JP3162055B2 - 組換免疫グロブリン - Google Patents
組換免疫グロブリンInfo
- Publication number
- JP3162055B2 JP3162055B2 JP06987484A JP6987484A JP3162055B2 JP 3162055 B2 JP3162055 B2 JP 3162055B2 JP 06987484 A JP06987484 A JP 06987484A JP 6987484 A JP6987484 A JP 6987484A JP 3162055 B2 JP3162055 B2 JP 3162055B2
- Authority
- JP
- Japan
- Prior art keywords
- chain
- human
- fragment
- cells
- dna
- 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.)
- Expired - Lifetime
Links
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Classifications
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- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/63—Introduction of foreign genetic material using vectors; Vectors; Use of hosts therefor; Regulation of expression
-
- A—HUMAN NECESSITIES
- A01—AGRICULTURE; FORESTRY; ANIMAL HUSBANDRY; HUNTING; TRAPPING; FISHING
- A01N—PRESERVATION OF BODIES OF HUMANS OR ANIMALS OR PLANTS OR PARTS THEREOF; BIOCIDES, e.g. AS DISINFECTANTS, AS PESTICIDES OR AS HERBICIDES; PEST REPELLANTS OR ATTRACTANTS; PLANT GROWTH REGULATORS
- A01N65/00—Biocides, pest repellants or attractants, or plant growth regulators containing material from algae, lichens, bryophyta, multi-cellular fungi or plants, or extracts thereof
- A01N65/40—Liliopsida [monocotyledons]
- A01N65/44—Poaceae or Gramineae [Grass family], e.g. bamboo, lemon grass or citronella grass
-
- A—HUMAN NECESSITIES
- A01—AGRICULTURE; FORESTRY; ANIMAL HUSBANDRY; HUNTING; TRAPPING; FISHING
- A01N—PRESERVATION OF BODIES OF HUMANS OR ANIMALS OR PLANTS OR PARTS THEREOF; BIOCIDES, e.g. AS DISINFECTANTS, AS PESTICIDES OR AS HERBICIDES; PEST REPELLANTS OR ATTRACTANTS; PLANT GROWTH REGULATORS
- A01N25/00—Biocides, pest repellants or attractants, or plant growth regulators, characterised by their forms, or by their non-active ingredients or by their methods of application, e.g. seed treatment or sequential application; Substances for reducing the noxious effect of the active ingredients to organisms other than pests
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
- C07K16/28—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants
- C07K16/30—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants from tumour cells
- C07K16/3007—Carcino-embryonic Antigens
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/46—Hybrid immunoglobulins
- C07K16/461—Igs containing Ig-regions, -domains or -residues form different species
- C07K16/462—Igs containing a variable region (Fv) from one specie and a constant region (Fc) from another
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/63—Introduction of foreign genetic material using vectors; Vectors; Use of hosts therefor; Regulation of expression
- C12N15/79—Vectors or expression systems specially adapted for eukaryotic hosts
- C12N15/80—Vectors or expression systems specially adapted for eukaryotic hosts for fungi
- C12N15/81—Vectors or expression systems specially adapted for eukaryotic hosts for fungi for yeasts
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/20—Immunoglobulins specific features characterized by taxonomic origin
- C07K2317/24—Immunoglobulins specific features characterized by taxonomic origin containing regions, domains or residues from different species, e.g. chimeric, humanized or veneered
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/01—Fusion polypeptide containing a localisation/targetting motif
- C07K2319/02—Fusion polypeptide containing a localisation/targetting motif containing a signal sequence
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/30—Non-immunoglobulin-derived peptide or protein having an immunoglobulin constant or Fc region, or a fragment thereof, attached thereto
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- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10—TECHNICAL SUBJECTS COVERED BY FORMER USPC
- Y10S—TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10S530/00—Chemistry: natural resins or derivatives; peptides or proteins; lignins or reaction products thereof
- Y10S530/866—Chemistry: natural resins or derivatives; peptides or proteins; lignins or reaction products thereof involving immunoglobulin or antibody fragment, e.g. fab', fab, fv, fc, heavy chain or light chain
-
- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10—TECHNICAL SUBJECTS COVERED BY FORMER USPC
- Y10S—TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10S530/00—Chemistry: natural resins or derivatives; peptides or proteins; lignins or reaction products thereof
- Y10S530/867—Chemistry: natural resins or derivatives; peptides or proteins; lignins or reaction products thereof involving immunoglobulin or antibody produced via recombinant dna technology
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- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10—TECHNICAL SUBJECTS COVERED BY FORMER USPC
- Y10S—TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10S930/00—Peptide or protein sequence
- Y10S930/01—Peptide or protein sequence
- Y10S930/30—Signal or leader sequence
Description
【発明の詳細な説明】
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。 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。 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。 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内で融てられて存
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.Biochem.Sc
i.,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 situ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 populat
ion)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。 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(Kohler e
t al.,Eur.J.Immunol.,6:511(1976))。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(198
0))、並びにヒト−ネズミハイブリドーマ(J.Schlom
et al.,同上,77:6841(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−次B細胞(primary B cell)が、ウィルスDN
Aでの形質転換によりin vitroで永久株化されている。 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。 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.Nat
l.Acad.Sci.,USA,77:2197(1980);S.L.Morrison,J.Imm
unol.123:793(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
(alteration)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(1971))、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 sit
u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。 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
らのみ少量で誘発することができる。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。 A.2.一般的構造特性 骨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.Ac
ad.Sci.,190:5(1971))。これらの単位は、分子量約2
3,000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、第1図に示すように、
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。 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。 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,Ig
A,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.413−4
36,Holt,Rinehart,Winston(1976))及びその他の細胞
反応(D.W.Andrews et al.,Clinical Immunobiology,p.
1−18,W.B.Sanders(1980);S.Kohlet 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。 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。DNAの各種
の平滑末端断片又は「粘着(付着性)」末端断片をin v
itro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。 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DNA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
るポリペプ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。 実際上、組換DNA技術の使用は、全く異種のポリペプ
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)ポリペプチドのアミノ酸配列の一部
に融合した異種ポリペプ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
ペプチド内で生物不活性にされている。 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。 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(NS
I)に関するものである。これらの抗体及びNSI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。 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ペプチドから成
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。 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(univalen
t)」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。 他の面に於いて、本発明は、上記のNSI,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。 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(aggregate)を意味し、通常第1図の「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。「免疫グロブリン種」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。 「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(homolo
gous)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。 「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(devalenc
e)」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。 「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。 「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。 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であっ
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が、
又は不変領域が向上した補体固定反応(complement fix
ation)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。 「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
然変誘異発技術(aligo−nucleotide−directed mutage
nesis techniques)によっても行なうことができる(Da
lbadie−McFarland et al.,Proc.Natl.Acad.Sci.,USA,7
9:6409(1982))。 「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(aggregation)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 effectiveness)を
損うことがなく、即ち抗原変調(antigenic modulatio
n)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。 「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(analog
ous)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。 「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。 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。 「発現ベクター」という用語は、そこに含有されるDN
A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。 「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(modification)は、こ
の形質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。 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。 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。 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 K12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.coli B及びE.coli X17
76(ATCC 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。 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(protot
rophic)、ATCC No.27325),稈菌例えばBacillus sub
tilus、及び他の腸内細菌例えばSalmonella typhimuriu
m又はSerratia marcesans及び各種のPseudomonas種を使
用することができる。 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、pBR322即ちE.coli種
から得られるプラズミド(Boliver et al.,Gene 2:95
(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(1978);Itakura et al.,Scien
ce,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.,8:4057(1
980);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(Si
ebenlist et al.,Cell,20:269(1980))。 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 cerevisiae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。Saccha
romycesに於ける発現については例えばプラスミドYRp7
(Stinchcomb et al.,Nature,282:39(1979);Kingsman
et al.,Gene,7:141(1979);Tschemper et 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trp 1遺伝子を含有する。酵母宿主細胞ゲノム
の特性としてtrp 1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。 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.Bio
l.Chem.,255:2073(1980))又はその他の糖分解酵素
(Hess et al.,J.Adv.Enzyme Reg.,7:149(1968);Hol
land 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。 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 Press,Kruse an
d Patterson編(1973))。この種の有用な宿主細胞系
の例は、VERO細胞及びHe La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MDC
K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
リボソーム結合部位,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。 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 a
l.,Nature,273:113(1978),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Hind IIIから複製のウィルスオリジン
内に存在するBgl I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。 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。 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。 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。 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.Cohe
n et al.によりProc.Natl.Acad.Sci.,USA,69:210(197
2)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。 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。 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1μgのプラ
スミド又はDNA断片を約20μ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。 平滑末端が必要ならば、この調製物を10ユニットのE.
coli DNA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。 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。 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0.5μgのDNA当り約
10ユニットのT4 DNA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。) 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(ATCC 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(Nucliec Acids Re
s.,9:309(1981))又はMaxam et al.の方法(Methods
in Enzymology,65:499(1980))によって配列決定し
た。 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。 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 m
RNA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。 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 mRNA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Pst I)により開裂し且つdG残部で延長したp
BR322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。 成功した形質転換体を釣り上げて、マイクロタイター
III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(im−print)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。 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。 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0036776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。 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。 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。 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(酵母及びグラム陽性菌)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。 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。 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。 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.,Enzymology of Post Tra
nslational Modification of Proteins,1:157−212(1
980)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)
721−728.Pierce Chemical Co.,Rockford,IL.(198
1))。 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.Natl.Acad.Sci.,USA,50:75
3(1963)。更に、蛋白質分解により生成される活性なI
gG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,52:1099(1964);
P.L.Whitney et al.,Proc.Natl.Acad.Sci.,USA,53:524
(1965))。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)。 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.,C
hemical Modification of Proteins,Holden−Day,San F
rancisco(1971))、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。 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。 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。 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「哺乳動物の抗体」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。 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。 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。 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mR
NA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。 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
時期早尚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。 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。 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するクローンニングする。
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。 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(1982))。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.Sche
inberg et al.,Science,215:19(1982))。 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。 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。 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。 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。 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。 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。 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。 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。 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。 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 胎児期癌の抗原(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.Exp.Me
d.,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る(T.R.Van
Nagell et al.,Cancer Res.,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.
Wagener et al.,J.Immunol.,130:2308(1983)(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.Podell et al.,Biochem.Biophys.Re
s.Commun.,81:176(1978)、次いで6Mグアニジン塩酸塩
と10mM 2−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 Associates
社製)に於いて100%A(0.1%,TFA−水)〜90%B(TF
A/H2O/MeCN:0.1/9.9/90)の直線勾配を用いて0.8ml/mi
n.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のの
ピークはH鎖とL鎖との7:3混合物であった。1.2nM(ナ
ノモル)のL鎖をJ.E.Shively,Methods in Enzymology,
79:31(1981)の方法により0.4nM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。 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。 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 al.,Virology,9
8:251(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,10mMトリスHCl(pH7.4)、1.5mM Mg
Cl2の10ml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
SDS(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2
5:1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Leder,Proc,Natl.Acad.Sci.,US
A,69:1408(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。 E.1.2.H鎖及びL鎖のDNA配列挿入物を有するプラズミド
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(1979)及びWickens e
t al.,J.Biol.Chem.,253:2483(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,275:617(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Ps
t I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8,500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。 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MOPC2
1κ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′GGTGGGAAGATGGA3′をκ鎖プローブ
として使用した。ネズミMOPC21γ鎖に対する可変領域DN
A配列の72塩基対3′に位置するコード配列に補完的な1
5元体、即ち5′GACCAGGCATCCCAG3′をγ鎖遺伝子プロ
ーブとして使用した。 両プローブは、ドイツ公開公報第264432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
(pH8)、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25μ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。 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2,000個のコ
ロニーをLB(Miller,Experiments in Molecular Geneti
cs,p.431−3,Cold Spring Harbor Lab.,Cold Spring Ha
rbor,New York(1972)+5μg/mlのテトラサイクリン
を含有するマイクロタイターIIIの穴に個々に接種し、D
MSO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12.5
μg/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
(pH7.5)、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/ml E.coli t−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Wallace et al.,Nucleic Acids
Research,9:879(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40×106cpm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Du
pont Lightning−Plus強化スクリーンを用いてKodak X
R−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20種のコロニーを
特性化した。 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Pst I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cDNA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(1980)(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.,NucleicAcids Research,9:309
(1981))。第2図はpK17G4のcDNA挿入物のヌクレオチ
ド配列を示し、第3図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DNA断片につき単離した。κ
鎖のアミノ酸配列は、pK17G4 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2
3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。pK17G4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2
14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。pK17G4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(第2図)。 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Pst I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Nco I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P
st IとNco I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Nco I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。 単離した1種のプラスミド(即ちpγ298)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。p
γ298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Pst I及びNco I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pγ298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。 第4図はネズミ抗−CEAH鎖の全ヌクレオチド配列を示
し(Smith,Methods Enzymol.,65:560(1980)のジデオ
キシヌクレオチド鎖停止法により決定する)、第5図は
翻訳配列を含んでいる。 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−CEA
γ1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−末端アミノ酸を完全に
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(MW52,258)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32
4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
(第4図)。 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、pKCEAtrp207−1* 第6図はpKCEAtrp207−1*の作成を示している。 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0036776号)に記載)
は、二重lacプロモーターに続いてEcoR I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BamH Iで消
化し、EcoR I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EcoR I−BamH I断片に結合し、この結合混合
物を使用してE.coli 294を形質転換した。TetRAmpR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プロモーターとの間にEcoR I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Klenow及びdNTPの充填及び再結
合によって得た。 5μgのpHGH207−1*をEcoR Iで消化し、これら末
端を60mM NaCl,7mM MgCl2,7mMトリスHCl(pH7.4)及
び1mMの各dNTPを含有する50μ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BamH I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。 このDNAを10mMトリス(pH8),1mM EDTAの50μ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。 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Pst I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/CHCl3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Ava IIによって消化し
た。333bpのPst I−Ava II 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。 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: 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20μの反応
液中で10ユニットのT4DNAキナーゼにより5未満で燐酸
化した。約200ngのPst I−Ava II DNA断片を20μ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DNA溶液を60mM NaCl,7mM MgCl2,7m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。37℃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Sau 3A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Sau 3A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。 100ngの断片1(上記)と50ngの断片2とを20mMトリ
スHCl(pH7.5),10mM MgCl2,10mM DTT,2.5mM ATP及
び1ユニットのT4DNAリガーゼの20μ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
K12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(第6図)。 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Pst I cDNA挿入物断片をAva
IIで部分消化させ、Ava II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P
st I−平滑末端Ava II DNA断片を単離し、精製し、Hpa
II制限エンドヌクレアーゼ消化にかけた。497塩基対のH
pa II−平滑末端Ava II DNA断片(断片3)を単離し、
ゲル電気泳動の後に精製した。 10μgのpKCEAInt1DNAをAva Iで消化し、DNAポリメラ
ーゼI大断片で延長化し、Xba Iで消化した。大平滑末
端Ava I−Xba Iベクター断片と、小平滑末端Ava I−Xba
I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Hpa II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Xba I−Hpa II DNA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、1
4℃にて1晩培養し、反応混合物をE.coli K12菌株294
で形質転換した。6種のアンピシリン耐性形質転換体か
らのプラズミド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。 最終的な作成は、pKCEAInt2からのtrpプロモーターを
含むK−CEA断片をpKR322(XAP)中へ結合することによ
り行なった(pBR322(XAP)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、p
BR322からAva I−Pva II断片の削除(欠失)に続く結合
によって作成した)。 K−CEA断片は、pKCEAInt2をAva I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、Pst I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。 pBR322(XAP)からの大型ベクター断片は、EcoR Iに
よる処理,ポリメラーゼによる平滑末端化及びPst I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。 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D
NAが適正な作成を示し、これをpKCEAtrp207−1*と命
名した。 E.1.8.ネズミ成熟抗−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* 第7図は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。 5μgのプラスミドpHGH207−1*をAva Iで消化し、
DNAポリメラーゼI大型断片(Klenow断片)で平滑末端
まで延長化し、フェノール/CHCl3で抽出し、エタノール
沈澱させた。DNAをBamH I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。 約5μgのpγ11をPst Iにより消化し、そして遺伝
子のC末端部分を有するr鎖cDNA挿入物切断片を精製
し、Ava IIで消化し、次いでAva II付着端部をクノール
で延長化し、次いでTaq Iの消化を行なった。375塩基対
の平滑端Ava II−Taq I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。 9μgのpγ298をTaq I及びBamH Iで消化して496塩
基対断片(断片C)を単離した。 ほぼ等モル量の断片A,B及びCを20μ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、pγC
EAInt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(第5図)。 N−末端配列を得るため、30μgのpγ298をPst I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Alu I及びRsa Iで消化して280塩基対断片を単離
した。15ヌクレオチドDNAプライマー、即ち をホスホトリエステル法(上記)により合成した。 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20μの反応混合物中に含有する10ユニットのT
4DNA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Alu I−Rsa I 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DN
A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/CHCl3で抽出し、
エタノール沈澱させ、Hpa IIで完全消化させた。予想さ
れた125塩基対の平滑末端−Hpa II DNA断片(断片D)
50ngをゲルから精製した。 第2の部分のpγ298DNAをPst I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BamH I及びHpa II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。 5μgのpγCEAInt1をEcoR Iで消化し、付着末端をD
NAポリメラーゼI(Klenow)と整列させ、BamH I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。 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20μ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2
94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DNA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。 H鎖遺伝子の発現に使用した発現プラスミドpγCEAt
rp207−1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。 pBR322(XAP)を上記のようにEcoR Iで消化し、DNAポ
リメラーゼ(Klenow)によりdNTPの存在下で平滑末端化
させ、次いでPst I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pγCEAInt2をPst Iに続き、BamH I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Ava Iによる
pγCEAInt2の部分消化、Klenowによる平滑末端化及びB
amH I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。 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。 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.27325)を標準技術によ
りpγCEAtrp207−1又はpKCEAtrp207−1で形質転換さ
せた。 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Pst I−Pvu I断片の開裂及び再結
合によって改変させた改変pKCEAtrp207−1及びpKCEAtr
p207−1△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pγCEA
Int2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。 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M9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(IA
A)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.,250:4007(19
75)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PAGE(10%)を用いて分画
し、銀染色剤により染色し(D.Goldman et al.,Scienc
e,211:1437(1981)、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ブロット
(Western blot)にかけた(W.N.Burnett et al.,Anal.
Biochem.,112:195(1981))。 pγCEAtrp207−1で形質転換させた細胞は、SDS PA
GE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。pKCEAtrp207−1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。これらを第8A,8B及
び8C図に示す。 第8A図は、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IAA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。 第8B図は、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pγCE
Atrp207−1比較からの抽出物であり、レーン8,9及び10
はCEA.66−E3細胞からの様々な量の抗CEA−κ鎖であ
る。 第8C図は、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pγCEAtrp207−
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。これら結果を第9図に示す。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: (細胞1g当り) E.coli(W3110/pγCEAtrp207−1*) 5mgγ E.coli(W3110/pKCEAtrp207−1*) 1.5mgκ E.coli(W3110/pKCEAtrp207−1*△,pγCEAInt2)0.5m
gκ,1.0mgγ 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: E.coli(W3110/pγCEAtrp207−1*)を5μg/mlのテ
トラサイクリンを含有する500ml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10の発酵培地に移した。増殖の際にグルコ
ースを追加し、OD 550=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OD 550=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。 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、IA
A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。 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ELISA
により測定した。マイクロタイタープレート(Dynatech
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100μ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%BSA200μ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。50μの各試
料を各ウェルに加えた。PBSに於ける0.5%BSA中10μg,5
μg,500ng,100ng,50ng,10ng,5ng及び1ngの抗−CEA/mlの
50μ試料と、ブランクとしてのPBSに於ける0.5%BSA5
0μのみとから成る標準曲線(第10図に示す)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。 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10
μ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100μを加えた。この基質を37℃
にて90分間培養した発色させた。 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,Dynatech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。 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3,00
0rpmにて20分間の遠心分離により部分清澄化させた。1m
M PMSF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。 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
(pH8),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、25℃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。 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650μを500mg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。 ng/ml 組換 E.4.キメラ抗体の作成 第11図及び第12図はネズミ抗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。 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5GGGCACTCGACACAA3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(Takahashi 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
al.,Proc.Natl.Acad.USA,79:1984(1982)(この文献
を引用して本明細書に包含する)。 第11図に示したように、クローン化ヒトγ2プラスミ
ド(pγ2)から2つの断片が得られる。第1の断片
は、Pvu IIによる消化に続きAva III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、Ava III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。(Pvu II
−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Ava III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。)pγCEA 207−1をEcoR Iで消化し、Kle
now及びdNTPで処理して付着性末端充填し、Pvu II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。 ネズミγ1遺伝子に於けるPvu II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Pvu II部位を
包囲する位置及びDNA配列と同一である。 上記断片の3方向結合から得られるプラスミド(pChi
m1)は、trpプロモーターの影響下で、ネズミ抗−CEAγ
1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。 第12図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pChim1の改変を示し
ている。まず、Nco Iで処理し、Klenow及びdNTPで平滑
末端化させ、Pvu II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。Pvu IIで処
理し、可変領域で開裂する任意の制限酵素で処理し、Kl
enow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pγ2から第2の断片を作成する。 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Xba I−Pv
u IIの断片を切断しMessing et al.,Nulice Acids Re
s.,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Adelman 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Xba
I−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。 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。 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。 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216−2
30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.,USA,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: 「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′CTAACACCATGTCAGGGTを使用して、Wa
llace et al.,Science,209:1396(1980)の方法又はAde
lman et al.,DNA,2:183(1983)の方法によってpγCE
Atrp207−1*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P32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。 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。 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:pγCEAFabtrp207−1* 第13図はpγCEAFabtrp207−1*の作成を示してい
る。5μgのpBR322をHind IIIで消化し、Klenow及びdN
TPで処理して付着性末端を平滑化し、Pst Iで消化し、B
AP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。 5μgのpγCEAtrp207−1をBamH I及びPst I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1570bpのDNA断片(断片I
I)を単離し、電気泳動の後に精製した。 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、20μgのpγ298か
ら260bpのNco I−Nde I 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(第4図)にハイ
ブリダイズし、これは次の配列を有する: 停止コドンの第3塩基を上記のpBR322開裂物の充填Hi
nd III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、20μ中に0.5mMのATPを含有する10
ユニットのT4DNA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Nco I−Nde I 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,7mM MgC
l2,7mM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/CHCl3で抽出し、エタノール沈澱
し、Bam HI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−BamH IのD
NA断片、即ち断片IIIの約50ngを単離し、精製した。 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 K12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Hind III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。 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pKCEA
trp207−1*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。
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。 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。 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。 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内で融てられて存
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.Biochem.Sc
i.,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 situ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 populat
ion)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。 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(Kohler e
t al.,Eur.J.Immunol.,6:511(1976))。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(198
0))、並びにヒト−ネズミハイブリドーマ(J.Schlom
et al.,同上,77:6841(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−次B細胞(primary B cell)が、ウィルスDN
Aでの形質転換によりin vitroで永久株化されている。 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。 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.Nat
l.Acad.Sci.,USA,77:2197(1980);S.L.Morrison,J.Imm
unol.123:793(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
(alteration)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(1971))、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 sit
u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。 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
らのみ少量で誘発することができる。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。 A.2.一般的構造特性 骨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.Ac
ad.Sci.,190:5(1971))。これらの単位は、分子量約2
3,000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、第1図に示すように、
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。 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。 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,Ig
A,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.413−4
36,Holt,Rinehart,Winston(1976))及びその他の細胞
反応(D.W.Andrews et al.,Clinical Immunobiology,p.
1−18,W.B.Sanders(1980);S.Kohlet 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。 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。DNAの各種
の平滑末端断片又は「粘着(付着性)」末端断片をin v
itro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。 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DNA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
るポリペプ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。 実際上、組換DNA技術の使用は、全く異種のポリペプ
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)ポリペプチドのアミノ酸配列の一部
に融合した異種ポリペプ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
ペプチド内で生物不活性にされている。 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。 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(NS
I)に関するものである。これらの抗体及びNSI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。 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ペプチドから成
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。 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(univalen
t)」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。 他の面に於いて、本発明は、上記のNSI,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。 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(aggregate)を意味し、通常第1図の「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。「免疫グロブリン種」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。 「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(homolo
gous)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。 「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(devalenc
e)」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。 「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。 「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。 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であっ
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が、
又は不変領域が向上した補体固定反応(complement fix
ation)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。 「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
然変誘異発技術(aligo−nucleotide−directed mutage
nesis techniques)によっても行なうことができる(Da
lbadie−McFarland et al.,Proc.Natl.Acad.Sci.,USA,7
9:6409(1982))。 「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(aggregation)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 effectiveness)を
損うことがなく、即ち抗原変調(antigenic modulatio
n)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。 「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(analog
ous)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。 「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。 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。 「発現ベクター」という用語は、そこに含有されるDN
A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。 「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(modification)は、こ
の形質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。 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。 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。 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 K12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.coli B及びE.coli X17
76(ATCC 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。 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(protot
rophic)、ATCC No.27325),稈菌例えばBacillus sub
tilus、及び他の腸内細菌例えばSalmonella typhimuriu
m又はSerratia marcesans及び各種のPseudomonas種を使
用することができる。 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、pBR322即ちE.coli種
から得られるプラズミド(Boliver et al.,Gene 2:95
(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(1978);Itakura et al.,Scien
ce,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.,8:4057(1
980);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(Si
ebenlist et al.,Cell,20:269(1980))。 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 cerevisiae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。Saccha
romycesに於ける発現については例えばプラスミドYRp7
(Stinchcomb et al.,Nature,282:39(1979);Kingsman
et al.,Gene,7:141(1979);Tschemper et 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trp 1遺伝子を含有する。酵母宿主細胞ゲノム
の特性としてtrp 1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。 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.Bio
l.Chem.,255:2073(1980))又はその他の糖分解酵素
(Hess et al.,J.Adv.Enzyme Reg.,7:149(1968);Hol
land 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。 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 Press,Kruse an
d Patterson編(1973))。この種の有用な宿主細胞系
の例は、VERO細胞及びHe La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MDC
K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
リボソーム結合部位,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。 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 a
l.,Nature,273:113(1978),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Hind IIIから複製のウィルスオリジン
内に存在するBgl I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。 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。 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。 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。 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.Cohe
n et al.によりProc.Natl.Acad.Sci.,USA,69:210(197
2)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。 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。 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1μgのプラ
スミド又はDNA断片を約20μ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。 平滑末端が必要ならば、この調製物を10ユニットのE.
coli DNA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。 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。 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0.5μgのDNA当り約
10ユニットのT4 DNA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。) 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(ATCC 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(Nucliec Acids Re
s.,9:309(1981))又はMaxam et al.の方法(Methods
in Enzymology,65:499(1980))によって配列決定し
た。 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。 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 m
RNA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。 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 mRNA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Pst I)により開裂し且つdG残部で延長したp
BR322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。 成功した形質転換体を釣り上げて、マイクロタイター
III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(im−print)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。 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。 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0036776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。 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。 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。 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(酵母及びグラム陽性菌)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。 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。 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。 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.,Enzymology of Post Tra
nslational Modification of Proteins,1:157−212(1
980)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)
721−728.Pierce Chemical Co.,Rockford,IL.(198
1))。 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.Natl.Acad.Sci.,USA,50:75
3(1963)。更に、蛋白質分解により生成される活性なI
gG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,52:1099(1964);
P.L.Whitney et al.,Proc.Natl.Acad.Sci.,USA,53:524
(1965))。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)。 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.,C
hemical Modification of Proteins,Holden−Day,San F
rancisco(1971))、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。 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。 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。 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「哺乳動物の抗体」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。 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。 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。 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mR
NA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。 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
時期早尚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。 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。 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するクローンニングする。
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。 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(1982))。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.Sche
inberg et al.,Science,215:19(1982))。 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。 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。 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。 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。 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。 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。 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。 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。 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。 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 胎児期癌の抗原(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.Exp.Me
d.,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る(T.R.Van
Nagell et al.,Cancer Res.,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.
Wagener et al.,J.Immunol.,130:2308(1983)(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.Podell et al.,Biochem.Biophys.Re
s.Commun.,81:176(1978)、次いで6Mグアニジン塩酸塩
と10mM 2−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 Associates
社製)に於いて100%A(0.1%,TFA−水)〜90%B(TF
A/H2O/MeCN:0.1/9.9/90)の直線勾配を用いて0.8ml/mi
n.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のの
ピークはH鎖とL鎖との7:3混合物であった。1.2nM(ナ
ノモル)のL鎖をJ.E.Shively,Methods in Enzymology,
79:31(1981)の方法により0.4nM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。 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。 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 al.,Virology,9
8:251(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,10mMトリスHCl(pH7.4)、1.5mM Mg
Cl2の10ml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
SDS(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2
5:1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Leder,Proc,Natl.Acad.Sci.,US
A,69:1408(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。 E.1.2.H鎖及びL鎖のDNA配列挿入物を有するプラズミド
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(1979)及びWickens e
t al.,J.Biol.Chem.,253:2483(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,275:617(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Ps
t I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8,500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。 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MOPC2
1κ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′GGTGGGAAGATGGA3′をκ鎖プローブ
として使用した。ネズミMOPC21γ鎖に対する可変領域DN
A配列の72塩基対3′に位置するコード配列に補完的な1
5元体、即ち5′GACCAGGCATCCCAG3′をγ鎖遺伝子プロ
ーブとして使用した。 両プローブは、ドイツ公開公報第264432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
(pH8)、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25μ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。 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2,000個のコ
ロニーをLB(Miller,Experiments in Molecular Geneti
cs,p.431−3,Cold Spring Harbor Lab.,Cold Spring Ha
rbor,New York(1972)+5μg/mlのテトラサイクリン
を含有するマイクロタイターIIIの穴に個々に接種し、D
MSO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12.5
μg/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
(pH7.5)、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/ml E.coli t−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Wallace et al.,Nucleic Acids
Research,9:879(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40×106cpm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Du
pont Lightning−Plus強化スクリーンを用いてKodak X
R−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20種のコロニーを
特性化した。 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Pst I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cDNA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(1980)(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.,NucleicAcids Research,9:309
(1981))。第2図はpK17G4のcDNA挿入物のヌクレオチ
ド配列を示し、第3図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DNA断片につき単離した。κ
鎖のアミノ酸配列は、pK17G4 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2
3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。pK17G4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2
14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。pK17G4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(第2図)。 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Pst I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Nco I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P
st IとNco I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Nco I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。 単離した1種のプラスミド(即ちpγ298)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。p
γ298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Pst I及びNco I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pγ298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。 第4図はネズミ抗−CEAH鎖の全ヌクレオチド配列を示
し(Smith,Methods Enzymol.,65:560(1980)のジデオ
キシヌクレオチド鎖停止法により決定する)、第5図は
翻訳配列を含んでいる。 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−CEA
γ1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−末端アミノ酸を完全に
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(MW52,258)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32
4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
(第4図)。 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、pKCEAtrp207−1* 第6図はpKCEAtrp207−1*の作成を示している。 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0036776号)に記載)
は、二重lacプロモーターに続いてEcoR I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BamH Iで消
化し、EcoR I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EcoR I−BamH I断片に結合し、この結合混合
物を使用してE.coli 294を形質転換した。TetRAmpR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プロモーターとの間にEcoR I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Klenow及びdNTPの充填及び再結
合によって得た。 5μgのpHGH207−1*をEcoR Iで消化し、これら末
端を60mM NaCl,7mM MgCl2,7mMトリスHCl(pH7.4)及
び1mMの各dNTPを含有する50μ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BamH I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。 このDNAを10mMトリス(pH8),1mM EDTAの50μ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。 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Pst I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/CHCl3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Ava IIによって消化し
た。333bpのPst I−Ava II 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。 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: 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20μの反応
液中で10ユニットのT4DNAキナーゼにより5未満で燐酸
化した。約200ngのPst I−Ava II DNA断片を20μ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DNA溶液を60mM NaCl,7mM MgCl2,7m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。37℃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Sau 3A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Sau 3A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。 100ngの断片1(上記)と50ngの断片2とを20mMトリ
スHCl(pH7.5),10mM MgCl2,10mM DTT,2.5mM ATP及
び1ユニットのT4DNAリガーゼの20μ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
K12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(第6図)。 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Pst I cDNA挿入物断片をAva
IIで部分消化させ、Ava II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P
st I−平滑末端Ava II DNA断片を単離し、精製し、Hpa
II制限エンドヌクレアーゼ消化にかけた。497塩基対のH
pa II−平滑末端Ava II DNA断片(断片3)を単離し、
ゲル電気泳動の後に精製した。 10μgのpKCEAInt1DNAをAva Iで消化し、DNAポリメラ
ーゼI大断片で延長化し、Xba Iで消化した。大平滑末
端Ava I−Xba Iベクター断片と、小平滑末端Ava I−Xba
I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Hpa II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Xba I−Hpa II DNA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、1
4℃にて1晩培養し、反応混合物をE.coli K12菌株294
で形質転換した。6種のアンピシリン耐性形質転換体か
らのプラズミド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。 最終的な作成は、pKCEAInt2からのtrpプロモーターを
含むK−CEA断片をpKR322(XAP)中へ結合することによ
り行なった(pBR322(XAP)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、p
BR322からAva I−Pva II断片の削除(欠失)に続く結合
によって作成した)。 K−CEA断片は、pKCEAInt2をAva I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、Pst I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。 pBR322(XAP)からの大型ベクター断片は、EcoR Iに
よる処理,ポリメラーゼによる平滑末端化及びPst I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。 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D
NAが適正な作成を示し、これをpKCEAtrp207−1*と命
名した。 E.1.8.ネズミ成熟抗−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* 第7図は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。 5μgのプラスミドpHGH207−1*をAva Iで消化し、
DNAポリメラーゼI大型断片(Klenow断片)で平滑末端
まで延長化し、フェノール/CHCl3で抽出し、エタノール
沈澱させた。DNAをBamH I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。 約5μgのpγ11をPst Iにより消化し、そして遺伝
子のC末端部分を有するr鎖cDNA挿入物切断片を精製
し、Ava IIで消化し、次いでAva II付着端部をクノール
で延長化し、次いでTaq Iの消化を行なった。375塩基対
の平滑端Ava II−Taq I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。 9μgのpγ298をTaq I及びBamH Iで消化して496塩
基対断片(断片C)を単離した。 ほぼ等モル量の断片A,B及びCを20μ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、pγC
EAInt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(第5図)。 N−末端配列を得るため、30μgのpγ298をPst I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Alu I及びRsa Iで消化して280塩基対断片を単離
した。15ヌクレオチドDNAプライマー、即ち をホスホトリエステル法(上記)により合成した。 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20μの反応混合物中に含有する10ユニットのT
4DNA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Alu I−Rsa I 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DN
A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/CHCl3で抽出し、
エタノール沈澱させ、Hpa IIで完全消化させた。予想さ
れた125塩基対の平滑末端−Hpa II DNA断片(断片D)
50ngをゲルから精製した。 第2の部分のpγ298DNAをPst I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BamH I及びHpa II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。 5μgのpγCEAInt1をEcoR Iで消化し、付着末端をD
NAポリメラーゼI(Klenow)と整列させ、BamH I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。 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20μ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2
94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DNA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。 H鎖遺伝子の発現に使用した発現プラスミドpγCEAt
rp207−1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。 pBR322(XAP)を上記のようにEcoR Iで消化し、DNAポ
リメラーゼ(Klenow)によりdNTPの存在下で平滑末端化
させ、次いでPst I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pγCEAInt2をPst Iに続き、BamH I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Ava Iによる
pγCEAInt2の部分消化、Klenowによる平滑末端化及びB
amH I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。 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。 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.27325)を標準技術によ
りpγCEAtrp207−1又はpKCEAtrp207−1で形質転換さ
せた。 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Pst I−Pvu I断片の開裂及び再結
合によって改変させた改変pKCEAtrp207−1及びpKCEAtr
p207−1△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pγCEA
Int2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。 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M9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(IA
A)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.,250:4007(19
75)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PAGE(10%)を用いて分画
し、銀染色剤により染色し(D.Goldman et al.,Scienc
e,211:1437(1981)、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ブロット
(Western blot)にかけた(W.N.Burnett et al.,Anal.
Biochem.,112:195(1981))。 pγCEAtrp207−1で形質転換させた細胞は、SDS PA
GE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。pKCEAtrp207−1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。これらを第8A,8B及
び8C図に示す。 第8A図は、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IAA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。 第8B図は、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pγCE
Atrp207−1比較からの抽出物であり、レーン8,9及び10
はCEA.66−E3細胞からの様々な量の抗CEA−κ鎖であ
る。 第8C図は、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pγCEAtrp207−
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。これら結果を第9図に示す。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: (細胞1g当り) E.coli(W3110/pγCEAtrp207−1*) 5mgγ E.coli(W3110/pKCEAtrp207−1*) 1.5mgκ E.coli(W3110/pKCEAtrp207−1*△,pγCEAInt2)0.5m
gκ,1.0mgγ 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: E.coli(W3110/pγCEAtrp207−1*)を5μg/mlのテ
トラサイクリンを含有する500ml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10の発酵培地に移した。増殖の際にグルコ
ースを追加し、OD 550=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OD 550=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。 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、IA
A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。 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ELISA
により測定した。マイクロタイタープレート(Dynatech
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100μ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%BSA200μ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。50μの各試
料を各ウェルに加えた。PBSに於ける0.5%BSA中10μg,5
μg,500ng,100ng,50ng,10ng,5ng及び1ngの抗−CEA/mlの
50μ試料と、ブランクとしてのPBSに於ける0.5%BSA5
0μのみとから成る標準曲線(第10図に示す)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。 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10
μ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100μを加えた。この基質を37℃
にて90分間培養した発色させた。 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,Dynatech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。 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3,00
0rpmにて20分間の遠心分離により部分清澄化させた。1m
M PMSF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。 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
(pH8),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、25℃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。 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650μを500mg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。 ng/ml 組換 E.4.キメラ抗体の作成 第11図及び第12図はネズミ抗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。 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5GGGCACTCGACACAA3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(Takahashi 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
al.,Proc.Natl.Acad.USA,79:1984(1982)(この文献
を引用して本明細書に包含する)。 第11図に示したように、クローン化ヒトγ2プラスミ
ド(pγ2)から2つの断片が得られる。第1の断片
は、Pvu IIによる消化に続きAva III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、Ava III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。(Pvu II
−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Ava III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。)pγCEA 207−1をEcoR Iで消化し、Kle
now及びdNTPで処理して付着性末端充填し、Pvu II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。 ネズミγ1遺伝子に於けるPvu II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Pvu II部位を
包囲する位置及びDNA配列と同一である。 上記断片の3方向結合から得られるプラスミド(pChi
m1)は、trpプロモーターの影響下で、ネズミ抗−CEAγ
1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。 第12図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pChim1の改変を示し
ている。まず、Nco Iで処理し、Klenow及びdNTPで平滑
末端化させ、Pvu II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。Pvu IIで処
理し、可変領域で開裂する任意の制限酵素で処理し、Kl
enow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pγ2から第2の断片を作成する。 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Xba I−Pv
u IIの断片を切断しMessing et al.,Nulice Acids Re
s.,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Adelman 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Xba
I−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。 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。 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。 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216−2
30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.,USA,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: 「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′CTAACACCATGTCAGGGTを使用して、Wa
llace et al.,Science,209:1396(1980)の方法又はAde
lman et al.,DNA,2:183(1983)の方法によってpγCE
Atrp207−1*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P32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。 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。 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:pγCEAFabtrp207−1* 第13図はpγCEAFabtrp207−1*の作成を示してい
る。5μgのpBR322をHind IIIで消化し、Klenow及びdN
TPで処理して付着性末端を平滑化し、Pst Iで消化し、B
AP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。 5μgのpγCEAtrp207−1をBamH I及びPst I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1570bpのDNA断片(断片I
I)を単離し、電気泳動の後に精製した。 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、20μgのpγ298か
ら260bpのNco I−Nde I 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(第4図)にハイ
ブリダイズし、これは次の配列を有する: 停止コドンの第3塩基を上記のpBR322開裂物の充填Hi
nd III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、20μ中に0.5mMのATPを含有する10
ユニットのT4DNA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Nco I−Nde I 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,7mM MgC
l2,7mM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/CHCl3で抽出し、エタノール沈澱
し、Bam HI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−BamH IのD
NA断片、即ち断片IIIの約50ngを単離し、精製した。 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 K12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Hind III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。 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pKCEA
trp207−1*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。
【図面の簡単な説明】
第1図は免疫グロブリンの一般的構造図であり、第2A図
及び第2B図はκ抗CEA鎖をコードするpK17G4のcDNA挿入
物の詳細な配列図であり、 第3図は対応するアミノ酸配列と共に示した第2図の断
片のコード配列図であり、 第4A図乃至第4C図はγ抗CEA鎖をコードするpγ298及び
pγ11のcDNA挿入物の結合詳細配列図であり、 第5A図及び第5B図は第4図の断片によりコードされた対
応アミノ酸配列図であり、 第6図及び第7図はそれぞれκ及びγ抗−CEA鎖に対す
る発現ベクターの作成概略図であり、 第8A,8B及び8C図はそれぞれ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写真であり、 第9図は第8図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写真であり、 第10図は抗CEA活性のELISA分析に対する標準曲線図であ
り、 第11図及び第12図はキメラ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り、 第13図は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。
及び第2B図はκ抗CEA鎖をコードするpK17G4のcDNA挿入
物の詳細な配列図であり、 第3図は対応するアミノ酸配列と共に示した第2図の断
片のコード配列図であり、 第4A図乃至第4C図はγ抗CEA鎖をコードするpγ298及び
pγ11のcDNA挿入物の結合詳細配列図であり、 第5A図及び第5B図は第4図の断片によりコードされた対
応アミノ酸配列図であり、 第6図及び第7図はそれぞれκ及びγ抗−CEA鎖に対す
る発現ベクターの作成概略図であり、 第8A,8B及び8C図はそれぞれ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写真であり、 第9図は第8図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写真であり、 第10図は抗CEA活性のELISA分析に対する標準曲線図であ
り、 第11図及び第12図はキメラ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り、 第13図は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。
─────────────────────────────────────────────────────
フロントページの続き
(73)特許権者 999999999
シテイ・オブ・ホープ
アメリカ合衆国、カリフオルニア・
91010、デユアート、イースト・デユア
ート・ロード・1450
(72)発明者 シユミユエル・カビリイ
アメリカ合衆国、カリフオルニア・
91006、アーカーデイア、サウス・セカ
ンド・アヴエニユー・325
(72)発明者 ヘルベルト・ルイス・ヒンケル
アメリカ合衆国、カリフオルニア・
94010、バーリンゲイム、イーストン・
ドライヴ・2621
(72)発明者 ウイリアム・エバンス・ホウムズ
アメリカ合衆国、カリフオルニア・
94044、パシフイカ、イーストレイク・
29
(72)発明者 アーサー・デイル・リツグス
アメリカ合衆国、カリフオルニア・
91750、ラ・ヴアーン、セント・アンド
レス・アヴエニユー・4852
(72)発明者 ロナルド・バーネル・ウエツゼル
アメリカ合衆国、カリフオルニア・
94127、サン・フランシスコ、アーバ
ノ・ドライヴ・455
(56)参考文献 特開 昭58−162599(JP,A)
特表 昭60−500892(JP,A)
Claims (1)
- (57)【特許請求の範囲】 1.ヒト由来の不変領域およびヒト以外の哺乳動物種由
来の可変領域を有する非ヒト/ヒトキメラ重鎖または軽
鎖であって、非ヒト可変領域をコードする遺伝子および
ヒト不変領域をコードする遺伝子が直接結合するよう作
製されたキメラ重鎖をコードする融合遺伝子を含有する
プラスミド、および同様に作製されたキメラ軽鎖をコー
ドする融合遺伝子を含有するプラスミドによって大腸菌
宿主を同時形質転換し、遺伝子産物を発現させ、そして
得られた発現産物を変性し再構成することによって得る
ことのできる該キメラ重鎖または軽鎖。 2.該鎖が、キメラ特性を有することとは別に、少なく
とも1個のアミノ酸の予め定められた変更、削除または
付加を有する、第1項に記載の非ヒト/ヒトキメラ重鎖
または軽鎖。 3.該変更、削除または付加が不変領域部分にある第2
項に記載の非ヒト/ヒトキメラ重鎖または軽鎖。 4.該変更、削除または付加が1〜7アミノ酸のもので
ある第2項に記載の非ヒト/ヒトキメラ重鎖または軽
鎖。 5.軽鎖がκ鎖であり、そして/または重鎖がγ鎖であ
る第1項に記載の非ヒト/ヒトキメラ重鎖または軽鎖。
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 Child Applications (2)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
JP6241576A Division 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 Division JP3559795B2 (ja) | 1983-04-08 | 1994-10-05 | 組換免疫グロブリンの調製方法 |
Publications (2)
Publication Number | Publication Date |
---|---|
JPS60155132A JPS60155132A (ja) | 1985-08-15 |
JP3162055B2 true JP3162055B2 (ja) | 2001-04-25 |
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 |
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 |
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 |
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 |
JP2001104856A Pending JP2001346591A (ja) | 1983-04-08 | 2001-04-03 | 組換免疫グロブリンの調製方法 |
Family Applications After (4)
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 |
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 |
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 |
JP2001104856A Pending JP2001346591A (ja) | 1983-04-08 | 2001-04-03 | 組換免疫グロブリンの調製方法 |
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) | ES8602119A1 (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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DE69226877T2 (de) | 1991-05-31 | 1999-03-11 | Genentech Inc | Behandlung der hiv-assoziierten immun-thrombopenie purpura |
WO1994004679A1 (en) | 1991-06-14 | 1994-03-03 | Genentech, Inc. | Method for making humanized antibodies |
GB9115364D0 (en) | 1991-07-16 | 1991-08-28 | Wellcome Found | Antibody |
WO1993006217A1 (en) | 1991-09-19 | 1993-04-01 | Genentech, Inc. | EXPRESSION IN E. COLI OF ANTIBODY FRAGMENTS HAVING AT LEAST A CYSTEINE PRESENT AS A FREE THIOL, USE FOR THE PRODUCTION OF BIFUNCTIONAL F(ab')2 ANTIBODIES |
US5686072A (en) | 1992-06-17 | 1997-11-11 | Board Of Regents, The University Of Texas | Epitope-specific monoclonal antibodies and immunotoxins and uses thereof |
WO1994009363A1 (en) | 1992-10-14 | 1994-04-28 | Board Of Regents, The University Of Texas System | Cancer diagnosis and therapy |
US5736137A (en) | 1992-11-13 | 1998-04-07 | Idec Pharmaceuticals Corporation | Therapeutic application of chimeric and radiolabeled antibodies to human B lymphocyte restricted differentiation antigen for treatment of B cell lymphoma |
EP0714409A1 (en) * | 1993-06-16 | 1996-06-05 | Celltech Therapeutics Limited | Antibodies |
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US6979556B2 (en) | 2000-12-14 | 2005-12-27 | Genentech, Inc. | Separate-cistron contructs for secretion of aglycosylated antibodies from prokaryotes |
-
1983
- 1983-04-08 US US06/483,457 patent/US4816567A/en not_active Expired - Lifetime
- 1983-04-28 KR KR1019830001806A patent/KR840008264A/ko not_active Application Discontinuation
-
1984
- 1984-04-04 AU AU26429/84A patent/AU598441B2/en not_active Expired
- 1984-04-04 NZ NZ222543A patent/NZ222543A/en unknown
- 1984-04-04 NZ NZ222542A patent/NZ222542A/en unknown
- 1984-04-04 NZ NZ207746A patent/NZ207746A/en unknown
- 1984-04-05 IE IE840/84A patent/IE57198B1/en not_active IP Right Cessation
- 1984-04-05 ZA ZA842583A patent/ZA842583B/xx unknown
- 1984-04-05 DK DK198401796A patent/DK174048B1/da not_active IP Right Cessation
- 1984-04-06 ES ES531372A patent/ES8602119A1/es not_active Expired
- 1984-04-06 EP EP84302368A patent/EP0125023B2/en not_active Expired - Lifetime
- 1984-04-06 AT AT84302368T patent/ATE64151T1/de not_active IP Right Cessation
- 1984-04-06 JP JP06987484A patent/JP3162055B2/ja not_active Expired - Lifetime
- 1984-04-06 DE DE8484302368T patent/DE3484664D1/de not_active Expired - Lifetime
- 1984-04-06 KR KR1019840001806A patent/KR840008693A/ko not_active Application Discontinuation
- 1984-04-06 IL IL7145584A patent/IL71455A/en not_active IP Right Cessation
- 1984-04-09 CA CA000451580A patent/CA1218613A/en not_active Expired
-
1988
- 1988-06-10 US US07/205,419 patent/US6331415B1/en not_active Expired - Lifetime
-
1990
- 1990-03-20 AU AU52013/90A patent/AU639910B2/en not_active Expired
-
1992
- 1992-10-15 DK DK126292A patent/DK170895B1/da not_active IP Right Cessation
-
1994
- 1994-10-05 JP JP24156594A patent/JP3559795B2/ja not_active Expired - Lifetime
- 1994-10-05 JP JP6241576A patent/JPH07194384A/ja active Pending
- 1994-11-17 HK HK129394A patent/HK129394A/xx not_active IP Right Cessation
-
1995
- 1995-02-17 CY CY179395A patent/CY1793A/xx unknown
- 1995-04-13 US US08/422,187 patent/US7923221B1/en not_active Expired - Fee Related
-
2001
- 2001-04-03 JP JP2001104857A patent/JP2001346592A/ja active Pending
- 2001-04-03 JP JP2001104856A patent/JP2001346591A/ja active Pending
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