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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- Prior art keywords
- chain
- antibody
- dna
- fragment
- antibodies
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Pending
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- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
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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) | NZ222543A (ja) |
ZA (1) | ZA842583B (ja) |
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JP2010539911A (ja) * | 2007-09-24 | 2010-12-24 | ウーデ ゲゼルシャフト ミット ベシュレンクテル ハフツング | アミンでの発酵及び抽出により乳酸を製造する方法 |
WO2009119794A1 (ja) | 2008-03-27 | 2009-10-01 | タカラバイオ株式会社 | 感染症予防、治療剤 |
WO2010013498A1 (ja) | 2008-08-01 | 2010-02-04 | 学校法人聖マリアンナ医科大学 | 変形性関節症治療剤又は予防剤 |
WO2011093081A1 (ja) | 2010-01-29 | 2011-08-04 | Axis株式会社 | 変形性関節症治療剤を含有する注射剤 |
WO2011093082A1 (ja) | 2010-01-29 | 2011-08-04 | Axis株式会社 | 変形性関節症治療剤または予防剤を製造するための使用 |
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 |
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