JPH11262386A - 異種抗体の生成 - Google Patents

異種抗体の生成

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Publication number
JPH11262386A
JPH11262386A JP10352238A JP35223898A JPH11262386A JP H11262386 A JPH11262386 A JP H11262386A JP 10352238 A JP10352238 A JP 10352238A JP 35223898 A JP35223898 A JP 35223898A JP H11262386 A JPH11262386 A JP H11262386A
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Japan
Prior art keywords
locus
human
gene
cells
mouse
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Withdrawn
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JP10352238A
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English (en)
Inventor
Raju Kucherlapati
ラジュ クチェルラパティ
Aya Jakobovits
アヤ ジェイコボヴィッツ
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Amgen Fremont Inc
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Abgenix Inc
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First worldwide family litigation filed litigation Critical https://patents.darts-ip.com/?family=27041502&utm_source=google_patent&utm_medium=platform_link&utm_campaign=public_patent_search&patent=JPH11262386(A) "Global patent litigation dataset” by Darts-ip is licensed under a Creative Commons Attribution 4.0 International License.
Application filed by Abgenix Inc filed Critical Abgenix Inc
Publication of JPH11262386A publication Critical patent/JPH11262386A/ja
Withdrawn legal-status Critical Current

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    • A—HUMAN NECESSITIES
    • A01—AGRICULTURE; FORESTRY; ANIMAL HUSBANDRY; HUNTING; TRAPPING; FISHING
    • A01K—ANIMAL HUSBANDRY; AVICULTURE; APICULTURE; PISCICULTURE; FISHING; REARING OR BREEDING ANIMALS, NOT OTHERWISE PROVIDED FOR; NEW BREEDS OF ANIMALS
    • A01K67/00—Rearing or breeding animals, not otherwise provided for; New or modified breeds of animals
    • A01K67/027—New or modified breeds of vertebrates
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    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K16/00—Immunoglobulins [IG], e.g. monoclonal or polyclonal antibodies
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    • A—HUMAN NECESSITIES
    • A01—AGRICULTURE; FORESTRY; ANIMAL HUSBANDRY; HUNTING; TRAPPING; FISHING
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    • A01K67/00—Rearing or breeding animals, not otherwise provided for; New or modified breeds of animals
    • A01K67/027—New or modified breeds of vertebrates
    • A01K67/0275—Genetically modified vertebrates, e.g. transgenic
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    • A01K67/00—Rearing or breeding animals, not otherwise provided for; New or modified breeds of animals
    • A01K67/027—New or modified breeds of vertebrates
    • A01K67/0275—Genetically modified vertebrates, e.g. transgenic
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    • C07—ORGANIC CHEMISTRY
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    • C07K16/00—Immunoglobulins [IG], e.g. monoclonal or polyclonal antibodies
    • C07K16/12—Immunoglobulins [IG], e.g. monoclonal or polyclonal antibodies against material from bacteria
    • C07K16/1267—Gram-positive bacteria
    • C07K16/1282—Clostridium (G)
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K16/00—Immunoglobulins [IG], e.g. monoclonal or polyclonal antibodies
    • C07K16/18—Immunoglobulins [IG], e.g. monoclonal or polyclonal antibodies against material from animals or humans
    • C07K16/24—Immunoglobulins [IG], e.g. monoclonal or polyclonal antibodies against material from animals or humans against cytokines, lymphokines or interferons
    • C07K16/241—Tumor Necrosis Factors
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K16/00—Immunoglobulins [IG], e.g. monoclonal or polyclonal antibodies
    • C07K16/18—Immunoglobulins [IG], e.g. monoclonal or polyclonal antibodies against material from animals or humans
    • C07K16/24—Immunoglobulins [IG], e.g. monoclonal or polyclonal antibodies against material from animals or humans against cytokines, lymphokines or interferons
    • C07K16/244—Interleukins [IL]
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K16/00—Immunoglobulins [IG], e.g. monoclonal or polyclonal antibodies
    • C07K16/18—Immunoglobulins [IG], e.g. monoclonal or polyclonal antibodies against material from animals or humans
    • C07K16/24—Immunoglobulins [IG], e.g. monoclonal or polyclonal antibodies against material from animals or humans against cytokines, lymphokines or interferons
    • C07K16/244—Interleukins [IL]
    • C07K16/248—IL-6
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K16/00—Immunoglobulins [IG], e.g. monoclonal or polyclonal antibodies
    • C07K16/18—Immunoglobulins [IG], e.g. monoclonal or polyclonal antibodies against material from animals or humans
    • C07K16/28—Immunoglobulins [IG], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants
    • C07K16/2803—Immunoglobulins [IG], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants against the immunoglobulin superfamily
    • C07K16/2812—Immunoglobulins [IG], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants against the immunoglobulin superfamily against CD4
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K16/00—Immunoglobulins [IG], e.g. monoclonal or polyclonal antibodies
    • C07K16/18—Immunoglobulins [IG], e.g. monoclonal or polyclonal antibodies against material from animals or humans
    • C07K16/28—Immunoglobulins [IG], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants
    • C07K16/2851—Immunoglobulins [IG], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants against the lectin superfamily, e.g. CD23, CD72
    • C07K16/2854—Immunoglobulins [IG], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants against the lectin superfamily, e.g. CD23, CD72 against selectins, e.g. CD62
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
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    • C07K16/00—Immunoglobulins [IG], e.g. monoclonal or polyclonal antibodies
    • C07K16/18—Immunoglobulins [IG], e.g. monoclonal or polyclonal antibodies against material from animals or humans
    • C07K16/28—Immunoglobulins [IG], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants
    • C07K16/2875—Immunoglobulins [IG], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants against the NGF/TNF superfamily, e.g. CD70, CD95L, CD153, CD154
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K16/00—Immunoglobulins [IG], 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
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    • C12N15/79—Vectors or expression systems specially adapted for eukaryotic hosts
    • C12N15/85—Vectors or expression systems specially adapted for eukaryotic hosts for animal cells
    • C12N15/8509—Vectors or expression systems specially adapted for eukaryotic hosts for animal cells for producing genetically modified animals, e.g. transgenic
    • A—HUMAN NECESSITIES
    • A01—AGRICULTURE; FORESTRY; ANIMAL HUSBANDRY; HUNTING; TRAPPING; FISHING
    • A01K—ANIMAL HUSBANDRY; AVICULTURE; APICULTURE; PISCICULTURE; FISHING; REARING OR BREEDING ANIMALS, NOT OTHERWISE PROVIDED FOR; NEW BREEDS OF ANIMALS
    • A01K2207/00—Modified animals
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    • A—HUMAN NECESSITIES
    • A01—AGRICULTURE; FORESTRY; ANIMAL HUSBANDRY; HUNTING; TRAPPING; FISHING
    • A01K—ANIMAL HUSBANDRY; AVICULTURE; APICULTURE; PISCICULTURE; FISHING; REARING OR BREEDING ANIMALS, NOT OTHERWISE PROVIDED FOR; NEW BREEDS OF ANIMALS
    • A01K2217/00—Genetically modified animals
    • A—HUMAN NECESSITIES
    • A01—AGRICULTURE; FORESTRY; ANIMAL HUSBANDRY; HUNTING; TRAPPING; FISHING
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    • A01K2217/05—Animals comprising random inserted nucleic acids (transgenic)
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    • A01—AGRICULTURE; FORESTRY; ANIMAL HUSBANDRY; HUNTING; TRAPPING; FISHING
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    • A01K2217/07—Animals genetically altered by homologous recombination
    • A01K2217/072—Animals genetically altered by homologous recombination maintaining or altering function, i.e. knock in
    • A—HUMAN NECESSITIES
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Abstract

(57)【要約】 【課題】 免疫原に応答し、ヒト抗体又はそのアナログ
を生成する非霊長類哺乳動物細胞及びその製造方法並び
にその製造のために使用されるベクター及び細胞を提供
する。 【解決手段】 不活性化ベクターを用い相同組換え事象
により非霊長類哺乳動物の内在性免疫グロブリン遺伝子
座を不活性化し、かつ、該非霊長類哺乳動物のゲノム中
にヒト免疫グロブリン遺伝子を導入することにより、内
在性免疫グロブリン遺伝子を産生する能力を欠き、ヒト
免疫グロブリンを産生する能力を有するトランスジェニ
ック非霊長類哺乳動物が得られる。

Description

【発明の詳細な説明】
【０００１】
【発明の属する技術分野】本発明の分野は種々の哺乳類
宿主における異種移植された特異的結合たんぱく質の生
産に関する。
【０００２】
【従来の技術】モノクローナル抗体は診断および治療に
有用である。それらの特異的エピトープに対する結合を
利用してそのエピトープを有する分子を同定したり、ま
たそれら自身または他のものと組合わせて特定の部分に
指向させ診断や治療を行うこともできる。
【０００３】モノクロナール抗体には重鎖と軽鎖があ
り、それらが結合してエピトープに対する結合領域を形
成している。これらの鎖の各々は可変部と不変部から成
り立っている。不変部のアミノ酸配列はその抗体を生産
する宿主およびその抗体の特定のイソタイプに特異的で
ある。
【０００４】不変部の配列およびその抗体を生産する種
との関係からその宿主の循環系への異種抗体の導入は免
疫応答を起こす。異種抗体を慢性病などの場合に反復し
て導入するとそれが速やかに破壊されるか、また悪影響
をもつためその抗体の投与は実際には行なえない。それ
ゆえ、同系または同種抗体源を提供する努力がはらわれ
てきた。１つの方法として、その宿主由来の重鎖および
軽鎖遺伝子を同定し、不変部をコードする領域を同定す
る組換えＤＮＡ技術がある。これらの領域を特定のエピ
トープを指向する他の種の免疫グロブリン遺伝子と結合
させた。
【０００５】
【発明が解決しようとする課題】しかしながら、生成し
た部分的異種キメラ抗体は全体的異種抗体よりも実質的
に有用であるが多くの欠点も有している。その可変およ
び不変部の同定、単離および結合は実質的な研究を必要
とする。さらに、ある種の不変部の他の種の可変部への
結合はその可変部の特異性やアフィニティーを変化さ
せ、その可変部の望ましい性質を失うこともある。ま
た、その可変部における種特異的な枠組みや超可変配列
がある。これらの枠組みや超可変配列は不都合な抗原応
答を示すかもしれない。それゆえ、目的の免疫原で宿主
を免疫化して宿主に抗体する同種抗体を作ることがより
好ましいことである。霊長類特にヒトにはこの方法は実
践的ではない。生産されたヒト抗体は目的のエピトープ
に対して予め免疫化された宿主に由来する脾臓の偶発的
な提供に基づいている。ヒトの末梢血液リンパ球をモノ
クロナール抗体の生産に使用し得るが特に融合はうまく
行なわれておらず通常IgＭのみに限られる。さらにヒト
のたんぱく質、すなわち多くの治療および診断における
標的に対するヒトの抗体応答を生成させるのは特に難し
い。それゆえヒトの同種抗体生成に対する別の経路を見
つけることは興味深い。
【０００６】（関連文献）トーマス（Thomas）およびカ
ペチ（Capecchi）、Cell、５１、５０３−５１２、１９
８７。コラー（Koller）およびスミシーズ（Smithies）
Proc．Natl．Acad．Sci ．ＵＳＡ、８６、８９３２−８
９３５、１９８９。この文献は胚幹細胞における相同組
換えによるＢ２ミクログロブリン遺伝子座の不活性化を
報告している。バーマン（Berman）等、ＥＭＢＯ、Ｊ、
７、７２７−７３８、１９８８、はヒトIgＶＨ部位につ
いて報告している。バーク（Burke)等、Science 、２３
６、８０６−８１２、１９８７はイーストの人工的染色
体ベクターについて報告している。またガルザ（Garza)
等、Science 、２４６、６４１−６４６、１９８９およ
びブラウンスタイン（Brown Stein)等、Science 、２４
４、１３４８−１３５１、１９８９参照。サカノ（Saka
no) 等は免疫グロブリン重鎖遺伝子の多様性セグメント
について報告している。ターカー（Turcker)等、Proc．
Natl．Acad．Sci ．ＵＳＡ、７８、７６８４−７６８
８、１９８１はマウスIgＡ重鎖遺伝子配列について報告
している。ブランケンスタイン（Blanken Stein)および
クルウィンケル(Kruwinkel) 、Eur ．J ．Immol ．、１
７、１３５１−１３５７、１９８７はマウスの可変重鎖
領域について報告している。また、ジョイナー(Joyner)
等、Nature、３３８、１５３−１５５、１９８９、トラ
バー（Traver）等、Proc．Natl．Acad．Sci ．ＵＳＡ、
８６、５８９８−５９・２、１９８９およびパンチス
（Panchis)等、Proc．Natl．Acad．Sci ．ＵＳＡ、８
７、５１・９−５１１３、１９９０参照。
【０００７】
【課題を解決するための手段】異種特異的結合たんぱく
質を適当な免疫原で哺乳類宿主を免疫化することにより
非霊長類の哺乳類宿主中で生産した。
【０００８】この宿主は、（１）内在する免疫グロブリ
ンを生産できない；（２）外来免疫グロブリン遺伝子座
が少なくとも１つの免疫グロブリン不変部またはそのた
んぱく質、軽鎖および重鎖の少なくとも１つの可変部成
分を提供する免疫グロブリン配列、および機能性免疫グ
ロブリンサブユニットの切断および構築を目的とする適
当なスプライシング部位をもつ少なくとも１つのイント
ロンを含む、以上（１）および（２）を特徴とするもの
である。したがって、哺乳類宿主は内在または外来の免
疫グロブリン遺伝子座の機能性Ｊ領域をスプライシング
によって生成し得る少なくとも１つの異種不変部または
そのたんぱく質を含み、その宿主の全免疫グロブリン遺
伝子座は一部または全部の異種免疫グロブリン遺伝子座
で置換されていることもあるし、また宿主細胞の染色体
および不活性化した内在免疫グロブリン領域に挿入した
形で異種免疫グロブリン遺伝子座を有することもある。
これらの種々の代替法は少なくとも部分的に重鎖および
軽鎖について免疫グロブリン遺伝子座における相同組換
えを使用することによって行なわれる。
【０００９】
【発明の実施の形態】霊長類以外、特にヒト以外の新し
いトランスジェニック哺乳類宿主で、ある免疫原に対す
る免疫応答を発現し、その応答が霊長類、特にヒトの不
変および、または可変部または目的とするそのような別
のエクェクターペプチド配列を有する抗体を生成するも
のが提供される。この宿主は内在する免疫グロブリンサ
ブユニットをコードする遺伝子座の置換および、または
不活性化の結果として異種または修正した抗体を生産し
得ることを特徴とする。この修正は機能性ペプチドへＣ
末端で結合した可変部結合部位の構築を提供する不変部
の少なくとも１部を維持している。この機能性ペプチド
は多くの形や構造をとり得るし、また酵素、成長因子、
結合たんぱく質、リガンド、サイトカイン、エフェクタ
ーたんぱく質、キレートたんぱく質などとしても働き得
る。この抗体はどのイソタイプ、すなわち、IgＡ、Ｄ、
Ｅ、ＧまたはＭ、またはイソタイプのサブタイプもとり
得る。目的のトランスジェニック宿主を得るために多く
の戦術をとり得る。種々のトランスジェニック宿主を使
用し得る。この中には特に、マウス、ウサギ、ヒツジ、
ブタ、ウマ、イヌ、ネコなど通常は霊長類以外のものが
含まれる。ほとんどの場合、抗体の生産のための不朽化
に使用するＢ−リンパ球の生産にはマウスが使用され
る。マウスは扱いやすく、大量に増やせ、かつ非常に広
い免疫レパートリーを有することが知られているので、
通常マウスが選ばれる。それゆえ以下の議論ではマウス
に関して述べるが、同様の操作に従い他の動物、特に哺
乳類もマウスと容易に置換し得る。１つの方策では各ス
テップとして、ヒトの重鎖および軽鎖免疫グロブリン遺
伝子複合体をマウスの生殖系列に導入するが、別のステ
ップにおいて、対応するマウス遺伝子は機能を失わせら
れる。ヒトの重鎖および軽鎖遺伝子を適当な真核または
原核性微生物中で再構築し、生成したＤＳＡフラグメン
トは受精したマウス卵母細胞または胚幹細胞の前核に導
入し得る。内在性マウス免疫グロブリン遺伝子座の不活
性化はマウス胚幹細胞における相同組換えによる適当な
遺伝子の破壊によって行なわれる。各々の場合部分的に
修正した胚幹細胞から誘導され、胚系列から遺伝的修正
を伝達し得るキメラ動物ができる。ヒトの免疫グロブリ
ン遺伝子座をもつマウスと不活性化したマウスとの生殖
で純粋にヒトの抗体のみを作る動物が出来上る。
【００１０】次の戦術では、ヒトの重鎖および軽鎖免疫
グロブリン遺伝子のフラグメントを用いてマウス胚幹細
胞における相同組換えを利用し直接対応するマウス遺伝
子を置換する。つづいて胚幹細胞由来の細胞が生殖系列
に寄与するキメラトランスジェニック動物を作製する。
【００１１】これらの戦術は、多くの動物における免疫
グロブリン鎖遺伝子の既知の組織に基づいている。とい
うのは組織、個々のドメインをコードするエクソンの相
対的位置、スプライス部位や転写要素の位置などの理解
の程度は様々である。ヒトの場合、免疫グロブリン重鎖
遺伝子は染色体１４の上にある。転写の５´→３´方向
で、この遺伝子座は大きな一群の可変部遺伝子
（ＶＨ）、多様性（Ｄ）領域遺伝子、つづいて連結（Ｊ
Ｈ）領域遺伝子および不変（ＣＨ）遺伝子群を含む。こ
の遺伝子座の大きさは約２．５００キロベース(kb)と見
積られる。Ｂ−細胞発生の際、生殖系列IgＨ遺伝子座由
来の不連続な遺伝子セグメントはＤＮＡの物理的再配列
により並置される。生産すべき機能性重鎖Igポリペプチ
ドを得るため、Ｖ Ｈ、ＤおよびＪＨ領域由来の３つの不
連続なＤＮＡセグメントは特定の配列ＶＨ−ＤＪＨで結
合しなければならない。この配列は機能性ユニットＶＨ
ＤＪＨを生ずる。一度ＶＨ−ＤＪＨが生成してしまえ
ば、エクソンとイントロンを含む特異的ＶＨ−ＤＪＨＣ
Ｈをテンプレートとして用いて、Ig遺伝子座の転写につ
づいて特異的重鎖が生産される。Ig軽鎖にはヒト染色体
２上のκ遺伝子座およびヒト染色体２２上のλ遺伝子座
の２つがある。IgＬ遺伝子座の構造はＤ領域がないこと
以外IgＨ遺伝子座の構造と同じである。IgＨの転位につ
づいて、軽鎖遺伝子座の転位も同様にκまたはλ鎖のＶ
ＬおよびＪＬ結合によって行なわれる。λおよびκ遺伝
子座のサイズは各々約１０００kbである。特定のＢ−細
胞における転位IgＨおよびIgκまたはIgλ軽鎖の発現は
抗体分子の生成を可能にする。IgＨｈｕ遺伝子座を単
離、クローン化および転移させるためにイーストの人工
的染色体を使用できる。１つまたは数個のイースト人工
染色体（ＹＡＣ）クローンの中に全IgＨｈｕ遺伝子座を
含ませる。このことはIg軽鎖遺伝子座についても同様で
ある。つづいて適当な重鎖または軽鎖ＹＡＣクローンを
イースト受容細胞に導入し、ホモロジーの重複領域間の
相同組換えにより、本来の生殖系列Ig遺伝子座の再構成
を行う。このようにしてヒトIg鎖をコードするＤＮＡフ
ラグメントが単離できる。
【００１２】広範囲の高アフィニティー抗体を得るため
に１つが全Ｖ領域を含む必要はない。種々のＶ領域遺伝
子群がＶ領域クラスター内に散在している。したがっ
て、Ｖ領域の全補足物よりもむしろヒト重鎖および軽鎖
Ig遺伝子座の既知Ｖ領域遺伝子の一部を得ることにより
（バーマン（Berman）等、ＥＭＢＯ．Ｊ．（１９８８）
７：７２７−７３８）、トランスジェニック宿主は免疫
化され、強い免疫応答を所持し、高アフィニティー抗体
を提供し得る。この様にして、染色体の比較的小さいＤ
ＮＡフラグメント、たとえば第１ｂ図に示したIgＨｈｕ
遺伝子座の６７０kbフラグメントが使用できる。このNo
t Ｉ−Not Ｉ制限フラグメントは種々のＤおよびＪ領域
の組換えおよび体細胞変異により多様性が増加する非常
に多様なＶ領域を提供する。
【００１３】異種宿主におけるヒト抗体の生産のために
はその宿主が抗体生産に関して必要な酵素や他の因子を
提供し、一方では免疫グロブリンの重鎖および軽鎖サブ
ユニットの発現と競合する内在性遺伝子を欠いている必
要がある。したがって、生殖系列転位、スプライシン
グ、体細胞変異などに関する酵素や他の因子は異種宿主
中で機能的である。欠いているものは内在性免疫グロブ
リンサブユニットの生産に関する種々のエクソンを含む
機能性天然領域である。
【００１４】このヒトＤＮＡを受精した卵母細胞または
胚幹細胞の前核に導入する。この組込みは採用する戦術
によりランダムまたは相同的に行なわれる。反復ステッ
プまたはブリーディングと組合せたトランスホーメーシ
ョンを用いて宿主免疫グロブリンの軽鎖または重鎖サブ
ユニットを実質的に含まないヒト抗体を生産し得るトラ
ンスジェニック動物が得られる。
【００１５】このヒト免疫グロブリン遺伝子座を不活性
化するために、内在性免疫グロブリンサブユニットの生
産を阻害する免疫グロブリン重鎖および軽鎖遺伝子座に
ＤＮＡを導入する相同組換えを用いる。２つの重鎖対立
遺伝子および各２つの対立遺伝子を含む２つの軽鎖遺伝
子座があるのでλ遺伝子座を無視することもできるが各
々の対立遺伝子の不活性化を起こす多重トランスホーメ
ーションがなければならない。（トランスホーメーショ
ンとはたとえば接合、トランスホーメーション、トラン
スフェクション、トランスダクション、エレクトロポレ
ーション、リポフェクション、バイオリスティクスなど
生細胞にＤＮＡを導入する技術を示している）。相同組
換えを用いて胚幹細胞へ相同的ＤＮＡを導入し、その修
正細胞を受容性胚盤胞に導入することによりその遺伝子
座の各々を機能的に不活性化させる。つづく育生でその
不活性化遺伝子座の生殖系列伝達が可能となる。それゆ
え、ヘテロ接合体の子供を育てヘテロ接合体の親からホ
モ接合体の子供を選択するか、または再び匹敵する遺伝
子座の相同組換えおよび不活性化のために胚幹細胞を使
用し得る。
【００１６】トランスホーメーションのステップ数は類
似する内在性免疫グロブリンとの相同組換えのためのヒ
ト免疫グロブリンサブユニット遺伝子座の少なくともフ
ラグメントを提供することにより減少することができ、
その結果ヒトの遺伝子座は宿主の免疫グロブリンサブユ
ニット遺伝子座の不活性化を伴って宿主免疫グロブリン
遺伝子座の少なくとも一部の置換が起こる。単一の不活
性化を起こすトランスホーメーションとホモ接合体の子
供を生ずるヘテロ接合体の子供の育生は特に興味深い。
ヒト遺伝子座を不活性化のための宿主遺伝子座に対する
置換または挿入に使用する場合、トランスホーメーショ
ンの数は３回に限られ、またすでに示したようにあまり
使用されないλ遺伝子座を無視しトランスホーメーショ
ンを２回に限ることもできる。それとは別に各遺伝子座
の不活性化に予め１つ以上の不活性化した遺伝子座を有
する子孫由来の胚幹細胞を用いた別のステップを行うこ
ともできる。この場合はトランスホーメーションのみを
使用し、ヒトの遺伝子座はランダムに宿主ゲノムに組込
まれ、合わせて８回のトランスホーメーションを要して
もよい。
【００１７】不活性化のためにその遺伝子座の免疫グロ
ブリンサブユニットの発現を阻止する標的遺伝子座にお
けるいかなる障害も使用し得る。したがって、この障害
はＶ、ＪまたはＣ領域中のエンハンサー、たとえば５´
側上流またはイントロンを含む領域中および重鎖（この
機会はＤ領域に存在する）またはこれらを組合せた領域
で起こる。したがって重要な因子はIg生殖系列遺伝子転
位が阻害されるか、または免疫グロブリンサブユニット
をコードする機能的メッセージが転写の失敗かまたはそ
のメッセージのグロセシングの失敗などにより生産され
ないことである。免疫グロブリンサブユニット遺伝子座
の不活性化だけを考える場合、障害は免疫グロブリンサ
ブユニット遺伝子座のＪ領域に導入することが望まし
い。したがって、機能性Ｊ領域を欠き、かつＪ領域の上
流または下流に隣接してＪ領域の配列を含むか、または
Ｊ領域に不活性化を起こす挿入があるその領域の全部ま
たは一部を含む構築物を作製する。この挿入は５０bp以
上であり、このような挿入は機能性ｍＲＮＡの形成を破
壊する。Ｊ領域全体または一部、通常この遺伝子座の少
なくとも約７５％、好ましくは少なくとも約９０％を欠
失していることが望ましい。好ましいなら、相同的領域
である２つの隣接配列間の障害はＪ領域を越えて可変部
および、または不変部まで拡張し得る。
【００１８】マーカー遺伝子を用いてこのＪ領域を置換
することが望ましい。様々なマーカーが使用できるが特
にポジティブ選択が可能なものが良い。ネオマイシンホ
スホトランスフィラーゼ遺伝子を発現するＧ４１８耐性
が特に興味深い。標的遺伝子構築物の上流および、また
は下流には２重交叉が起こっているかどうかを同定でき
る遺伝子を置く。この目的にはヘルペスシンプレックス
スウイルスのチミジンキナーゼ遺伝子が使われる。とい
うのはチミジンキナーゼ遺伝子を発現する細胞はアシク
ロビアまたはガンシクロビアなどのヌクレオシドアナロ
グの使用、つまり機能性ＨＳＶ−ｔｋ遺伝子を含む細胞
へのこれらの細胞毒性により死滅するからである。これ
らヌクレオシドアナログに対する感受性の欠除はＨＳＶ
−チミジンキナーゼ遺伝子の欠除を示し、つまり、相同
組換えにより二重交叉が起こっていることを示してい
る。
【００１９】ゲノム中のマーカー遺伝子の存在は組込み
が起こったことを示しているが、相同組込みが起こった
かどうかを決定する必要がある。これはいくつかの方法
で行うことができるが、ほとんどの場合、組込みの位置
を決めるのにＤＮＡ分析が行われる。この構築物の隣接
領域を越えた標的遺伝子座の存在に関し、挿入物に対す
るプローブを用い、かつその挿入物に隣接する５´側お
よび３´側領域を配列決定することにより、または欠失
が導入された場合その欠失を同定することにより望まし
い組込みが起こったことを確認する。
【００２０】相同組換えの検出にポリメラーゼチェーン
リアクション（ＰＣＲ）を使用できる。その構築物内の
配列に相補的であるプローブと構築物の外側や標的遺伝
子座の配列に相補的であるプローブが使用される。この
ようにして、相同組換えが起こった場合、相補鎖中に存
在する両方のプライマーを有するＤＮＡ鎖のみを得るこ
とができる。期待される大きさの配列を生ずるプローブ
の存在を示すことにより相同組換えが支持される。さら
にこの構築物には哺乳類宿主細胞中で機能的な複製シス
テムが含まれる。ほとんどの場合、これらの複製システ
ムにはシミアンウイルス４０、エプスタインーバーウイ
ルス、ポリオーマウイルス、パピローマウイルスなどの
ウイルス複製システムが含まれる。ＳＶ４０、メタラチ
オネイン−ＩおよびII遺伝子、β−アクチン遺伝子、ア
デノウイルス前期および後期遺伝子、ホスホグリセレー
トキナーゼ遺伝子、ＲＮＡポリメラーゼII遺伝子などウ
イルスまたは哺乳類遺伝子由来の種々の転写開始システ
ムが使用される。プロモーターに加えて、野生型エンハ
ンサーを用いマーカー遺伝子の発現をさらに促進するこ
とができる。相同組換えのための構築物を作製する場
合、この構築物の調製、各操作後のクローニング、制限
地図作成や配列決定などの解析、目的配列の増幅や単離
用に原核生物、特に大腸菌の複製システムが含まれる。
この構築物が大きい場合、一般に約５０kbを越える場
合、通常１００kbを越える場合で通常約１００kbp を越
えない場合イーストの人工染色体（ＹＡＣ）をこの構築
物のクローニングを使用する。
【００２１】この構築物を調製し、かつ原核生物の配列
など不都合な配列が除去されるとこれを標的細胞に導入
する。ＤＮＡを標的細胞に導入する簡便な方法が採用さ
れる。この方法にはスフェロプラスト融合、リポフェク
ション、エレクトロポレーション、カルシウム細胞法ま
たは直接的なマイクロインジェクションが含まれる。標
的細胞のトランスホーメーションまたはトランスフェク
ション後、先に示したネオマイシン耐性やアシクロビア
またはガンシクロビア耐性などポジィティブおよび、ま
たはネガティブマーカーにより標的細胞を選択する。望
ましい発現型を示す細胞はさらに制限分析、電気泳動、
サザン分析、ＰＣＲなどでさらに解析する。標的遺伝子
座の障害を示すフラグメントを同定することにより相同
組換えが起こり標的遺伝子座のコピーが不活性化した細
胞を同定し得る。
【００２２】上述の方法はまず胚幹細胞中の重鎖遺伝子
座を用いて行い、ついでこの細胞を成熟させることによ
り成熟した増殖性宿主が提供される。ついでヘテロ接合
性宿主を育生することにより、ホモ接合性宿主が得られ
ることもあり、また胚幹細胞を単離し、かつトランスホ
ームして第２のIgＨ遺伝子座を不活性化することもでき
る。そして望ましい全ての遺伝子座が不活性化するまで
このプロセスを繰り返した。それとは別に、軽鎖遺伝子
座で始めることもできる。いずれの段階でもヒトの遺伝
子座を導入し得る。すでに示したように標的遺伝子座を
類似するヒト遺伝子座と置換できる。このようにして類
似する宿主遺伝子座と同じ領域にヒト遺伝子座に置き、
その結果その遺伝子座の位置に関するいかなる調節もヒ
ト免疫グロブリン遺伝子座と実質的に同じとなる。たと
えば全ＶＨ遺伝子座（Ｖ、ＤおよびＪ配列を含む）また
はその一部を単離することおよびマウスの遺伝子座由来
の配列とヒト遺伝子座を宿主遺伝子座中好ましくは少な
くとも約５kbp 離して、より好ましくは少なくとも約１
０kbp 離して置くことにより宿主免疫グロブリン遺伝子
座の可変部とヒト免疫グロブリン遺伝子座を置換する組
換え事象においてこの領域にヒトのフラグメントを挿入
できる。このようにして宿主の内在性免疫グロブリンサ
ブユニットを生産する能力を破壊できるが、ヒトの免疫
グロブリン遺伝子座のプロモーターは宿主エンハンサー
によって活性化されかつ宿主の調節システムで調節され
る。
【００２３】相同組換えまたはランダム組込みにより宿
主ゲノム中にヒト遺伝子座が導入され、かつ種々のトラ
ンスジェニックまたは変異動物を適当に育生させること
により内在性免疫グロブリン遺伝子座が不活性化した宿
主動物ができれば内在性免疫グロブリンサブユニットを
生産する本来の能力を欠くがヒトのレパートリーの少な
くとも一部を含むヒト免疫グロブリンを生成する能力を
有する宿主が得られる。
【００２４】宿主がヒトのIgＨおよびヒトのIgκおよ
び、またはλ遺伝子座を含む場合、３つの宿主Ig遺伝子
座各々の２つのコピーを機能的に不活性化することは宿
主または宿主／ヒトキメラ抗体を生産することなしに純
粋にヒト抗体を生産し得る。特異的抗原で免疫化するこ
とによりこのような宿主株は特異的ヒト抗体を生産する
マウスＢ細胞を生産するであろう。このＢ細胞はヒトモ
ノクローナル抗体を継続的に生産させるためマウスミエ
ローマ細胞と融合するか、またはいずれかの他の方法で
不朽化する。
【００２５】本方法および戦術は完全な免疫グロブリン
の生産に限定する必要はなく、たとえばＣＨ１´、Ｃ
Ｈ２´、ＣＨ３´またはＣＨ４´またはこれらの組合わ
せ物など不変部の一部に結合した領域を提供する機会を
与える。それとは別に１つ以上のＣＨおよびＣκまたは
Ｃλ領域のエクソンは；たとえばプラスミノーゲン活性
化因子、スーパーオキサイドジスミューターゼなどの酵
素；リシン、アブリン、ジフテリア毒などのトキシンＡ
鎖；成長因子；ＴＮＦなどの細胞毒のような種々のたん
ぱく質をコードする配列と置き換わるか、または結合し
得る。たとえばＷＯ ８９／０７１４２；ＷＯ ８９／
０９３４４およびＷＯ ８８／０３５５９参照。目的の
たんぱく質を不変領域に挿入して可変部の修正不変部エ
クソンへのスプライシングを提供することにより、生成
する結合たんぱく質は免疫グロブリンとは異なるＣ末端
部分をもつことになる。挿入遺伝子に停止配列を与える
ことにより、このたんぱく質産物はＣ末端部分に挿入た
んぱく質をもつことになる。望ましいなら、可変部を他
のたんぱく質に結合するための適当なスプライス部位を
含む構築物を作製することにより不変部を他のたんぱく
質とそっくり置換することができる。抗体または抗体ア
ナログを生産するトランスジェニック宿主由来のＢ細胞
はマウスミエローマ細胞と融合しハイブリドーマを作る
か、またはたとえばオンコジーンによるトランスフェク
ションなど他の簡便なプロセスにより不朽化するのに使
用される。これらの不朽化細胞は連続培養するか、また
は腹水生産のために同様の宿主の腹腔に導入する。
【００２６】本発明はポリクローナルヒト抗血清、また
はヒトモノクローナル抗体または抗体アナログの生産を
提供する。哺乳類宿主を免疫原で免疫化した場合に生成
するヒト抗体はプロテインＡなどFc結合部を有するアク
ィニティーカラムなどを用いることにより他のたんぱく
質から単離する。
【００２７】胚幹細胞から動物を生産するためトランス
ホーメーション後にこの細胞をたとえばウシ胎児血清で
活性化したＤＭＥＭなど適当な培地中の支持細胞層に置
く。構築物を含む細胞は選択培地を用いて検出し、コロ
ニー成長のための十分な時間の後このコロニーをピック
アップし組込みまたは相同組換えの発生を分析する。先
に示したように構築物の内または外にあるが標的遺伝子
座にはないプライマーを用いたＰＣＲを使用できる。
【００２８】相同組換えを示すコロニーは胚操作および
胚盤胞注入に使用する。胚盤胞は排卵から３〜５日後子
宮を洗い出すことにより母体から得られる。胚幹細胞を
トリプシン処理した後修正した細胞を胚盤胞を含む液滴
に加える。少なくとも１個最高３０個の修正・胚幹細胞
を胚盤胞の胞胚腔に注入する。注入後、少なくとも１
個、せいぜい約１５個の胚盤胞を擬似妊娠母体の各子宮
に戻す。それからこの母体に子供を産ませ、構築物を含
む変異細胞についてその子供をスクリーニングした。
【００２９】哺乳類動物はヒト以外、特に霊長類以外の
マウス、ラット、モルモットなどの実験動物、家畜、ペ
ットなどが使用される。以下の例は説明を目的としたも
ので本発明を制限するものではない。
【００３０】
【実施例】［実施例１］マウス重鎖Ｊ遺伝子の不活性化 （１）不活性化ベクターの構築 マウス重鎖Ｊ遺伝子および隣接配列を含む６．４kb Ｅ
coＲＩフラグメントをサカノ（Sakano）等、Nature２９
０、５６２−５６５、１９８１に報告されているプロー
ブを用いてBal b/c マウス胚ゲノムライブラリーからク
ローン化する。このフラグメント(mＤＪ）をＥcoＲＩ消
化したｐＵＣ１９プラスミド（pmＤＪ）に挿入する。４
Ｊ遺伝子を含む２．９kbフラグメントをＸhoＩ−ＳcaＩ
消化によって欠失させる（pmＤＳＪＮeo、図Ｉ参照）。
ヘルペスシンプレックスウイルスチミジンキナーゼ遺伝
子（ＨＳＶ−ｔｋ）プロモーターおよびポリオーマエン
ハンサーでコントロールされるネオマイシン耐性遺伝子
を含む１１５０bpＸhoＩ−ＢamＨＩフラグメントをp Ｍ
Ｃ１Ｎeoから単離する（トーマス（Thomas）およびカペ
チ（Capecchi）、Cell、５１、５０３−５１２、１９８
７）。合成アダプターをこのフラグメントに付加しＢam
ＨＩ末端をＳcaＩ末端に変換し、生成したフラグメント
をＸhoＩ−ＳcaＩ pmＤδＪに結合して、５´から３´
方向のネオマイシンおよび重鎖プロモーターの順序が同
じである不活性化ベクター（pmＤδＪ、Ｎeo）を作製す
る。このプラスミドをＥＳ細胞へのトランスフェクショ
ン前にＮdeＩ消化で線状化する。相同組換え事象を推進
する配列は各々ネオマイシン遺伝子の５´側および３´
側に存在する３kbおよび０．５kbフラグメントである。
【００３１】基本的に報告されているマイトマイシン処
理初期胚フィブロプラスト支持細胞層上で（ドーチマン
（Doetschman）等、Ｊ．Embryol.Exp.Morphol.８７、２
７−４５、１９８５）、ＥＳ細胞系列Ｅ１４ＴＧ２ａ
（フーパー（Hooper）等、Nature、３２６、２９２−２
９５、１９８７）を培養する。胚フィブロブラストは１
４〜１７日前にネオマイシントランスジーンとホモ接合
のオスと交配したメスのＣ５７ＢＬ／ｂ由来の胚から調
製する（ゴスラー（Gossler)等、ＰＮＡＳ８３、９０６
５−６０６９、１９８６）。これらの細胞はＧ４１８を
含む培地で増殖し得る。エレクトロポーション条件はボ
グス（Boggs)等、Ex.Hematol. （ＮＹ）１４９、９８８
−９９４、１９８６に報告されている。ＥＳ細胞をトリ
プシン処理し、４×１０７／ｍｌ濃度となるように培養
培地に懸濁してから、最初の実験では１２ｎＭ濃度のＤ
ＮＡ存在下で、また第２の実験では５ｎＭ ＤＮＡの存
在下でエレクトロポレーションする。１５０〜２５０μ
Ｆの容量で３００Ｖの電圧が５mm長および１００mm２断
面積のエレクトロポレーションセルの場合至適条件であ
ることが分った。５×１０６個のエレクトロポレーショ
ンした細胞を１５％ウシ胎児血清（ＦＢＳ）および０．
１ｍＭ ２−メルカプトエタノールを補ったダルベコ修
正イーグル培地（ＤＭＥＭ）を含む１００mmプレート中
のマイトマイシン処理したフィブロブラスト上にプレー
ティングする。この培地はエレクトロポレーションから
２４時間後２０μｇ／ｍｌＧ４１８を含む培地と置き換
える。
【００３２】エレクトロポレーションから１０〜１４日
後に生ずるＥＳコロニーをキャピラリーピペットで吸い
とりＰＣＲ分析に使用する。採取コロニーの半分を予め
マイトマイシン処理支持細胞を接種した１４穴プレート
に保存する。３〜４個のプールを合せた他の半分を約
０．５ｍｌ ＰＢＳを含むエッペンドルフチューブに移
し、ＰＣＲによる相同組換えの分析に使用する。ＰＣＲ
反応の条件は基本的にキム（Kim)およびスミシー（Smit
hies）、Nucleic Acids Res 、１６、８８８７−８８９
３、１９８８に報告されている。ペレット化の後、ＥＳ
細胞を５μｌのＰＢＳに懸濁し、各チューブに５５μｌ
の水を加えて溶解する。各チューブを９５℃で１０分間
加熱することによりＤＮase を失活させる。５５℃で３
０分間プロテインナーゼＫで処理した後、各溶解物３０
μｌをＰＣＲバッファ（各プライマー１．５μｇ、３Ｕ
Ｔaqポリメラーゼ、１０％ＤＭＳＯおよび各０．２ｍ
ＭのｄＮＴＰ）を含む２０μｌの反応混合物を含むチュ
ーブに移す。ＰＣＲ増幅は９２℃、６５秒のメルティン
グ、６５℃１０分間のアニーリングおよび伸長の条件下
サーモサイクラーを用いて５５サイクル行う。２つのプ
ライマーオリゴヌクレオチド；TGGCGGACCGCTATCCCCCAGG
AC およびTAGCCTGGGTCCCTCCTTACを用いる。これらは各
々ネオマイシン遺伝子の開始コドンの３´側６５０塩基
の領域および挿入部位の３´側１１００塩基のところに
あるマウス重鎖遺伝子に存在する配列に対応している。
２０μｌの反応混合物をアガロースゲルで電気泳動しナ
イロンメンブレン（ゼータバインド）に移す。このメン
ブレンはＪ−Ｃ領域の３２Ｐラベルした９９１ bp×ba
Ｉフラグメントで探る。
【００３３】［実施例２］ＥＳ細胞中のマウスIg重鎖Ｊ
遺伝子の不活性化 （１）不活性化ベクターの構築 Ｂalｂ／ｃマウス胚ゲノムライブラリーからクローン化
しｐＵＣ１８（ｐＪＨ）に挿入した、マウス免疫グロブ
リン重鎖Ｊ領域遺伝子および隣接配列を含む６．１kb
ＥcoＲＩフラグメントをＸhoＩおよびＮaeＩで消化し４
個のＪ遺伝子を含む約２．３kbのフラグメントを欠失さ
せた（図２（Ａ）参照）。ＢamＨＩ部位を平滑化し、ヘ
ルペスシンプレックスウイルスチミジンキナーゼ遺伝子
（ＨＳＶ−ｔｋ）プロモーターおよびポリオーマエンハ
ンサーを含む約１．１kbｐ×hoＩ−ＢamＨＩフラグメン
トをｐＭＣ１Ｎeoから単離した（トーマス（Thomas) お
よびカペチ（Capecchi）、Cell、５１、５０３−５１
２、１９８７）。このフラグメントをＸhoＩ−ＮaeＩ欠
失化ｐＪＨに挿入し不活性化ベクターを生成した（pmＨ
δＪ、図２（Ｂ）参照）。これはネオマイシンおよび重
鎖遺伝子の転写方向が同じである。このプラスミドをＥ
Ｓ細胞のトランスフェクション前にＮdeＩ消化で線状化
した。相同組換え事象を起こす配列は各々ネオマイシン
遺伝子の５´および３´側に位置する約２．８kbp およ
び約１．１kbp フラグメントである。
【００３４】（２）ＥＳ細胞の培養、エレクトロポレー
ションおよび選択 ＥＳ細胞系列Ｅ１４ＴＧ２ａ（コラー（Koller）および
スミシーズ（Smithies）１９８９、ＰＮＡＳ、ＵＳＡ、
８６、８９３２−８９３５）を報告されている方法でマ
イトマイシンＣ処理胚フィブロブラスト支持細胞層上で
培養した（コラー（Koller）およびスミシーズ（Smithi
es）１９８９、ＰＮＡＳ、ＵＳＡ、８６、８９３２−８
９３５）。ＥＳ細胞をトリプシン処理し、２×１０７／
ｍｌの濃度でＨＢＳバッファ（pH７．０５、１３７ｍＭ
NaCl、５ｍＭ KCl 、２ｍＭCaCl２、０．７ｍＭ Na
２ＨＰＯ４、２１ｍＭＨＥＰＥＳ pH７．１）に懸濁し
てから、線状化した不活性化ベクター５０μｇ／ｍｌ存
在上エレクトロポレーションした。エレクトロポレーシ
ョンは２４０Ｖ、５００μＦ容量条件下、バイオラッド
ジーンパルサーを用いて行った。５×１０６個のエレク
トロポレーション細胞を１５％ウシ胎児血清および０．
１ｍＭ２−メルカプトエタノールを補ったダルブコ修正
イーグル培地（ＤＭＥＭ）を含む１００mmプレート内の
マイトマイシンＣ処理フィブロブラスト上にプレーティ
ングした。エレクトロポレーションから２４時間後培地
を２００μｇ／ｍｌ Ｇ４１８を含む培地と置換した。
エレクトロポレーションから１２〜１４日後生じたＧ４
１８耐性ＥＳコロニーをキャピラリーピペットで吸い取
りポリメラーゼチェーンリアクション（ＰＣＲ）を用い
て分析した。各採取コロニーの半分をマイトマイシンＣ
処理した支持細胞を含む２４穴プレートの各ウェルに移
した。４つのプールを合せたもう半分のコロニーは０．
３ｍｌのＰＢＳを含むエッペンドルフチューブに移し、
ジョイナー（Joyner）等（Nature、３３８、１５３−１
５５、１９８９）によって報告された方法でＰＣＲ分析
用に細胞溶解物を調製した。このＰＣＲ反応物には５〜
２０μｌの細胞溶解物、１μＭの各プライマー、１．５
ｕ Tag ポリメラーゼおよび２００μＭ ｄＮＴＰが含
まれている。ＰＣＲ増幅は９４℃１分間のメルティン
グ、５５℃２分間のアニーリングおよび７２℃、３分間
の伸長の条件でサーマルサイクラー（パーキンエルマー
シータス）を用い４５サイクル行った。２つのプライマ
ーオリゴヌクレオチドの配列はACGGTATCGCCGCTCCCGAT
およびAGTCACTGTAAAGACTTCGGGTA であり、これらはネオ
マイシン遺伝子のＢamＨＩ部位の５´側約１２０塩基の
ところにある配列および挿入部位の３´側約１６０塩基
のところに位置するマウス重鎖遺伝子に存在する配列に
対応している。相同組換えが起こると約１．４kbp のフ
ラグメントが生成する。２０μｌの反応混合物を１％ア
ガロースゲルで電気泳動しエチジウムブロマイドで染色
してからナイロンメンブレン（ジーンスクリーン）に移
した。このフィルターを挿入部位の３´側マウス重鎖遺
伝子中に存在する３２Ｐラベルした約１．４kbp のＥco
ＲＩ−ＰstＩフラグメントで探った（図２参照）。さら
に分析するため、ＥＳ細胞からゲノムＤＮＡを調製し、
業者の推薦する方法に従って制限酵素で消化した後その
フラグメントを１％アガロースゲルで分離した。このＤ
ＮＡをナイロンメンブレン（ジーンスクリーン）に移
し、上述の３２Ｐラベル化フラグメントで探った。
【００３５】（３）Ｇ４１８耐性ＥＳコロニーの分析 最初の実験ではプールしたコロニーのＰＣＲ分析で１３
６個のＧ４１８は耐性コロニーを代表する３４個のプー
ルから期待される大きさの（約１．４kbp)の１つのポジ
ティブＰＣＲシグナルが検出された。このポジティブプ
ールに寄与する４個のコロニーを各々ＰＣＲで分析し、
ポジティブクローンＥＳ３３Ｄ５を同定した。第２の実
験で得られた５４０個のＧ４１８耐性コロニーの分析で
さらに４個のポジティブクローンが同定された（ＥＳ４
１−１、ＥＳ６１−１、ＥＳ６５−１、ＥＳ１１０−
１）。
【００３６】目的とするＪ遺伝子の１つのコピーの破壊
を確認するため（この遺伝子は常染色体性で２コピー存
在する）、ＰＣＲポジティブクローンを増幅し、そのゲ
ノムＤＮＡを調製後Ｈind IIIまたはＳcaＩで消化して
ＥcoＲＩ−ＰstＩプローブを用いたサザン分析で解析し
た。
【００３７】相同組換えによるネオマイシン遺伝子の挿
入によりＪ遺伝子の置換が起こり、欠失したＪ遺伝子領
域に存在する２つのＨind III部位の消失により本来の
遺伝子座にある等価なフラグメントよりも約１．９kbp
長いＥcoＲＩ−ＰstＩプローブで検出し得るＨind III
フラグメントが生成する（図２（Ｃ）参照）。Ｈind II
I消化による５個のポジティブクローンのサザン分析は
重鎖Ｊ遺伝子の２つのコピーが破壊されたことを示すパ
ターンを示した。３つのラベル化したフラグメントが検
出された。１つは同じ強度で未処理細胞中に存在するも
のと同じサイズのフラグメント（約７６０bp）で、もう
１つは未処理細胞中に存在するものと同じサイズ（約
２．３kbp ）であるがＰＣＲポジティブクローンの場合
は強度が低いフラグメントであり、また別のフラグメン
トはＰＣＲポジティブクローンのみに存在し相同組換え
によって期待されるサイズ（約４．２kbp)のものであ
る。同様に相同組換えによるＪ遺伝子のネオマイシン遺
伝子による置換で１つのＳacＩ部位の消失および本来の
遺伝子座にある等価なフラグメントよりも約７０bp小さ
いＥcoＲＩ−ＰstＩプローブで検出可能なフラグメント
の出現が起こる（図２（Ｃ）参照）。ＳacＩ消化による
クローンのサザン分析は１つは本来の対立遺伝子および
１つは目的の対立遺伝子の予想されるパターンを示し
た。つまり未処理細胞に検出されるものと同じサイズで
あるが５個のポジティブクローンでは強度が減少してい
る約４．０kbp のフラグメント、および同定されたクロ
ーンのみに存在し目的の相同組換えで期待されるサイズ
の約３．４kbp のフラグメントが出現した。ネオマイシ
ン遺伝子に対するプローブを用いたサザンブロットの再
ハイブリダイゼーションはＨind IIIおよびＳacＩ消化
から生ずる各々４．２kbp および３．４kbp のフラグメ
ントは目的の事象によって期待されるようにそのプロー
ブにハイブリダイズすることを示す。
【００３８】［実施例３］ マウスにおけるマウス免疫
グロブリン重鎖Ｊ遺伝子の不活性化 （１）マウス胚盤胞への目的のＥＳ細胞の注入およびキ
メラ孫の生成 マウスはジャクソンラボラトリーズ（バーハーバー、Ｍ
Ｅ）から購入した。日令３．５才のＣ５７ＢＬ／６胚盤
胞はコラー（Koller）等、１９８９（上述）に報告され
ている方法で週令４〜５才の排卵誘発化したメスから入
手した。ＥＳ細胞をトリプシン処理し、新鮮なＤＭＥＭ
培地で１度洗浄した後Ｍ２培地中約１×１０６／ｍｌと
なるように希釈した。約５μｌの細胞をパラフィン油の
下の胚盤胞を含むＭ２培地１５０μｌの液滴に添加し
た。１０〜１５個の細胞を各胚盤胞の胞胚腔に注入し
た。６〜９個のＥＳ細胞含有胚盤胞を２．５日前に精管
切除したオスと交配し擬似妊娠したＣ５７ＢＬ／６×Ｄ
ＢＡ Ｆ１の各子宮に戻した。注入した胚盤胞由来の子
供は１６〜１８日後に産まれた。子供に対するＥＳ細胞
の寄与は子供の色で判定した。胚盤胞は色が黒いＣ５７
ＢＬ／６マウスから得た。目的の細胞系列が由来する親
系列ＥＳ細胞系列Ｅ１４ＴＧ２ａは１２９／Ｄ／ａマウ
スから単離した。このマウスは３つのカラー遺伝子、ア
ゴーチ遺伝子座の優性ＡＷ対立遺伝子、ｐ遺伝子座の劣
性ピンク眼稀薄対立遺伝子およびＣ遺伝子座の劣性Ｃ
ｃｈ対立遺伝子の組合せ効果でクリーム色である。動物
の形成にＥＳ細胞が関与した子供は褐色とクリーム色を
示している。不活性化したマウス免疫グロブリン重鎖を
有するＥＳ細胞系列ＥＳ４１−１を先に述べたようにＣ
５７ＢＬ／６マウス胚盤胞に注入した。１８の子供のう
ちの６個は高度の色のキメラ性を有していた（７０〜９
０％）。不活性化ＥＳ細胞を注入した胚盤胞を移植した
メス由来のキメラ新生児から単離したＤＮＡのＰＣＲ分
析は変異した免疫グロブリン重鎖遺伝子座が脾臓、胸
腺、腎臓、肝臓、脳および皮膚など種々の器官に存在す
ることを示した。
【００３９】（２）ＥＳ細胞におけるマウスＩｇカッパ
鎖Ｊ遺伝子の不活性化 マウス免疫グロブリンカッパ鎖Ｊ領域遺伝子および３´
隣接配列を含む５．６kbＨind III−ＢamＨＩフラグメ
ントをＢalb ／ｃマウス胚ゲノムライブラリーからクロ
ーン化し、ｐＢlue script ＳＫベクターに挿入してプ
ラスミドｐＫＪを生成した。ｐＫＪをＨind IIIおよび
ＰstＩで消化し５Ｊ遺伝子を含む約１．７kbフラグメン
トを欠失させた（図３参照）。カッパＪ領域に隣接する
Ｈind III部位の５´側領域を含む５７０bp平滑末端Ｈi
nd IIIフラグメントをＰＣＲによりマウスゲノムＤＮＡ
からクローン化した。このフラグメントをＨind III−
ＳmaＩ消化したｐＩｃクローニングベクターに挿入し
（マーシュ（Marsh)等、１９８４、Gene、３２、４８１
−４８５）、ＫpnＩ−ＸhoＩで切断した。ＢamＨＩ部位
を平滑化したヘルペスシンプレックスウイルスチミジン
キナーゼ遺伝子（ＨＳＶ−ｔｋ）プロモーターおよびポ
リオーマエンハンサーで発現されるネオマイシン耐性遺
伝子を含む約１．１kb ＸhoＩ−ＢamＨＩフラグメント
をｐＭＣ１Ｎeoから単離した（トーマス（Thomas) およ
びカペチ（Capecchi）、１９８７、上述）。ネオマイシ
ンフラグメントをＨind III−ＰstＩ欠失化ｐＫＪに挿
入し、カッパ配列の５´側にあるＰstＩ部位を平滑化し
た。このプラスミドをＫpnＩおよびＸhoＩで消化し、そ
の５７０bpＫpnＩ−ＸhoＩカッパフラグメントをＫpnＩ
−ＸhoＩ切断したベクターのネオマイシン遺伝子の５´
側に挿入して不活性化ベクター（pmＫδＪ、図３参照）
を生成した。pmＫδＪにおいてネオマイシンおよびカッ
パ鎖遺伝子の転写方向は同じである。ＥＳ細胞へのトラ
ンスフェクション前にこのプラスミドをＡpaＬＩで線状
化した。この線状化配列は各々ネオマイシン遺伝子の３
´および５´側に存在する細胞性配列と相同的な約３．
８kbおよび５７０bpの配列を有している。
【００４０】（３）Ｇ４１８耐性ＥＳコロニーの分析 カッパ不活性化ベクターのＥＳ細胞へのエレクトロポレ
ーションおよび相同組換えに関するスクリーニングは免
疫グロブリン重鎖の不活性化について述べた方法で行っ
た。Ｇ４１８耐性ＥＳコロニーを２つのプライミングオ
リゴヌクレオチド：CGGTTGCTGTTGTATCCATAACTCおよびCA
TCAGAGCAGCCGATTGTCTGを用いたＰＣＲにより相同組換え
について分析した。これらのオリゴヌクレオチドは挿入
部位の５´側約６７bpのところにあるマウスカッパ鎖遺
伝子に存在する配列およびネオマイシン遺伝子のＸhoＩ
部位の３´側３７０bpのところにある配列に対応してい
る。挿入部位の５´側約１０bpの位置から始まる３２Ｐ
ラベル化した８０塩基のオリゴヌクレオチドをプローブ
として用い目的とするＰＣＲ産物を検出した。相同組換
えにより約１０３０bpフラグメントが生ずる。６５０個
のＧ４１８耐性コロニーのＰＣＲ分析で３個のポジティ
ブコロニー（ＥＳ５６−１、ＥＳ６９−４、ＥＳ１４７
−１）が検出された。これらのコロニーのサザン分析で
Ｊ領域の欠失に継がるカッパ免疫グロブリン遺伝子座へ
の不活性ベクターの組込みが確認された。
【００４１】［実施例４］トランスジェニックマウスに
おけるヒトＩｇの生産 （１）例：トランスジェニックマウスＤＮＡベクターに
おけるヒト重鎖の生産 ヒト重鎖ＶＨ６−Ｄ−Ｊ−Ｃμ−Ｃδ領域を含むＳpeＩ
断片（バーマン（Berman）等、ＥＭＢＯ Ｊ．（１９８
８）７、７２７−７３８、図４参照）をバーマン（Berm
an）等（ＥＭＢＯ Ｊ．（１９８８）７、７２７−７３
８）によって報告されているＤＮＡプローブを用いイー
ストの人工染色体（ＹＡＣ）ベクター（バルケ（Burke)
等、Science 、２３６、８０６−８１２）にクローン化
したヒトライブラリーから単離した。約１００kbと見積
られる１つのクローンが得られた。この単離したＹＡＣ
クローンはヒト重鎖用の放射性ラベルしたプローブ（バ
ーマン（Berman）等、上述）を用いたパルスフィールド
ゲル電気泳動（バルケ（Burke)等、上述、ブラウンスタ
イン（Brownstein) 等、Science 、２４４、１３４８−
１３５１）で確認した。
【００４２】（２）胚へのＹＡＣクローンの導入 目的のＹＡＣを含むイースト細胞からアガロース片に含
まれる高分子量ＤＮＡを調製した（すなわちIgＨ遺伝子
座由来の先に示したＳpeＩフラグメントを含むＹＡ
Ｃ）。このＤＮＡをＣＨＥＦゲル装置でサイズ分別し、
低融点アガロースゲルからＹＡＣバンドを切り出した。
このゲルフラグメントをポリアミンで平衡化し、融解後
アガラーゼで処理してアガロースを消化した。このポリ
アミンコートしたＤＮＡを受精したマウスの胚のオスの
前核に注入し、これを外科的に上述の擬似妊娠したメス
の子宮に導入した。この新生児のトランスジェニック性
を尾から単離したＤＮＡのスロット・ブロットによって
分析し、またヒト重鎖の生産を少量の血清を採取し、ウ
サギの抗ヒト抗体を用いてIg鎖の存在を検定した。
【００４３】マイクロインジェクションの代替法とし
て、ＹＡＣ ＤＮＡはＥＳ細胞：イーストプロトプラス
ト融合によりマウスのＥＳ細胞中に導入する（トレーバ
ー（Traver）等、１９８９ Proc．Natl.Acad.Sci.ＵＳ
Ａ，８６、５８９８−５９０２、パクニス(Pachnis）
等、１９９０、ibid ８７、５１０９−５１１３）。ま
ずｐＭＣ１Ｎeo由来のネオマイシン耐性遺伝子およびイ
ースト選択可能マーカーをプラスミド中の本質的でない
ＹＡＣベクター配列に挿入する。この構築物を用いてＪ
ｇＨ ＹＡＣを含むイースト株をトランスホームし、ま
た、ｐＭＣ１Ｎeoは相同組換えによってIgＨ ＹＡＣの
ベクター配列に組込む。この修正ＹＡＣをプロトプラス
ト融合によってＥＳ細胞に移す（トレーバー(Traver)
等、１９８９、パクニス(Pachnis）等、１９９０）。本
来のヒトIgＨ配列を含むＧ４１８耐性ＥＳ細胞を用いて
キメラマウスを作る。
【００４４】［実施例５］キメラマウスによるヒトＩｇ
の生産 （１）ヒト重鎖置換ベクターの構築 ヒトの置換配列には先に述べたヒトーＹＡＣライブラリ
ーから単離したヒトＶ Ｈ６−Ｄ−Ｊ−Ｃμ−Ｃδ重鎖領
域を含むゲノムＤＮＡのＳpeＩ１００kbp フラグメント
が含まれる。相同組換え置換を起こす隣接するマウス重
鎖配列としては、マウスＣε−Ｃα重鎖の１０kbp Ｂam
ＨＩフラグメントおよびマウス重鎖可変部のＪ５５８フ
ラグメントの５´側半分を含む５´Ｊ５５８がヒト配列
のそれぞれ３´側と５´側に含まれる（図４）。これら
のマウス配列は各々タカー（Tucker)等、ＰＮＡＳ Ｕ
ＳＡ、７８、７６８４−７６８８、１９８１およびブラ
ンケンスタイン(Blankenstein)およびクラウィンケル(K
rawinckel)（１９８７、上述）に報告されているプロー
ブを用いてマウス胚ゲノムライブラリーから単離する。
ヘルペスシンプレックスウイルスチミジンキナーゼ遺伝
子（ＨＳＶ−ｔｋ）プロモーターおよびポリオーマエン
ハンサーで発現されるネオマイシン耐性遺伝子を含む１
１５０bpＸhoＩ−ＢamＨＩフラグメントはｐＭＣ１Ｎeo
から単離する（コラー(Koller)およびスミシーズ(Smith
ies)、１９８９、上述）。合成アダプターをこのフラグ
メントに付加してＸhoＩ末端をＢamＨＩ末端に変換し、
これをプラスミド中のＢamＨＩマウスＣε−Ｃαに連結
する。
【００４５】ヒト重鎖遺伝子座を含むＹＡＣクローンか
ら挿入物の各末端のＤＮＡ配列をインバースＰＣＲ（シ
ルバーマン(Silverman) 等、ＰＮＡＳ、８６、７４８５
−７４８９、１９８９）または大腸菌におけるプラスミ
ドレスキュー（バルケ(Burke）等、１９８７、ガルザ
（Garza)等、Science 、２４６、６４１−６４６、１９
８９；トレーバー(Traver)等１９８９）により回収する
（図４参照）。ＹＡＣの５´Ｖ６末端由来の単離したヒ
ト配列をプラスミド中のマウスＪ５５８配列に連結し、
同様に、ＹＡＣの３´Ｃδ末端由来のヒト配列を上述の
ＮeoおよびマウスＣε−Ｃαを含むプラスミド中のＮeo
遺伝子に連結する。次に、ヒトＶ６−マウスＪ５５８セ
グメントを本来のIgＨ ＹＡＣ中には存在しないイース
ト選択可能マーカー（ＨＩＳ３）、セントロメア（ＣＥ
Ｎ）および単一のテロメア（ＴＥＬ）を含むハーフＹＡ
Ｃクローニングベクターにサブクローン化する。同様に
ヒトＣδ−Ｎeo−マウスＣε−Ｃαを別のイースト選択
可能マーカー（ＬＥＵ２）および単一のＴＥＬを含む別
のハーフＹＡＣベクターにサブクローニングする。ヒト
Ｖ６ＤＮＡを含むハーフＹＡＣベクターを線状化し、こ
れを用いて染色体ＨＩＳ３およびＬＥＵ３遺伝子座を欠
失し、かつIgＨ ＹＡＣを有するイースト株をトランス
ホームする。ヒスチジン栄養要求性による選択でヒトＶ
６ＤＮＡ配列間で相同組換えを起こし組換えＹＡＣを含
むイーストコロニーを検出する。それからヒトＣδＤＮ
Ａを含むハーフＹＡＣベクターを線状化し、これを用い
て前のステップで生成したイースト株をトランスホーム
する。ロイシン栄養要求性による選択で完全なIgＨ置換
ＹＡＣを含むイースト株を得る（図４）。このＹＡＣを
単離し、胚について先に示したマイクロインジェクショ
ン法でＥＳ細胞に導入する。
【００４６】上述の操作に従い、免疫化によりある抗原
に特異的なヒト抗体またはそのアナログを生成し得る抗
原的またはキメラ的非霊長類、特にマウス宿主を作る。
この方法ではヒト宿主に使用できない免疫原でマウスを
免疫化できるので、ヒトモノクローナル抗体を得るとき
に発生する問題が避けられる。さらに、ヒト宿主では許
容されない二次免疫注射やアジュバントを使用し得る。
【００４７】このＢ細胞を目的の抗体を連続的に生産す
るために不朽化する。不朽化した細胞は免疫グロブリン
またはそのアナログをコードし、かつインビトロ突然変
異誘発や他の変異技術を用いて変異させ、その抗体の性
質を改変するのに用いる遺伝子の単離に使用することが
できる。これらの変異遺伝子は相同組換えをするために
不朽化細胞に戻し、哺乳類細胞の連続的な望ましい抗体
原を提供するのに使用される。本発明はヒトの抗体がヒ
ト宿主における抗体生産と同様の方法で生産される場合
簡便なヒト抗体原を提供する。マウス細胞はヒト抗体の
生産に関するマウス細胞中でのヒトＤＮＡの活性化およ
び転位を簡便に提供する。
【００４８】本明細書で引用する全ての刊行物および特
許出願は各刊行物または特許出願が特定して、かつ個々
に参考として引用されていることが示されているのと同
様に参考として引用されている。
【００４９】これまで示してきた発明は明確に理解され
るように図および例を用いて詳細に説明されているが、
本発明の精神または範囲を逸脱することなしに特定の変
化や修正を行い得ることは当業者にとって明白であろ
う。
【００５０】
【発明の効果】以上の通り、本発明は免疫原に応答しヒ
ト抗体またはそのアナログを生成する不活性化した内在
性Ｉｇ遺伝子座及び機能性ヒトＩｇ遺伝子座を有するこ
とを特徴とする。
【図面の簡単な説明】
【図１】 マウス重鎖Ｊ遺伝子及び不活性化ベクターの
各制限酵素地図を示す図である。
【図２】 マウス重鎖Ｊ遺伝子、不活性化ベクター、野
生型ＥＳ細胞ゲノム及び目的のＥＳ細胞ゲノムの各制限
酵素地図を示す図である。
【図３】 マウスカッパ鎖遺伝子並びにカッパ鎖不活性
化ベクターの各制限酵素地図を示す図である。
【図４】 ヒト重鎖遺伝子座、マウス重鎖遺伝子座及び
ヒト重鎖置換ＹＡＣベクターの各制限酵素地図を示す図
である。
───────────────────────────────────────────────────── フロントページの続き (51)Int.Cl.6 識別記号 ＦＩ Ａ６１Ｋ 39/395 Ｃ０７Ｋ 16/00 Ｃ０７Ｋ 16/00 16/46 16/46 Ｃ１２Ｎ 15/00 Ａ (Ｃ１２Ｐ 21/00 Ｃ１２Ｒ 1:91）

Claims (5)

    【特許請求の範囲】
  1. 【請求項１】 不活性化された内在性免疫グロブリン遺
    伝子座を有する細胞の製造方法であって、内在性免疫グ
    ロブリン遺伝子座の一部と相同性を有するＤＮＡ配列と
    該内在性免疫グロブリン遺伝子座との相同組換えにより
    該内在性免疫グロブリン遺伝子座の不変（Ｃ）領域の少
    なくとも一部に障害を導入することを特徴とする製造方
    法。
  2. 【請求項２】 該内在性免疫グロブリン遺伝子座が免疫
    グロブリン重鎖遺伝子座であることを特徴とする請求項
    １に記載の製造方法。
  3. 【請求項３】 該障害が、マーカー遺伝子と該内在性免
    疫グロブリン遺伝子座の不変（Ｃ）領域の少なくとも一
    部との置換によるものであることを特徴とする請求項１
    または請求項２に記載の製造方法。
  4. 【請求項４】 該マーカー遺伝子が、ネオマイシン耐性
    遺伝子であることを特徴とする請求項３に記載の製造方
    法。
  5. 【請求項５】 該細胞が、マウス由来の細胞であること
    を特徴とする請求項１乃至請求項４のいずれかに記載の
    製造方法。
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