥＡtrp２０７−１
＊△及びpγＣＥＡＩnt２で二重形質転換させたものと
を上記と同様に増殖させた。但し、ＩＡＡ添加後６時間
に於ける収穫時のＯＤ５５０は２５−３０であった。次
いで、これらの細胞を遠心分離により収穫し凍結した。
【０１３５】Ｅ．２．再編成抗体の分析方法 抗−ＣＥＡ活性を再編成の成功に対する基準としてＥＬ
ＩＳＡにより測定した。マイクロタイタープレート(Ｄy
natech Ｉmmulon社製)のウェルにＣＥＡを飽和させ、
０．１Ｍ炭酸塩緩衝液(pＨ９．３)中の２〜５μgＣＥＡ
／ml溶液１００μlを室温で１２時間培養することによ
り行なった。次いで、これらのウェルを燐酸塩緩衝液
(ＰＢＳ)で４回洗浄し、ＰＢＳに於ける０．５％ＢＳＡ
２００μlを３７℃で２時間培養し、ＰＢＳで４回洗浄
することによりＢＳＡで飽和させた。５０μlの各試料
を各ウェルに加えた。ＰＢＳに於ける０．５％ＢＳＡ中
１０μg,５μg、５００ng、１００ng、５０ng、１０n
g、５ng及び１ngの抗−ＣＥＡ／mlの５０μl試料と、ブ
ランクとしてのＰＢＳに於ける０．５％ＢＳＡ５０μl
のみとから成る標準曲線(図３０に示す)を作成した。全
ての試料をプレート中で３７℃にて９０分間培養した。
ＩＳＡにより測定した。マイクロタイタープレート(Ｄy
natech Ｉmmulon社製)のウェルにＣＥＡを飽和させ、
０．１Ｍ炭酸塩緩衝液(pＨ９．３)中の２〜５μgＣＥＡ
／ml溶液１００μlを室温で１２時間培養することによ
り行なった。次いで、これらのウェルを燐酸塩緩衝液
(ＰＢＳ)で４回洗浄し、ＰＢＳに於ける０．５％ＢＳＡ
２００μlを３７℃で２時間培養し、ＰＢＳで４回洗浄
することによりＢＳＡで飽和させた。５０μlの各試料
を各ウェルに加えた。ＰＢＳに於ける０．５％ＢＳＡ中
１０μg,５μg、５００ng、１００ng、５０ng、１０n
g、５ng及び１ngの抗−ＣＥＡ／mlの５０μl試料と、ブ
ランクとしてのＰＢＳに於ける０．５％ＢＳＡ５０μl
のみとから成る標準曲線(図３０に示す)を作成した。全
ての試料をプレート中で３７℃にて９０分間培養した。
【０１３６】次いで、これらのプレートをＰＢＳで４回
洗浄し、ヒツジ抗−ネズミＩgＧ−アルカリホスフェー
ト(ＴＡＧＯ,Ｉnc．)をＰＢＳに於ける０．５％ＢＳＡ
中の２４ユニット／mlの酵素濃度１０μlを加えること
により各ウェルに施した。この溶液を３７℃にて９０分
間培養した。これらプレートをＰＢＳで４回洗浄した
後、基質へエタノールアミン緩衝塩(pＨ９．５)に於け
るp−ニトロフェニルホスフェート(Ｓigma社製)の０．
４mg／ml溶液１００μlを加えた。この基質を３７℃に
て９０分間培養した発色させた。
洗浄し、ヒツジ抗−ネズミＩgＧ−アルカリホスフェー
ト(ＴＡＧＯ,Ｉnc．)をＰＢＳに於ける０．５％ＢＳＡ
中の２４ユニット／mlの酵素濃度１０μlを加えること
により各ウェルに施した。この溶液を３７℃にて９０分
間培養した。これらプレートをＰＢＳで４回洗浄した
後、基質へエタノールアミン緩衝塩(pＨ９．５)に於け
るp−ニトロフェニルホスフェート(Ｓigma社製)の０．
４mg／ml溶液１００μlを加えた。この基質を３７℃に
て９０分間培養した発色させた。
【０１３７】各ウェルのＡ450を１．５の閾域、１．０
の較正値及び０．０００１に設定したＰＢＳ(Ｂlank)ウ
ェルに於ける０．５％ＢＳＡにセットしたマイクロエリ
サ・オート・リーダー(Ｍicroelisa Ａuto Ｒeader,Ｄy
natech社製)により読み取った。Ａ450のデータをＶＡＸ
系に於けるＲＳ−１で表にし、標準曲線データを４パラ
メータのロジスチックモデルに当てはめた。未知試料の
濃度をＡ450データに基いて算出した。
の較正値及び０．０００１に設定したＰＢＳ(Ｂlank)ウ
ェルに於ける０．５％ＢＳＡにセットしたマイクロエリ
サ・オート・リーダー(Ｍicroelisa Ａuto Ｒeader,Ｄy
natech社製)により読み取った。Ａ450のデータをＶＡＸ
系に於けるＲＳ−１で表にし、標準曲線データを４パラ
メータのロジスチックモデルに当てはめた。未知試料の
濃度をＡ450データに基いて算出した。
【０１３８】Ｅ．３．組換抗体の再編成及び分析 上記Ｅ．１．１０に記載したように、作成した凍結細胞
を冷溶菌緩衝液(１０mＭトリスＨＣl(pＨ７．５),１mＭ
ＥＤＴＡ,０．１Ｍ ＮaＣl,１mＭ弗化フェニルメチ
ルスルホニル(ＰＭＳＦ))に於いて解凍させ、音波処理
で溶菌させた。溶菌物を３,０００rpmにて２０分間の遠
心分離により部分清澄化させた。１mＭＰＭＳＦを追加
して蛋白質分解酵素から上清を保護し、直ちに使用する
か又は−８０℃で凍結保存した。凍結溶菌物は、決して
２回以上解凍させなかった。
を冷溶菌緩衝液(１０mＭトリスＨＣl(pＨ７．５),１mＭ
ＥＤＴＡ,０．１Ｍ ＮaＣl,１mＭ弗化フェニルメチ
ルスルホニル(ＰＭＳＦ))に於いて解凍させ、音波処理
で溶菌させた。溶菌物を３,０００rpmにて２０分間の遠
心分離により部分清澄化させた。１mＭＰＭＳＦを追加
して蛋白質分解酵素から上清を保護し、直ちに使用する
か又は−８０℃で凍結保存した。凍結溶菌物は、決して
２回以上解凍させなかった。
【０１３９】Ｅ．coliで産生した抗−ＣＥＡＨ鎖(γ)の
Ｓ−スルホン化物を次のように作成した:不溶性物体と
してＨ鎖を含有するpγＣＥＡtrp２０７−１＊で形質転
換させた組換Ｅ．coli細胞を溶菌し、上記と同様に遠心
分離した。ペレットを同じ緩衝液中に再懸濁させ、音波
処理し、再遠心分離した。このペレットを緩衝液で１回
洗浄し、６Ｍグアニジン塩酸塩,０．１ＭトリスＨＣl(p
Ｈ８),１mＭ ＥＤＴＡ,２０mg／ml亜硫酸ナトリウム及
び１０mg／mlテトラチオン酸ナトリウムに懸濁させ、２
５℃にて約１６時間反応させた。反応混合物を８Ｍ尿
素,０．１ＭトリスＨＣl(pＨ８)に対し、透析し、４℃
で貯蔵してγ−ＳＳＯ3の３mg／ml溶液を得た。
Ｓ−スルホン化物を次のように作成した:不溶性物体と
してＨ鎖を含有するpγＣＥＡtrp２０７−１＊で形質転
換させた組換Ｅ．coli細胞を溶菌し、上記と同様に遠心
分離した。ペレットを同じ緩衝液中に再懸濁させ、音波
処理し、再遠心分離した。このペレットを緩衝液で１回
洗浄し、６Ｍグアニジン塩酸塩,０．１ＭトリスＨＣl(p
Ｈ８),１mＭ ＥＤＴＡ,２０mg／ml亜硫酸ナトリウム及
び１０mg／mlテトラチオン酸ナトリウムに懸濁させ、２
５℃にて約１６時間反応させた。反応混合物を８Ｍ尿
素,０．１ＭトリスＨＣl(pＨ８)に対し、透析し、４℃
で貯蔵してγ−ＳＳＯ3の３mg／ml溶液を得た。
【０１４０】各種のＩgＧ鎖を産生する各種のＥ．coli
菌株の細胞から得られる細胞溶菌物６５０μlを５００m
gの尿素に加えた。これに２０mＭまでのβ−メルカプト
エタノールと５０mＭまでのトリスＨＣl(pＨ８．５)
と、１mＭまでのＥＤＴＡとを加え、また或る実験では
γ−ＳＳＯ3を０．１mg／mlまで加えた。２５℃で３０
〜９０分間静置した後、この反応混合物を４℃にて０．
１Ｍグリシン酸ナトリウム(pＨ１０．８),０．５Ｍ尿
素,１０mＭグリシンエチルエステル,５mＭ還元グルタチ
オン,０．１mＭ酸化グルタチオンから成り、緩衝液に対
して透析した。この緩衝液をＮ飽和した水から調製し、
透析を蓋付ウィートン瓶にて行なった。１６〜４８時間
後、透析袋を１mＭ ＰＭＳＦを含有する４℃の燐酸塩
緩衝液に移し、更に１６〜２４時間透析を続けた。透析
物をＥ．２に記載したようにＣＥＡを結合する能力につ
きＥＬＩＳＡによって分析した。下記の結果は標準曲線
と比較して得られた数値をng／ml抗−ＣＥＡとして示
す。更に、ＥＬＩＳＡ反応マイナスκ鎖のみを産生する
細胞のバックグラウンド(１０８ng／ml)から、及び反応
混合物に於けるγ及びκ鎖のレベルの推定値から計算し
た再編成効率をも示す。
菌株の細胞から得られる細胞溶菌物６５０μlを５００m
gの尿素に加えた。これに２０mＭまでのβ−メルカプト
エタノールと５０mＭまでのトリスＨＣl(pＨ８．５)
と、１mＭまでのＥＤＴＡとを加え、また或る実験では
γ−ＳＳＯ3を０．１mg／mlまで加えた。２５℃で３０
〜９０分間静置した後、この反応混合物を４℃にて０．
１Ｍグリシン酸ナトリウム(pＨ１０．８),０．５Ｍ尿
素,１０mＭグリシンエチルエステル,５mＭ還元グルタチ
オン,０．１mＭ酸化グルタチオンから成り、緩衝液に対
して透析した。この緩衝液をＮ飽和した水から調製し、
透析を蓋付ウィートン瓶にて行なった。１６〜４８時間
後、透析袋を１mＭ ＰＭＳＦを含有する４℃の燐酸塩
緩衝液に移し、更に１６〜２４時間透析を続けた。透析
物をＥ．２に記載したようにＣＥＡを結合する能力につ
きＥＬＩＳＡによって分析した。下記の結果は標準曲線
と比較して得られた数値をng／ml抗−ＣＥＡとして示
す。更に、ＥＬＩＳＡ反応マイナスκ鎖のみを産生する
細胞のバックグラウンド(１０８ng／ml)から、及び反応
混合物に於けるγ及びκ鎖のレベルの推定値から計算し
た再編成効率をも示す。
【０１４１】 ng／ml 組換 抗−ＣＥＡ ％ ＩＦＮ−αＡを産生するＥ．coli Ｗ３１１０(比較) ０ −Ｅ．coli (Ｗ３１１０／pＫＣＥＡtrp２０７−１＊) １０８ −Ｅ．coli (Ｗ３１１０／pＫＣＥＡtrp２０７−１＊) ＋γ−ＳＳＯ3 ８４８ ０．３３Ｅ．coli (Ｗ３１１０／pＫＣＥＡtrp２０７−１＊△, pγＣＥＡＩnt２) １５８０ ０．７６ ハイブリドーマ抗−ＣＥＡ κ−ＳＳＯ3 及びγ−ＳＳＯ3 ５４０ ０．４０
【０１４２】Ｅ．４．キメラ抗体の作成 図３１及び図３２はネズミ抗ＣＥＡ可変領域とヒトγ２
不変領域とから成るキメラＨ(γ)鎖のための発現ベクタ
ーの作成を示している。
不変領域とから成るキメラＨ(γ)鎖のための発現ベクタ
ーの作成を示している。
【０１４３】ヒトγ２Ｈ鎖をコード化するＤＮＡ配列は
次のように作成される:ヒト多発性骨髄腫細胞系から標
準技術により得たcＤＮＡライブラリーを５'ＧＧＧＣＡ
ＣＴＣＧＡＣＡＣＡＡ３'で検索して、ヒトγ２鎖に対
するcＤＮＡ挿入物を含有するプラスミドを得(Ｔakahas
hi et al．,Ｃell,２９:６７１(１９８２))(この文献を
引用して本明細書に包含する)、分析してヒトγ２に於
ける公知配列によりこれを同定する(Ｊ．Ｅllison et a
l．,Ｐroc．Ｎatl．Ａcad．ＵＳＡ,７９:１９８４(１９
８２)）(この文献を引用して本明細書に包含する)。
次のように作成される:ヒト多発性骨髄腫細胞系から標
準技術により得たcＤＮＡライブラリーを５'ＧＧＧＣＡ
ＣＴＣＧＡＣＡＣＡＡ３'で検索して、ヒトγ２鎖に対
するcＤＮＡ挿入物を含有するプラスミドを得(Ｔakahas
hi et al．,Ｃell,２９:６７１(１９８２))(この文献を
引用して本明細書に包含する)、分析してヒトγ２に於
ける公知配列によりこれを同定する(Ｊ．Ｅllison et a
l．,Ｐroc．Ｎatl．Ａcad．ＵＳＡ,７９:１９８４(１９
８２)）(この文献を引用して本明細書に包含する)。
【０１４４】図３１に示したように、クローン化ヒトγ
２プラスミド(pγ２)から２つの断片が得られる。第１
の断片は、ＰvuＩＩによる消化に続きＡvaＩＩＩでの消
化及び不変領域の部分を勧誘する小さいＤＮＡ断片の６
％ＰＡＧＥを用いる精製によって生ぜしめる。第２の断
片は、pγ２をγ２の３'未翻訳領域に於いて開裂する
(ヌクレオチド配列から推定される)制限酵素で消化し、
Ｋlenow及びdＮＴＰを充填し、ＡvaＩＩＩで開裂させ
て、６％ＰＡＧＥを用いて小さい方の断片を単離するこ
とにより得られる。(ＰvuＩＩ−３'未翻訳断片を供給す
るための２工程且つ２断片の組成物の選択は、３末端に
対しＡvaＩＩＩ部位が近接するため産生物に対する明確
な経路を与え、従って３'未翻訳領域部位に適合する遺
伝子配列に於ける制限部位を更に必要としない。)pγＣ
ＥＡ２０７−１をＥcoＲＩで消化し、Ｋlenow及びdＮＴ
Ｐで処理して付着性末端充填し、ＰvuＩＩで消化し、こ
の場合大きいベクター断片は６％ＰＡＧＥにより単離さ
れたプロモーターを含有する。
２プラスミド(pγ２)から２つの断片が得られる。第１
の断片は、ＰvuＩＩによる消化に続きＡvaＩＩＩでの消
化及び不変領域の部分を勧誘する小さいＤＮＡ断片の６
％ＰＡＧＥを用いる精製によって生ぜしめる。第２の断
片は、pγ２をγ２の３'未翻訳領域に於いて開裂する
(ヌクレオチド配列から推定される)制限酵素で消化し、
Ｋlenow及びdＮＴＰを充填し、ＡvaＩＩＩで開裂させ
て、６％ＰＡＧＥを用いて小さい方の断片を単離するこ
とにより得られる。(ＰvuＩＩ−３'未翻訳断片を供給す
るための２工程且つ２断片の組成物の選択は、３末端に
対しＡvaＩＩＩ部位が近接するため産生物に対する明確
な経路を与え、従って３'未翻訳領域部位に適合する遺
伝子配列に於ける制限部位を更に必要としない。)pγＣ
ＥＡ２０７−１をＥcoＲＩで消化し、Ｋlenow及びdＮＴ
Ｐで処理して付着性末端充填し、ＰvuＩＩで消化し、こ
の場合大きいベクター断片は６％ＰＡＧＥにより単離さ
れたプロモーターを含有する。
【０１４５】ネズミγ１遺伝子に於けるＰvuＩＩ部位を
包囲する位置及びＤＮＡ配列は、ヒトγ２遺伝子に於け
るＰvuＩＩ部位を包囲する位置及びＤＮＡ配列と同一で
ある。
包囲する位置及びＤＮＡ配列は、ヒトγ２遺伝子に於け
るＰvuＩＩ部位を包囲する位置及びＤＮＡ配列と同一で
ある。
【０１４６】上記断片の３方向結合から得られるプラス
ミド(pＣhim１)は、trpプロモーターの影響下で、ネズ
ミ抗−ＣＥＡγ１鎖の可変領域及び不変領域の１部並び
にγ２ヒト鎖の１部を含有する。事実、pＣhim１は、
Ｅ．coliに形質転換させた場合、キメラＨ鎖を発現する
が、ネズミからヒトへの変化は可変領域対不変領域の接
合部に於いて生じないものである。
ミド(pＣhim１)は、trpプロモーターの影響下で、ネズ
ミ抗−ＣＥＡγ１鎖の可変領域及び不変領域の１部並び
にγ２ヒト鎖の１部を含有する。事実、pＣhim１は、
Ｅ．coliに形質転換させた場合、キメラＨ鎖を発現する
が、ネズミからヒトへの変化は可変領域対不変領域の接
合部に於いて生じないものである。
【０１４７】図３２は発現により生ずる蛋白質がネズミ
抗−ＣＥＡ抗体からの可変領域とヒトγ２鎖からの不変
領域とを含有するようにpＣhim２を作成するためのpＣh
im１の改変を示している。まず、ＮcoＩで処理し、Ｋle
now及びdＮＴＰで平滑末端化させ、ＰvuＩＩにより開裂
させ、ネズミ抗−ＣＥＡに対する一定コード化領域に於
ける短セグメントを除き、殆んど完全プラスミドである
大型ベクター断片を単離することにより、pＣhim１から
断片を作成する。ＰvuＩＩで処理し、可変領域で開裂す
る任意の制限酵素で処理し、Ｋlenow及びdＮＴＰで平滑
末端化し、この連鎖の可変領域と不変領域との間の接合
部から成る短い断片を単離することにより、上記のpγ
２から第２の断片を作成する。
抗−ＣＥＡ抗体からの可変領域とヒトγ２鎖からの不変
領域とを含有するようにpＣhim２を作成するためのpＣh
im１の改変を示している。まず、ＮcoＩで処理し、Ｋle
now及びdＮＴＰで平滑末端化させ、ＰvuＩＩにより開裂
させ、ネズミ抗−ＣＥＡに対する一定コード化領域に於
ける短セグメントを除き、殆んど完全プラスミドである
大型ベクター断片を単離することにより、pＣhim１から
断片を作成する。ＰvuＩＩで処理し、可変領域で開裂す
る任意の制限酵素で処理し、Ｋlenow及びdＮＴＰで平滑
末端化し、この連鎖の可変領域と不変領域との間の接合
部から成る短い断片を単離することにより、上記のpγ
２から第２の断片を作成する。
【０１４８】上記２つの断片を結合すれば、中間的プラ
スミドが得られ、このプラスミドはネズミ抗−ＣＥＡ抗
原の不変領域の小部分と、ヒトγ鎖の可変領域の小部分
とを含有する外来ＤＮＡ断片以外には正確である。この
修復はＸbaＩ−ＰvuＩＩの断片を切断しＭessing et a
l．,Ｎucleic acids Ｒes．,９:３０９(１９８１)に記
載されたＭ１３ファージ中へクローン化させ、次いでＡ
delman et al．,ＤＮＡ,２:１８３(１９８３)に記載さ
れたように試験管内に於ける部位指向性の削除突然変異
によって行なった。このように改変させたＸbaＩ−Ｐvu
ＩＩ断片を再び中間プラスミドに結合してpＣhim２を生
成させる。このプラスミドは適当な宿主に於いて、明確
に作成されたネズミ可変領域／ヒト不変領域キメラＨ鎖
を発現することができる。
スミドが得られ、このプラスミドはネズミ抗−ＣＥＡ抗
原の不変領域の小部分と、ヒトγ鎖の可変領域の小部分
とを含有する外来ＤＮＡ断片以外には正確である。この
修復はＸbaＩ−ＰvuＩＩの断片を切断しＭessing et a
l．,Ｎucleic acids Ｒes．,９:３０９(１９８１)に記
載されたＭ１３ファージ中へクローン化させ、次いでＡ
delman et al．,ＤＮＡ,２:１８３(１９８３)に記載さ
れたように試験管内に於ける部位指向性の削除突然変異
によって行なった。このように改変させたＸbaＩ−Ｐvu
ＩＩ断片を再び中間プラスミドに結合してpＣhim２を生
成させる。このプラスミドは適当な宿主に於いて、明確
に作成されたネズミ可変領域／ヒト不変領域キメラＨ鎖
を発現することができる。
【０１４９】同様にして、γ鎖でなくヒトκ鎖に対する
cＤＮＡ作成のためのmＲＮＡ鋳型を使用してキメラＬ鎖
のための発現プラスミドを作成する。
cＤＮＡ作成のためのmＲＮＡ鋳型を使用してキメラＬ鎖
のための発現プラスミドを作成する。
【０１５０】次いで、上記２つのプラスミドをＥ．coli
Ｗ３１１０に二重形質転換させ、これら細胞を増殖さ
せ、上記Ｅ．１−Ｅ．３に示したように連鎖を再編成す
る。
Ｗ３１１０に二重形質転換させ、これら細胞を増殖さ
せ、上記Ｅ．１−Ｅ．３に示したように連鎖を再編成す
る。
【０１５１】Ｅ．５．改変ネズミ抗−ＣＥＡ抗体の作成 Ｅ．５．１．改変ネズミ抗−ＣＥＡＨ鎖遺伝子の直接発
現用プラスミドベクターの作成 ネズミ抗−ＣＥＡＨ鎖の不変領域に於けるアミノ酸２１
６−２３０の区域のシステイン残基及び得られるジスル
フィド結合は、補体結合に対し重要であると思われる
(Ｋlein et al．,Ｐroc．Ｎatl．Ａcad．Ｓci．,ＵＳ
Ａ,７８:５２４(１９８１))が、得られる抗体の抗原結
合性にとっては重要でない。本発明の方法による再編成
の際、不正確なジスルフィド結合形成の可能性を減少さ
せるため、３個のシステインに対するコドンを含むアミ
ノ酸残基２３６−２３２をコードするヌクレオチドを次
のようにして欠失する:
現用プラスミドベクターの作成 ネズミ抗−ＣＥＡＨ鎖の不変領域に於けるアミノ酸２１
６−２３０の区域のシステイン残基及び得られるジスル
フィド結合は、補体結合に対し重要であると思われる
(Ｋlein et al．,Ｐroc．Ｎatl．Ａcad．Ｓci．,ＵＳ
Ａ,７８:５２４(１９８１))が、得られる抗体の抗原結
合性にとっては重要でない。本発明の方法による再編成
の際、不正確なジスルフィド結合形成の可能性を減少さ
せるため、３個のシステインに対するコドンを含むアミ
ノ酸残基２３６−２３２をコードするヌクレオチドを次
のようにして欠失する:
【０１５２】「デリーター(deleter,欠失剤)」デオキシオ
リゴヌクレオチド即ち５'ＣＴＡＡＣＡＣＣＡＴＧＴＣ
ＡＧＧＧＴを使用して、Ｗallace et al．,Ｓcience,２
０９:１３９６(１９８０)の方法又はＡdelman et al．,
ＤＮＡ,２:１８３(１９８３)の方法によってpγＣＥＡt
rp２０７−１＊から遺伝子の適切な部分を欠失させる。
要するに、「デリーター」デオキシオリゴヌクレオチドを
変性pγＣＥＡtrp２０７−１＊ＤＮＡと共にアニール
し、プライマー修復合成をin vitroで行ない、次いでＰ
32標識したデリーター配列と推定欠失クローンとのハイ
ブリゼーションにより選別(screening)する。
リゴヌクレオチド即ち５'ＣＴＡＡＣＡＣＣＡＴＧＴＣ
ＡＧＧＧＴを使用して、Ｗallace et al．,Ｓcience,２
０９:１３９６(１９８０)の方法又はＡdelman et al．,
ＤＮＡ,２:１８３(１９８３)の方法によってpγＣＥＡt
rp２０７−１＊から遺伝子の適切な部分を欠失させる。
要するに、「デリーター」デオキシオリゴヌクレオチドを
変性pγＣＥＡtrp２０７−１＊ＤＮＡと共にアニール
し、プライマー修復合成をin vitroで行ない、次いでＰ
32標識したデリーター配列と推定欠失クローンとのハイ
ブリゼーションにより選別(screening)する。
【０１５３】Ｅ．５．２．システイン欠如改変抗体の産
生 Ｅ．５．１．で作成したプラスミドを用いて、上記のよ
うに予めpＫＣＥＡtrp２０７−１＊で形質転換したＥ．
coli菌株を形質転換する。これら細胞を増殖させ、組換
抗体鎖を抽出し、Ｅ．１．１０．に記載したように改変
抗体を再編成する。
生 Ｅ．５．１．で作成したプラスミドを用いて、上記のよ
うに予めpＫＣＥＡtrp２０７−１＊で形質転換したＥ．
coli菌株を形質転換する。これら細胞を増殖させ、組換
抗体鎖を抽出し、Ｅ．１．１０．に記載したように改変
抗体を再編成する。
【０１５４】Ｅ．６．Ｆabの作成 Ｅ．６．１．ネズミ抗−ＣＥＡγ１Ｆab断片遺伝子の直
接発現用プラスミドベクターの作成:pγＣＥＡＦabtrp
２０７−１＊ 図３３はpγＣＥＡＦabtrp２０７−１＊の作成を示して
いる。５μgのpＢＲ３２２をＨindＩＩＩで消化し、Ｋl
enow及びdＮＴＰで処理して付着性末端を平滑化し、Ｐs
tＩで消化し、ＢＡＰで処理した。大ベクター断片、即
ち断片Ｉを６％ＰＡＧＥを用い、電気溶出することによ
り回収した。
接発現用プラスミドベクターの作成:pγＣＥＡＦabtrp
２０７−１＊ 図３３はpγＣＥＡＦabtrp２０７−１＊の作成を示して
いる。５μgのpＢＲ３２２をＨindＩＩＩで消化し、Ｋl
enow及びdＮＴＰで処理して付着性末端を平滑化し、Ｐs
tＩで消化し、ＢＡＰで処理した。大ベクター断片、即
ち断片Ｉを６％ＰＡＧＥを用い、電気溶出することによ
り回収した。
【０１５５】５μgのpγＣＥＡtrp２０７−１をＢamＨ
Ｉ及びＰstＩの両者で消化し、trpプロモーターと、可
変領域をコードし不変領域まで続き更に抗−ＣＥＡγ１
鎖のヒンジ領域まで続く遺伝子配列とを含有する約１５
７０bpのＤＮＡ断片(断片ＩＩ)を単離し、電気泳動の後
に精製した。
Ｉ及びＰstＩの両者で消化し、trpプロモーターと、可
変領域をコードし不変領域まで続き更に抗−ＣＥＡγ１
鎖のヒンジ領域まで続く遺伝子配列とを含有する約１５
７０bpのＤＮＡ断片(断片ＩＩ)を単離し、電気泳動の後
に精製した。
【０１５６】完全Ｈ鎖でなく、抗−ＣＥＡγ１鎖Ｆab断
片が発現されるためには、停止コドンが遺伝子中の適当
な位置に作成されることが必要である。このため、２０
μgのpγ２９８から２６０bpのＮcoＩ−ＮdeＩ ＤＮＡ
断片を単離し、精製した。１３ヌクレオチドＤＮＡプラ
イマー、即ちその相補鎖がＦab遺伝子の最後の３個のＣ
−末端アミノ酸と停止コドンに対し必要とされる３個の
うち２個の塩基とをコードするものをホスホトリエステ
ル法(上記)によって合成した。このプローブはヌクレオ
チド７５４−７６７(図９、図１０、図１１、図１２、
図１３および図１４)にハイブリダイズし、これは次の
配列を有する:
片が発現されるためには、停止コドンが遺伝子中の適当
な位置に作成されることが必要である。このため、２０
μgのpγ２９８から２６０bpのＮcoＩ−ＮdeＩ ＤＮＡ
断片を単離し、精製した。１３ヌクレオチドＤＮＡプラ
イマー、即ちその相補鎖がＦab遺伝子の最後の３個のＣ
−末端アミノ酸と停止コドンに対し必要とされる３個の
うち２個の塩基とをコードするものをホスホトリエステ
ル法(上記)によって合成した。このプローブはヌクレオ
チド７５４−７６７(図９、図１０、図１１、図１２、
図１３および図１４)にハイブリダイズし、これは次の
配列を有する:
【０１５７】停止コドンの第３塩基を上記のpＢＲ３２
２開裂物の充填ＨindＩＩＩ部位の末端ヌクレオチドに
より供給する。このプライマー５００ngを、２０μl中
に０．５mＭのＡＴＰを含有する１０ユニットのＴ４Ｄ
ＮＡキナーゼを用いる反応液中の５'末端の燐酸化によ
りプライマー修復反応に使用し、これを約２００ngのＮ
coＩ−ＮdeＩ ＤＮＡ断片と混合した。混合物を９５℃
で３分間加熱変性させ、ドライアイスエタノール中で急
冷した。この変性したＤＮＡ溶液を６０mＭ ＮaＣl,７
mＭ ＭgＣl2,７mＭトリスＨＣl(pＨ７．４),１２mＭの
各dＮＴＰとなし、１２ユニットのＤＮＡポリメラーゼ
Ｉ−大断片を加えた。３７℃で２時間インキュベーショ
ンした後、このプライマー修復反応物をフェノール／Ｃ
ＨＣl3で抽出し、エタノール沈澱し、ＢamＨＩで消化
し、反応物を６％ポリアクリルアミドゲルで電気泳動に
かけた。１８１bp平滑末端−ＢamＨＩのＤＮＡ断片、即
ち断片ＩＩＩの約５０ngを単離し、精製した。
２開裂物の充填ＨindＩＩＩ部位の末端ヌクレオチドに
より供給する。このプライマー５００ngを、２０μl中
に０．５mＭのＡＴＰを含有する１０ユニットのＴ４Ｄ
ＮＡキナーゼを用いる反応液中の５'末端の燐酸化によ
りプライマー修復反応に使用し、これを約２００ngのＮ
coＩ−ＮdeＩ ＤＮＡ断片と混合した。混合物を９５℃
で３分間加熱変性させ、ドライアイスエタノール中で急
冷した。この変性したＤＮＡ溶液を６０mＭ ＮaＣl,７
mＭ ＭgＣl2,７mＭトリスＨＣl(pＨ７．４),１２mＭの
各dＮＴＰとなし、１２ユニットのＤＮＡポリメラーゼ
Ｉ−大断片を加えた。３７℃で２時間インキュベーショ
ンした後、このプライマー修復反応物をフェノール／Ｃ
ＨＣl3で抽出し、エタノール沈澱し、ＢamＨＩで消化
し、反応物を６％ポリアクリルアミドゲルで電気泳動に
かけた。１８１bp平滑末端−ＢamＨＩのＤＮＡ断片、即
ち断片ＩＩＩの約５０ngを単離し、精製した。
【０１５８】約１００ngの断片Ｉとそれぞれ約１００ng
の断片ＩＩ及びＩＩＩを１晩結合させ、Ｅ．coli Ｋ１
２菌株２９４に形質転換した。数種のテトラサイクリン
耐性形質転換体からのプラスミドＤＮＡを適正な構成の
ものにつき分析し、修復平滑末端充填ＨindＩＩＩ接合
部を介するヌクレオチド配列を決定してＴＧＡ停止コド
ンを証明した。
の断片ＩＩ及びＩＩＩを１晩結合させ、Ｅ．coli Ｋ１
２菌株２９４に形質転換した。数種のテトラサイクリン
耐性形質転換体からのプラスミドＤＮＡを適正な構成の
ものにつき分析し、修復平滑末端充填ＨindＩＩＩ接合
部を介するヌクレオチド配列を決定してＴＧＡ停止コド
ンを証明した。
【０１５９】Ｅ．６．２．Ｆab蛋白質の産生 Ｅ．６．１で作成したプラスミドを上記のように予めp
ＫＣＥＡtrp２０７−１＊で形質転換したＥ．coli菌株
を形質転換する。これら細胞を増殖させ、組換抗体鎖に
つき抽出し、Ｆab蛋白質をＥ．１．１０に記載したよう
に再編成する。
ＫＣＥＡtrp２０７−１＊で形質転換したＥ．coli菌株
を形質転換する。これら細胞を増殖させ、組換抗体鎖に
つき抽出し、Ｆab蛋白質をＥ．１．１０に記載したよう
に再編成する。
【図１】 免疫グロブリンの一般的構造図を示す図であ
る。
る。
【図２】 κ抗ＣＥＡ鎖をコードするpＫ１７Ｇ４のcＤ
ＮＡ挿入物の詳細な配列を示す図である。
ＮＡ挿入物の詳細な配列を示す図である。
【図３】 κ抗ＣＥＡ鎖をコードするpＫ１７Ｇ４のcＤ
ＮＡ挿入物の詳細な配列を示す図である。
ＮＡ挿入物の詳細な配列を示す図である。
【図４】 κ抗ＣＥＡ鎖をコードするpＫ１７Ｇ４のcＤ
ＮＡ挿入物の詳細な配列を示す図である。
ＮＡ挿入物の詳細な配列を示す図である。
【図５】 κ抗ＣＥＡ鎖をコードするpＫ１７Ｇ４のcＤ
ＮＡ挿入物の詳細な配列を示す図である。
ＮＡ挿入物の詳細な配列を示す図である。
【図６】 対応するアミノ酸配列と共に示した図２、図
３、図４および図５の断片のコード配列を示す図であ
る。
３、図４および図５の断片のコード配列を示す図であ
る。
【図７】 対応するアミノ酸配列と共に示した図２、図
３、図４および図５の断片のコード配列を示す図であ
る。
３、図４および図５の断片のコード配列を示す図であ
る。
【図８】 対応するアミノ酸配列と共に示した図２、図
３、図４および図５の断片のコード配列を示す図であ
る。
３、図４および図５の断片のコード配列を示す図であ
る。
【図９】 γ抗ＣＥＡ鎖をコードするpγ２９８及びpγ
１１のcＤＮＡ挿入物の結合詳細配列を示す図である。
１１のcＤＮＡ挿入物の結合詳細配列を示す図である。
【図１０】 γ抗ＣＥＡ鎖をコードするpγ２９８及びp
γ１１のcＤＮＡ挿入物の結合詳細配列を示す図であ
る。
γ１１のcＤＮＡ挿入物の結合詳細配列を示す図であ
る。
【図１１】 γ抗ＣＥＡ鎖をコードするpγ２９８及びp
γ１１のcＤＮＡ挿入物の結合詳細配列を示す図であ
る。
γ１１のcＤＮＡ挿入物の結合詳細配列を示す図であ
る。
【図１２】 γ抗ＣＥＡ鎖をコードするpγ２９８及びp
γ１１のcＤＮＡ挿入物の結合詳細配列を示す図であ
る。
γ１１のcＤＮＡ挿入物の結合詳細配列を示す図であ
る。
【図１３】 γ抗ＣＥＡ鎖をコードするpγ２９８及びp
γ１１のcＤＮＡ挿入物の結合詳細配列を示す図であ
る。
γ１１のcＤＮＡ挿入物の結合詳細配列を示す図であ
る。
【図１４】 γ抗ＣＥＡ鎖をコードするpγ２９８及びp
γ１１のcＤＮＡ挿入物の結合詳細配列を示す図であ
る。
γ１１のcＤＮＡ挿入物の結合詳細配列を示す図であ
る。
【図１５】 図９、図１０、図１１、図１２、図１３お
よび図１４の断片によりコードされた対応アミノ酸配列
を示す図である。
よび図１４の断片によりコードされた対応アミノ酸配列
を示す図である。
【図１６】 図９、図１０、図１１、図１２、図１３お
よび図１４の断片によりコードされた対応アミノ酸配列
を示す図である。
よび図１４の断片によりコードされた対応アミノ酸配列
を示す図である。
【図１７】 図９、図１０、図１１、図１２、図１３お
よび図１４の断片によりコードされた対応アミノ酸配列
を示す図である。
よび図１４の断片によりコードされた対応アミノ酸配列
を示す図である。
【図１８】 図９、図１０、図１１、図１２、図１３お
よび図１４の断片によりコードされた対応アミノ酸配列
を示す図である。
よび図１４の断片によりコードされた対応アミノ酸配列
を示す図である。
【図１９】 図９、図１０、図１１、図１２、図１３お
よび図１４の断片によりコードされた対応アミノ酸配列
を示す図である。
よび図１４の断片によりコードされた対応アミノ酸配列
を示す図である。
【図２０】 κ及びγ抗−ＣＥＡ鎖に対する発現ベクタ
ーの作成概略を示す図である。
ーの作成概略を示す図である。
【図２１】 κ及びγ抗−ＣＥＡ鎖に対する発現ベクタ
ーの作成概略を示す図である。
ーの作成概略を示す図である。
【図２２】 κ及びγ抗−ＣＥＡ鎖に対する発現ベクタ
ーの作成概略を示す図である。
ーの作成概略を示す図である。
【図２３】 κ及びγ抗−ＣＥＡ鎖に対する発現ベクタ
ーの作成概略を示す図である。
ーの作成概略を示す図である。
【図２４】 κ及びγ抗−ＣＥＡ鎖に対する発現ベクタ
ーの作成概略を示す図である。
ーの作成概略を示す図である。
【図２５】 κ及びγ抗−ＣＥＡ鎖に対する発現ベクタ
ーの作成概略を示す図である。
ーの作成概略を示す図である。
【図２６】 γ鎖,κ鎖及びこれら両者に対する遺伝子
を発現するＥ．coli抽出物につき行なったサイジングゲ
ル操作の結果を示す薄膜上に形成された微細なパターン
を表している写真である。
を発現するＥ．coli抽出物につき行なったサイジングゲ
ル操作の結果を示す薄膜上に形成された微細なパターン
を表している写真である。
【図２７】 γ鎖,κ鎖及びこれら両者に対する遺伝子
を発現するＥ．coli抽出物につき行なったサイジングゲ
ル操作の結果を示す薄膜上に形成された微細なパターン
を表している写真である。
を発現するＥ．coli抽出物につき行なったサイジングゲ
ル操作の結果を示す薄膜上に形成された微細なパターン
を表している写真である。
【図２８】 γ鎖,κ鎖及びこれら両者に対する遺伝子
を発現するＥ．coli抽出物につき行なったサイジングゲ
ル操作の結果を示す薄膜上に形成された微細なパターン
を表している写真である。
を発現するＥ．coli抽出物につき行なったサイジングゲ
ル操作の結果を示す薄膜上に形成された微細なパターン
を表している写真である。
【図２９】 図２６、図２７および図２８と同様に形質
転換された細胞抽出物のウェスタンブロットの結果を示
す薄膜上に形成された微細なパターンを表している写真
である。
転換された細胞抽出物のウェスタンブロットの結果を示
す薄膜上に形成された微細なパターンを表している写真
である。
【図３０】 抗ＣＥＡ活性のＥＬＩＳＡ分析に対する標
準曲線図である。
準曲線図である。
【図３１】 キメラＨ鎖をコードする遺伝子の発現に対
するプラスミドの作成図である。
するプラスミドの作成図である。
【図３２】 キメラＨ鎖をコードする遺伝子の発現に対
するプラスミドの作成図である。
するプラスミドの作成図である。
【図３３】 Ｈ鎖のＦab領域をコードする遺伝子の発現
に対するプラスミドの作成図である。
に対するプラスミドの作成図である。
フロントページの続き (51)Int.Cl.6 識別記号 庁内整理番号 ＦＩ 技術表示箇所 // Ａ６１Ｋ 39/395 Ｖ Ｇ０１Ｎ 33/577 Ｂ (Ｃ１２Ｎ 1/21 Ｃ１２Ｒ 1:19） (Ｃ１２Ｐ 21/08 Ｃ１２Ｒ 1:19） (72)発明者 シュミュエル・カビリィ アメリカ合衆国、カリフォルニア・91006、 アーカーディア、サウス・セカンド・アヴ ェニュー・325 (72)発明者 ヘルベルト・ルイス・ヒンケル アメリカ合衆国、カリフォルニア・94010、 バーリンゲイム、イーストン・ドライヴ・ 2621 (72)発明者 ウィリアム・エバンス・ホウムズ アメリカ合衆国、カリフォルニア・94044、 パシフィカ、イーストレイク・29 (72)発明者 アーサー・デイル・リッグス アメリカ合衆国、カリフォルニア・91750、 ラ・ヴァーン、セント・アンドレス・アヴ ェニュー・4852 (72)発明者 ロナルド・バーネル・ウェッゼル アメリカ合衆国、カリフォルニア・94127、 サン・フランシスコ、アーバノ・ドライ ヴ・455
Claims (3)
- 【請求項１】 特定の同定された抗原に対して特異性を
有する免疫グロブリンであって、第１の抗体クラスまた
は第１の哺乳動物種の抗体の不変領域にホモローガスな
不変領域と、第２の異なった抗体クラスまたは哺乳動物
種の抗体の可変領域にホモローガスな可変領域を有する
免疫グロブリン、をコードしているＤＮＡであって、適
切な原核性または真核性宿主細胞に適合し得るプロモー
ターと機能的に結合しているＤＮＡ、を含有している複
製可能な発現ベクター。 - 【請求項２】 不変領域および可変領域が、それぞれ異
なった哺乳動物種の不変領域および可変領域とホモロー
ガスである請求項１に記載の発現ベクター。 - 【請求項３】 特定の同定された抗原に対して特異性を
有する免疫グロブリンであって、第１の抗体クラスまた
は第１の哺乳動物種の抗体の不変領域にホモローガスな
不変領域と、第２の異なった抗体クラスまたは哺乳動物
種の抗体の可変領域にホモローガスな可変領域を有する
免疫グロブリン、をコードしているＤＮＡであって、適
切な原核性または真核性宿主細胞に適合し得るプロモー
ターと機能的に結合しているＤＮＡ、を含有している複
製可能な発現ベクターで形質転換された組換え宿主細
胞。
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US483457 | 1983-04-08 | ||
| US06/483,457 US4816567A (en) | 1983-04-08 | 1983-04-08 | Recombinant immunoglobin preparations |
Related Parent Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP06987484A Division JP3162055B2 (ja) | 1983-04-08 | 1984-04-06 | 組換免疫グロブリン |
Related Child Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2001104857A Division JP2001346592A (ja) | 1983-04-08 | 2001-04-03 | 免疫グロブリンｄｎａ含有発現ベクター及び組換え宿主細胞 |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| JPH07194384A true JPH07194384A (ja) | 1995-08-01 |
Family
ID=23920101
Family Applications (5)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP06987484A Expired - Lifetime JP3162055B2 (ja) | 1983-04-08 | 1984-04-06 | 組換免疫グロブリン |
| JP6241576A Pending JPH07194384A (ja) | 1983-04-08 | 1994-10-05 | 免疫グロブリンｄｎａ含有発現ベクター及び組換え宿主細胞 |
| JP24156594A Expired - Lifetime JP3559795B2 (ja) | 1983-04-08 | 1994-10-05 | 組換免疫グロブリンの調製方法 |
| JP2001104856A Pending JP2001346591A (ja) | 1983-04-08 | 2001-04-03 | 組換免疫グロブリンの調製方法 |
| JP2001104857A Pending JP2001346592A (ja) | 1983-04-08 | 2001-04-03 | 免疫グロブリンｄｎａ含有発現ベクター及び組換え宿主細胞 |
Family Applications Before (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP06987484A Expired - Lifetime JP3162055B2 (ja) | 1983-04-08 | 1984-04-06 | 組換免疫グロブリン |
Family Applications After (3)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP24156594A Expired - Lifetime JP3559795B2 (ja) | 1983-04-08 | 1994-10-05 | 組換免疫グロブリンの調製方法 |
| JP2001104856A Pending JP2001346591A (ja) | 1983-04-08 | 2001-04-03 | 組換免疫グロブリンの調製方法 |
| JP2001104857A Pending JP2001346592A (ja) | 1983-04-08 | 2001-04-03 | 免疫グロブリンｄｎａ含有発現ベクター及び組換え宿主細胞 |
Country Status (16)
| Country | Link |
|---|---|
| US (3) | US4816567A (ja) |
| EP (1) | EP0125023B2 (ja) |
| JP (5) | JP3162055B2 (ja) |
| KR (2) | KR840008264A (ja) |
| AT (1) | ATE64151T1 (ja) |
| AU (2) | AU598441B2 (ja) |
| CA (1) | CA1218613A (ja) |
| CY (1) | CY1793A (ja) |
| DE (1) | DE3484664D1 (ja) |
| DK (2) | DK174048B1 (ja) |
| ES (1) | ES531372A0 (ja) |
| HK (1) | HK129394A (ja) |
| IE (1) | IE57198B1 (ja) |
| IL (1) | IL71455A (ja) |
| NZ (3) | NZ207746A (ja) |
| ZA (1) | ZA842583B (ja) |
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| WO2011093083A1 (ja) | 2010-01-29 | 2011-08-04 | Ａｘｉｓ株式会社 | 変形性関節症治療又は予防用医薬組成物及びその製造方法 |
| US9200077B2 (en) | 2010-01-29 | 2015-12-01 | Axis, Inc. | Injectable solution containing therapeutic agent for osteoarthritis |
| WO2012005076A1 (ja) | 2010-07-08 | 2012-01-12 | 本田技研工業株式会社 | 高周波加熱用コイル |
| WO2014021339A1 (ja) | 2012-07-30 | 2014-02-06 | 国立大学法人名古屋大学 | ヒトミッドカインに対するモノクローナル抗体 |
| WO2014042251A1 (ja) | 2012-09-13 | 2014-03-20 | 中外製薬株式会社 | 遺伝子ノックイン非ヒト動物 |
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