JPH11262396A - 異種抗体の生成 - Google Patents
異種抗体の生成Info
- Publication number
- JPH11262396A JPH11262396A JP10352241A JP35224198A JPH11262396A JP H11262396 A JPH11262396 A JP H11262396A JP 10352241 A JP10352241 A JP 10352241A JP 35224198 A JP35224198 A JP 35224198A JP H11262396 A JPH11262396 A JP H11262396A
- Authority
- JP
- Japan
- Prior art keywords
- locus
- gene segment
- transgenic non
- region
- human
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Pending
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Classifications
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- A—HUMAN NECESSITIES
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- A01K—ANIMAL HUSBANDRY; CARE OF BIRDS, FISHES, INSECTS; FISHING; REARING OR BREEDING ANIMALS, NOT OTHERWISE PROVIDED FOR; NEW BREEDS OF ANIMALS
- A01K67/00—Rearing or breeding animals, not otherwise provided for; New breeds of animals
- A01K67/027—New breeds of vertebrates
- A01K67/0275—Genetically modified vertebrates, e.g. transgenic
- A01K67/0278—Humanized animals, e.g. knockin
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- 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
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- A—HUMAN NECESSITIES
- A01—AGRICULTURE; FORESTRY; ANIMAL HUSBANDRY; HUNTING; TRAPPING; FISHING
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Abstract
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
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。
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。
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。
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。
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。
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。
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。
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。
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。
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。
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。
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。
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。
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。
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。
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。
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。
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。
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。
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。
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。
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。
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。
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。
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。
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。
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。
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。
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。
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。
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。
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。
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。
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。
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)。
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。
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。
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。
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。
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。
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。
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。
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。
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。
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。
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。
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。
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。
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。
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。
各制限酵素地図を示す図である。
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。
化ベクターの各制限酵素地図を示す図である。
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。
Claims (55)
- 【請求項1】 内在性免疫グロブリン遺伝子座を不活性
化するためのDNAであって、該DNAは、該内在性免
疫グロブリン遺伝子座の一部と相同性を有するDNA配
列を含み、該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
子座の少なくとも一部に障害を導入することにより、不
活性化するものであることを特徴とするDNA。 - 【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DNA。 - 【請求項3】 該障害が、該内在性免疫グロブリン重鎖
遺伝子座の多様性(D)領域の少なくとも一部における
障害であることを特徴とする請求項2に記載のDNA。 - 【請求項4】 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乃至請求項3のい
ずれかに記載のDNA。 - 【請求項5】 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4に記載のDN
A。 - 【請求項6】 該内在性免疫グロブリン遺伝子座が、マ
ウスの内在性免疫グロブリン遺伝子座であることを特徴
とする請求項1乃至請求項5のいずれかに記載のDN
A。 - 【請求項7】 ヒト免疫グロブリン遺伝子座の少なくと
も一部を含むDNA配列及び非霊長類哺乳動物細胞の選
択を可能にするマーカー遺伝子を含むことを特徴するイ
ースト人工染色体(YAC)DNA。 - 【請求項8】 該DNA配列が、ヒト免疫グロブリン遺
伝子座の少なくとも1つの可変部(V)遺伝子セグメン
ト、少なくとも1つの連結(J)領域遺伝子セグメント
及び少なくとも1つの不変(C)領域遺伝子セグメント
を含み、該可変部(V)遺伝子セグメント、該連結
(J)領域遺伝子セグメント及び該不変(C)領域遺伝
子セグメントが機能的ポリペプチドをコードするように
再配列されることができるものであることを特徴とする
請求項7に記載のDNA。 - 【請求項9】 該DNA配列が、さらにヒト免疫グロブ
リン遺伝子座の少なくとも1つの多様性(D)領域遺伝
子セグメントを含み、該可変部(V)遺伝子セグメン
ト、多様性(D)領域遺伝子セグメント、該連結(J)
領域遺伝子セグメント及び該不変(C)領域遺伝子セグ
メントが機能的ポリペプチドをコードするように再配列
されることができるものであることを特徴とする請求項
8に記載のDNA。 - 【請求項10】 該ヒト免疫グロブリン遺伝子座が、ヒ
ト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7乃至請求項9のいずれかに記載のDNA。 - 【請求項11】 該DNA配列が、V−J−Cの順序で
あることを特徴とする請求項8に記載のDNA。 - 【請求項12】 該DNA配列が、V−D−J−Cの順
序であることを特徴とする請求項9に記載のDNA。 - 【請求項13】 該不変(C)領域遺伝子セグメント
が、Cμ不変領域遺伝子セグメントであることを特徴と
する請求項12に記載のDNA。 - 【請求項14】 内在性免疫グロブリン遺伝子座を不活
性化する方法であって、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
ブリン遺伝子座の少なくとも一部に障害を導入すること
を特徴とする方法。 - 【請求項15】 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14記載の方法。 - 【請求項16】 該障害が、該内在性免疫グロブリン重
鎖遺伝子座の多様性(D)領域の少なくとも一部におけ
る障害であることを特徴とする請求項15に記載の方
法。 - 【請求項17】 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14乃至請求項1
6のいずれかに記載の方法。 - 【請求項18】 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17に記載の方
法。 - 【請求項19】 該内在性免疫グロブリン遺伝子座が、
マウスの内在性免疫グロブリン遺伝子座であることを特
徴とする請求項14乃至請求項18のいずれかに記載の
方法。 - 【請求項20】 ヒト免疫グロブリン遺伝子座の少なく
とも一部を含むDNA配列を非霊長類哺乳動物細胞のゲ
ノムに導入する方法であって、該DNA配列が、該DN
A配列及び非霊長類哺乳動物細胞の選択を可能にするマ
ーカー遺伝子を含むイースト人工染色体(YAC)ベク
ターを用いることにより導入されることを特徴とする方
法。 - 【請求項21】 該DNA配列が、ヒト免疫グロブリン
遺伝子座の少なくとも1つの可変部(V)遺伝子セグメ
ント、少なくとも1つの連結(J)領域遺伝子セグメン
ト及び少なくとも1つの不変(C)領域遺伝子セグメン
トを含み、該可変部(V)遺伝子セグメント、該連結
(J)領域遺伝子セグメント及び該不変(C)領域遺伝
子セグメントが機能的ポリペプチドをコードするように
再配列されることができるものであることを特徴とする
請求項20に記載の方法。 - 【請求項22】 該DNA配列が、さらにヒト免疫グロ
ブリン遺伝子座の少なくとも1つの多様性(D)領域遺
伝子セグメントを含み、該可変部(V)遺伝子セグメン
ト、多様性(D)領域遺伝子セグメント、該連結(J)
領域遺伝子セグメント及び該不変(C)領域遺伝子セグ
メントが機能的ポリペプチドをコードするように再配列
されることができるものであることを特徴とする請求項
21に記載の方法。 - 【請求項23】 該ヒト免疫グロブリン遺伝子座が、ヒ
ト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20乃至請求項22のいずれかに記載の方法。 - 【請求項24】 該DNA配列が、V−J−Cの順序で
あることを特徴とする請求項21に記載の方法。 - 【請求項25】 該DNA配列が、V−D−J−Cの順
序であることを特徴とする請求項22に記載の方法。 - 【請求項26】 該不変(C)領域遺伝子セグメント
が、Cμ不変領域遺伝子セグメントであることを特徴と
する請求項25に記載の方法。 - 【請求項27】 内在性免疫グロブリン遺伝子座の少な
くとも1つのコピーに障害を有するトランスジェニック
非霊長類哺乳動物であって、該障害の結果、該遺伝子座
のコピーが不活性化されていることを特徴とするトラン
スジェニック非霊長類哺乳動物。 - 【請求項28】 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27に記載のトランスジェニック非霊長類哺乳動
物。 - 【請求項29】 該障害が、該内在性免疫グロブリン重
鎖遺伝子座の多様性(D)領域における障害であること
を特徴とする請求項28に記載のトランスジェニック非
霊長類哺乳動物。 - 【請求項30】 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27乃至請求項2
9のいずれかに記載のトランスジェニック非霊長類哺乳
動物。 - 【請求項31】 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30に記載のト
ランスジェニック非霊長類哺乳動物。 - 【請求項32】 該非霊長類哺乳動物が、マウスである
ことを特徴とする請求項27乃至請求項31のいずれか
に記載のトランスジェニック非霊長類哺乳動物。 - 【請求項33】 該トランスジェニック非霊長類哺乳動
物が、さらに外来性免疫グロブリン遺伝子座の少なくと
も一部を含むDNA配列を有することを特徴とする請求
項27乃至請求項31のいずれかに記載のトランスジェ
ニック非霊長類哺乳動物。 - 【請求項34】 該外来性免疫グロブリン遺伝子座が、
外来性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33に記載のトランスジェニック非霊長類哺
乳動物。 - 【請求項35】 該非霊長類哺乳動物が、マウスである
ことを特徴とする請求項33または請求項34に記載の
トランスジェニック非霊長類哺乳動物。 - 【請求項36】 該外来性免疫グロブリン遺伝子座が、
ヒト免疫グロブリン遺伝子座であることを特徴とする請
求項33乃至請求項35のいずれかに記載のトランスジ
ェニック非霊長類哺乳動物。 - 【請求項37】 該DNA配列が、該外来性免疫グロブ
リンの不変(C)領域以外のペプチドにペプチド結合で
結合した可変部(V)を提供するDNA配列を含むもの
であることを特徴とする請求項33乃至請求項36のい
ずれかに記載のトランスジェニック非霊長類哺乳動物。 - 【請求項38】 ヒト免疫グロブリン遺伝子座の少なく
とも一部を含むDNA配列がゲノム中に導入されている
トランスジェニック非霊長類哺乳動物であって、該DN
A配列が、ヒト免疫グロブリン遺伝子座の少なくとも1
つの可変部(V)遺伝子セグメント、少なくとも1つの
連結(J)領域遺伝子セグメント及び少なくとも1つの
不変(C)領域遺伝子セグメントを含み、該可変部
(V)遺伝子セグメント、該連結(J)領域遺伝子セグ
メント及び該不変(C)領域遺伝子セグメントが機能的
ポリペプチドをコードするように再配列されることがで
きるものであることを特徴とするトランスジェニック非
霊長類哺乳動物。 - 【請求項39】 該DNA配列が、さらにヒト免疫グロ
ブリン遺伝子座の少なくとも1つの多様性(D)領域遺
伝子セグメントを含み、該可変部(V)遺伝子セグメン
ト、多様性(D)領域遺伝子セグメント、該連結(J)
領域遺伝子セグメント及び該不変(C)領域遺伝子セグ
メントが機能的ポリペプチドをコードするように再配列
されることができるものであることを特徴とする請求項
38に記載のトランスジェニック非霊長類哺乳動物。 - 【請求項40】 該ヒト免疫グロブリン遺伝子座が、ヒ
ト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38または請求項39に記載のトランスジェニッ
ク非霊長類哺乳動物。 - 【請求項41】 該DNA配列が、V−J−Cの順序で
あることを特徴とする請求項38に記載のトランスジェ
ニック非霊長類哺乳動物。 - 【請求項42】 該DNA配列が、V−D−J−Cの順
序であることを特徴とする請求項39に記載のトランス
ジェニック非霊長類哺乳動物。 - 【請求項43】 該少なくとも1つの不変(C)領域遺
伝子セグメントが、Cμ不変領域遺伝子セグメントであ
ることを特徴とする請求項42に記載のトランスジェニ
ック非霊長類哺乳動物。 - 【請求項44】 該トランスジェニック非霊長類哺乳動
物が、さらに内在性免疫グロブリン遺伝子座の少なくと
も1つのコピーに障害を有し、該障害の結果、該遺伝子
座のコピーが不活性化されていることを特徴とする請求
項38乃至請求項43のいずれかに記載のトランスジェ
ニック非霊長類哺乳動物。 - 【請求項45】 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44に記載のトランスジェニック非霊長類哺乳動
物。 - 【請求項46】 該障害が、該内在性免疫グロブリン重
鎖遺伝子座の多様性(D)領域の少なくとも一部におけ
る障害であることを特徴とする請求項45に記載のトラ
ンスジェニック非霊長類哺乳動物。 - 【請求項47】 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44乃至請求項4
6のいずれかに記載のトランスジェニック非霊長類哺乳
動物。 - 【請求項48】 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47に記載のト
ランスジェニック非霊長類哺乳動物。 - 【請求項49】 該非霊長類哺乳動物が、マウスである
ことを特徴とする請求項38乃至請求項48のいずれか
に記載のトランスジェニック非霊長類哺乳動物。 - 【請求項50】 特定の抗原に免疫反応性を有する異種
タンパクの製造方法であって、下記のいずれかの工程を
少なくとも含むことを特徴とする製造方法。 1)特定の抗原に対する免疫応答を刺激する条件下で請
求項33乃至請求項49のいずれかに記載のトランスジ
ェニック非霊長類哺乳動物を該抗原で免疫し、該トラン
スジェニック非霊長類哺乳動物の血中から該抗原に免疫
反応性を有する異種タンパクを回収する。 2)特定の抗原に対する免疫応答を刺激する条件下で
請求項33乃至請求項49のいずれかに記載のトランス
ジェニック非霊長類哺乳動物を該抗原で免疫し、 該トランスジェニック非霊長類哺乳動物からB細胞を
回収し、 該B細胞を不朽化し、 異種タンパクを産生する不朽化B細胞を取得し、 該不朽化B細胞の培養物から該異種タンパクを回収す
る。 - 【請求項51】 該異種タンパクが、ヒトタンパクであ
ることを特徴とする請求項50に記載の製造方法。 - 【請求項52】 該ヒトタンパクが、ヒト抗体またはヒ
ト抗体サブユニットであることを特徴とする請求項51
に記載の製造方法。 - 【請求項53】 請求項33乃至請求項49のいずれか
に記載のトランスジェニック非霊長類哺乳動物のB細胞
に由来する不朽化B細胞であって、該不朽化B細胞が特
定の抗原に免疫反応性を有する異種タンパクを産生する
ものであることを特徴とする不朽化B細胞。 - 【請求項54】 該異種タンパクが、ヒトタンパクであ
ることを特徴とする請求項53に記載の不朽化B細胞。 - 【請求項55】 該ヒトタンパクが、ヒト抗体またはヒ
ト抗体サブユニットであることを特徴とする請求項54
に記載の不朽化B細胞。
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US46600890A | 1990-01-12 | 1990-01-12 | |
US466008 | 1990-01-12 | ||
US61051590A | 1990-11-08 | 1990-11-08 | |
US610515 | 1990-11-08 |
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JP9147805A Division JP3068507B2 (ja) | 1990-01-12 | 1997-06-05 | 異種抗体の生成 |
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JPH11262396A true JPH11262396A (ja) | 1999-09-28 |
Family
ID=27041502
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JP03503394A Expired - Lifetime JP3068180B2 (ja) | 1990-01-12 | 1991-01-11 | 異種抗体の生成 |
JP9147795A Expired - Lifetime JP3068506B2 (ja) | 1990-01-12 | 1997-06-05 | 異種抗体の生成 |
JP9147805A Expired - Lifetime JP3068507B2 (ja) | 1990-01-12 | 1997-06-05 | 異種抗体の生成 |
JP10352243A Withdrawn JPH11243973A (ja) | 1990-01-12 | 1998-12-11 | 異種抗体の生成 |
JP10352238A Withdrawn JPH11262386A (ja) | 1990-01-12 | 1998-12-11 | 異種抗体の生成 |
JP10352240A Pending JPH11239490A (ja) | 1990-01-12 | 1998-12-11 | 異種抗体の生成 |
JP10352241A Pending JPH11262396A (ja) | 1990-01-12 | 1998-12-11 | 異種抗体の生成 |
JP10352242A Pending JPH11239491A (ja) | 1990-01-12 | 1998-12-11 | 異種抗体の生成 |
JP10352239A Pending JPH11262388A (ja) | 1990-01-12 | 1998-12-11 | 異種抗体の生成 |
JP2006035101A Withdrawn JP2006204301A (ja) | 1990-01-12 | 2006-02-13 | 異種抗体の生成 |
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Application Number | Title | Priority Date | Filing Date |
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JP03503394A Expired - Lifetime JP3068180B2 (ja) | 1990-01-12 | 1991-01-11 | 異種抗体の生成 |
JP9147795A Expired - Lifetime JP3068506B2 (ja) | 1990-01-12 | 1997-06-05 | 異種抗体の生成 |
JP9147805A Expired - Lifetime JP3068507B2 (ja) | 1990-01-12 | 1997-06-05 | 異種抗体の生成 |
JP10352243A Withdrawn JPH11243973A (ja) | 1990-01-12 | 1998-12-11 | 異種抗体の生成 |
JP10352238A Withdrawn JPH11262386A (ja) | 1990-01-12 | 1998-12-11 | 異種抗体の生成 |
JP10352240A Pending JPH11239490A (ja) | 1990-01-12 | 1998-12-11 | 異種抗体の生成 |
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JP10352242A Pending JPH11239491A (ja) | 1990-01-12 | 1998-12-11 | 異種抗体の生成 |
JP10352239A Pending JPH11262388A (ja) | 1990-01-12 | 1998-12-11 | 異種抗体の生成 |
JP2006035101A Withdrawn JP2006204301A (ja) | 1990-01-12 | 2006-02-13 | 異種抗体の生成 |
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US (3) | US5939598A (ja) |
EP (4) | EP0463151B1 (ja) |
JP (10) | JP3068180B2 (ja) |
KR (1) | KR100203511B1 (ja) |
AT (2) | ATE356869T1 (ja) |
AU (1) | AU633698B2 (ja) |
CA (1) | CA2050918A1 (ja) |
DE (2) | DE69120146T2 (ja) |
DK (2) | DK0710719T3 (ja) |
ES (2) | ES2284161T3 (ja) |
GR (1) | GR3020240T3 (ja) |
HK (2) | HK1007330A1 (ja) |
NO (2) | NO913558L (ja) |
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1991
- 1991-01-11 DE DE69120146T patent/DE69120146T2/de not_active Expired - Lifetime
- 1991-01-11 ES ES95115451T patent/ES2284161T3/es not_active Expired - Lifetime
- 1991-01-11 WO PCT/US1991/000245 patent/WO1991010741A1/en active IP Right Grant
- 1991-01-11 EP EP91903098A patent/EP0463151B1/en not_active Expired - Lifetime
- 1991-01-11 SG SG9601352A patent/SG48759A1/en unknown
- 1991-01-11 CA CA002050918A patent/CA2050918A1/en not_active Abandoned
- 1991-01-11 EP EP95115451A patent/EP0710719B1/en not_active Expired - Lifetime
- 1991-01-11 AT AT95115451T patent/ATE356869T1/de not_active IP Right Cessation
- 1991-01-11 DE DE69133566T patent/DE69133566T2/de not_active Expired - Lifetime
- 1991-01-11 DK DK95115451T patent/DK0710719T3/da active
- 1991-01-11 EP EP06006801A patent/EP1690934A3/en not_active Withdrawn
- 1991-01-11 EP EP06006802A patent/EP1690935A3/en not_active Withdrawn
- 1991-01-11 DK DK91903098.1T patent/DK0463151T3/da active
- 1991-01-11 ES ES91903098T patent/ES2087997T3/es not_active Expired - Lifetime
- 1991-01-11 JP JP03503394A patent/JP3068180B2/ja not_active Expired - Lifetime
- 1991-01-11 AU AU71814/91A patent/AU633698B2/en not_active Expired
- 1991-01-11 AT AT91903098T patent/ATE139258T1/de not_active IP Right Cessation
- 1991-09-10 NO NO91913558A patent/NO913558L/no not_active Application Discontinuation
- 1991-09-11 KR KR1019910701093A patent/KR100203511B1/ko not_active IP Right Cessation
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1992
- 1992-07-30 US US07/922,649 patent/US5939598A/en not_active Expired - Lifetime
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1995
- 1995-06-05 US US08/464,582 patent/US6114598A/en not_active Expired - Lifetime
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1996
- 1996-06-17 GR GR960401184T patent/GR3020240T3/el unknown
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1997
- 1997-06-05 JP JP9147795A patent/JP3068506B2/ja not_active Expired - Lifetime
- 1997-06-05 JP JP9147805A patent/JP3068507B2/ja not_active Expired - Lifetime
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1998
- 1998-06-24 HK HK98106528A patent/HK1007330A1/xx not_active IP Right Cessation
- 1998-09-21 HK HK98110786A patent/HK1009979A1/xx not_active IP Right Cessation
- 1998-12-11 JP JP10352243A patent/JPH11243973A/ja not_active Withdrawn
- 1998-12-11 JP JP10352238A patent/JPH11262386A/ja not_active Withdrawn
- 1998-12-11 JP JP10352240A patent/JPH11239490A/ja active Pending
- 1998-12-11 JP JP10352241A patent/JPH11262396A/ja active Pending
- 1998-12-11 JP JP10352242A patent/JPH11239491A/ja active Pending
- 1998-12-11 JP JP10352239A patent/JPH11262388A/ja active Pending
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2001
- 2001-10-31 NO NO20015332A patent/NO20015332D0/no unknown
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2004
- 2004-08-13 US US10/917,703 patent/US20050076395A1/en not_active Abandoned
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2006
- 2006-02-13 JP JP2006035101A patent/JP2006204301A/ja not_active Withdrawn
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