JPS6147500A - キメラモノクロ−ナル抗体及びその製造法 - Google Patents

キメラモノクロ−ナル抗体及びその製造法

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Publication number
JPS6147500A
JPS6147500A JP16937084A JP16937084A JPS6147500A JP S6147500 A JPS6147500 A JP S6147500A JP 16937084 A JP16937084 A JP 16937084A JP 16937084 A JP16937084 A JP 16937084A JP S6147500 A JPS6147500 A JP S6147500A
Authority
JP
Japan
Prior art keywords
human
cells
monoclonal antibody
chimeric monoclonal
animal
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.)
Granted
Application number
JP16937084A
Other languages
English (en)
Other versions
JPH0373280B2 (ja
Inventor
Katsu Taniguchi
克 谷口
Yoshikazu Kurosawa
黒沢　良和
Kozo Sugita
杉田　幸三
Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)
Japan Science and Technology Agency
Original Assignee
Research Development Corp of Japan
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Filing date
Publication date
Family has litigation
First worldwide family litigation filed litigation Critical https://patents.darts-ip.com/?family=15885326&utm_source=google_patent&utm_medium=platform_link&utm_campaign=public_patent_search&patent=JPS6147500(A) "Global patent litigation dataset” by Darts-ip is licensed under a Creative Commons Attribution 4.0 International License.
Application filed by Research Development Corp of Japan filed Critical Research Development Corp of Japan
Priority to JP16937084A priority Critical patent/JPS6147500A/ja
Priority to DE1985102665 priority patent/DE171496T1/de
Priority to DE19853587360 priority patent/DE3587360T2/de
Priority to EP85102665A priority patent/EP0171496B1/en
Priority to CA 476731 priority patent/CA1339201C/en
Publication of JPS6147500A publication Critical patent/JPS6147500A/ja
Publication of JPH0373280B2 publication Critical patent/JPH0373280B2/ja
Granted legal-status Critical Current

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Classifications

    • 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
    • C07K16/3053—Skin, nerves, brain
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K38/00—Medicinal preparations containing peptides
    • 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
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K2319/00—Fusion polypeptide

Abstract

(57)【要約】本公報は電子出願前の出願データであるた
め要約のデータは記録されません。

Description

【発明の詳細な説明】 ・本発明はキメラモノクローナル抗体及びその製造法に
関し、特に人体に投与した場合にアナフィラキシ−ショ
ックや血清病などの副作用の少ないモノクローナル抗体
及びその製造法に関する。
単−抗原決定基だけを認識するモノクローナル抗体は免
疫学全体に大きな影響を与え、その有用性は医学界にと
ソまらず生物学、薬学、化学などの多くの分野で証明さ
れている。そして、このモノクローナル抗体を得る方法
に関しては１９７５年に゛６旧ｅｒとＭｉｌｓｔｅｉユ
がヒツジ赤血球で免疫したマウスの牌細胞とマウスミエ
ローマ細胞と全細胞融合させることで実現しく　Ｎａｔ
ｕｒｅ２５６４９５−４９７（１９７５））、この外エ
プスタイン−／ぐ一ル（Ｅｐｓｔｅｉｎ−Ｂａｒｒ）ウ
ィルスにヨル方法ナトカする（特開昭５８−２０１’７
２３号参照）。しかして、これらのモノクローナル抗体
の多くけそれ自体がマウス等人間以外の動物に由来する
ためそれを人間に投与した場合には異種蛋白を注射する
ことになり、その結果、アナフィラキシ−ショックや血
清病などの副作用がおこることが予想される。そのため
、ヒトハイブリドーマを用いてヒトモノクローナル抗体
を作成する試みがなされている。
（例えば特願昭５７−１２６４２４、特願昭５７−５０
２０９０、特願昭５８−９０５１７、特願昭部” ８’、　−、、］、　２８３２３及び特願昭５７−５０
２０９号参照）これらによればヒト型のモノクローナル
抗体を得ることは可能であるが必ずしも再現性等の点に
おいて満足すべきものとは云えない。（Ｎａ−ｔｕｒｅ
３００３　：＋、　６〜３１７（１９８２）参照）また
、マウス等の動物は容易ＶＣ種々の抗原で免疫すること
は可能であるが人間については望む抗原を用いて自由に
免疫できないという欠点がある。
一方、ヒト型モノクローナル抗体を産生ずるヒトＸマウ
スハイブリＶ−マを作製してμ鎖特異的ｍＲＮＡを得た
のち相補鎖ＤＮＡを作製し、プラスミドｐＢＲ３２２に
組み込んで大腸菌にヒトモノクローナル片体全生産させ
る試みを行っているがこの方法も人間には自由に免疫で
きないという点で問題が残る。
本発明者はこれらの欠点全改善すべり枝々の研究全行い
本発明を完成するに至ったのである。すなわち本発明は
ヒト以外の動物由来の可変領域とヒト由来の定常領域か
らなるキメラモノクローナル抗体であって、とれの製造
方法はヒト以外の動１の抗体産生細胞から単離した活性
なりＨとＶＬ遺伝子及びヒトＤＮＡから単離した鮨とＯ
Ｌ遺伝子を発現ベクター例挿入し動物培養細胞に導入し
てキメラモノクローナル抗体を産生させることからなる
。ここで活性な■ゆと■１遺伝子　とは抗体産生細胞に
おいてＤＮＡの再配列によって出来たＶＨにちってはＶ
−ｒ）−Ｊ、ＶＬＫちうてはＶ−Ｊ構造を有する機能的
な遺伝子でちる。しかして１本発明においてヒト以外の
動物としてはマウス、ラット、サル、羊、ウサギ等であ
り、また、抗体産生細胞としては好ましくけハイプリ　
Ｐ　−マ、クローン化Ｂ細胞或はエプスタインパールウ
ィルスによる形質転換Ｂ細胞を用いることが望ましく１
発現ベクターとしてはｐｓ’Ｖ２−ｇｐｔ、ｐＳＶ２−
ｎｅｏ　、　ＳＶ４０が好適でちる。動物培養細胞には
、ヒト、サル、マウス等の動物に由来するリンノミ腫、
腎細胞、Ｌ細胞、　Ｏｏ８細胞、ＨｅＬａ細胞の何れか
を用いることができる゛しかして１本発明に従えばヒト
以外の動物は自由に免疫できるので容易に所望のキメラ
モノクローナル抗体を得ることができると共に１人間に
投与した場合動物由来のモノクローナル抗体に比して異
種蛋白による抗原性が著しく軽減されることが期待され
る。
次に実施例をもって本発明を説明する。
実施例 マウスＶ遺伝子の単離 腫瘍細胞Ｐ３Ｕ１と０５７８Ｌ／６マウスに自然発生し
た黒色腫瘍細胞で免疫し；ｇ　０５７ＢＬ／６マウスに
由来する肺臓細胞との融合細胞でちるハイブリドーマＤ
ＩＯ株（注、正式にはＭ２５９０株でちる。）は黒色腫
瘍細胞と選択的に反応する抗体を分泌し、この抗体のタ
イプはＨ鎖についてはＩｇＭ型で、Ｌ鎖については！に
である。先づＤＩＯ株、　Ｐ３Ｕ１株及び０５７ＢＬ１
５マウス腎臓からＤＮｉ＆’ｉ単離す（Ｃｅｌ１２４３
５３〜３５６（１９８１）参照）次に１０μｍのＤＮＡ
を制限酵素ＨｉｎｄｌＪとＥｃｏＲＪで切断する。制限
酵素のＨＩｎｄｆＭで切断したＤＩＯ株とＰ３Ｕ１株及
び０５７　Ｂ　Ｌ／６マウス腎臓のＤＮＡを電気泳動で
０．９係のアガロースゲルに展開し、ニトロセルロース
膜（８ｃｈｌｅｉｃｈｅｒ　ａｎｄ　５ｃｈｖｅｌｌ　
ｌＪ、　Ｍｏ１．８ｉｏ１．９８５０３〜５１５（１９
７５）参照）に転写し、一方に領域を含んだ２．７　Ｋ
ｂ　Ｈｉｎｄｌｌｊ−Ｈｉｎｄｌｌｌ断片に相当する（
利根用進氏よ＃）得た。Ｎａｔｕｒｅ　２８０２８８〜
２９４（１９７９）参照）　Ｊにプローブ（１０’　ｃ
ｐｍｌｏ、ＩＤＮＡ）を用いたハイブリダゼーションを
行ったシの結果を図ＩＡ（ａ）に示す。
ところで図１＆（ａ）より明らかなようにＤＩＯ株のＤ
ＮＡは６．５　、６．３及び６．Ｉ　Ｋｂの３つの再配
列したバンドが存在する。これらのうち６．３及び６．
ＩＫｂはＰ３ＵＩ　ＤＮＡに見られるものと同様のもの
でちる。
６．５　ＫｂのバンドはＶに−Ｊに構造を含む活性な遺
伝子であり、その特異性の発現に関与する遺伝子でちる
。分子サイズはλフアージのＨｉｎｄｌＩ［マーカーに
よって見積った。このサイズに相当するＤＮＡ断片をア
ガロース電気泳動により単離し、λファージＨｉｎｄｌ
ｌベクターλ７８８　（Ｋ、　Ｍｕｒｒａｙ氏（ニシン
バラ大学）よシ得ｆ（、Ｍｏ１ｅ、　Ｇｅｎ、　Ｇｅｎ
ｅｔ、　１５０５３−６１（１９７７）参照）に挿入し
、λファージにパッケージした。パッケージマウスチャ
ーには大腸菌ＢＴ（８２６８８とＢＨＢ２６９０’に用
いた。（Ｈｏｈｎ。
Ｂ、Ｍｅｔｈ、　Ｅｎｚｙｍｏｌ　６８２９９−３０９
（１９７９）参照）次にＪにプローブをスクリーニング
に用いベントンディビス法（５ｃｉｅｎｃｅ　１９６１
８０−１８２（１９７７）参照）にしたがってブラーク
ツ１イブリダイゼーシヨンを行いクローンＶＪに１４を
単離した。
このクローンの制限酵素地図を表１８（ａ）に示す。
このクローンＶＪに１４のＨｌｎｄ　ｉｌｌ挿入断片を
ノーザンハイプリダイゼーションを行うために単離した
。
Ｄ１０株からグアニジニウムチオシアネート法（Ｂｉｏ
ｃｈｅｍｉｓｔｒｙ　１８５２９４〜５２９９　（１９
７９）参照）により全ＲＮＡを分離し、オリザｄＴセル
ロースカラムの素通シ画分からポリん構造をもつｍＲＮ
Ａを得た。図１ｘ（ｂ）はＤＩＯ株のｍＲＮＡと、クロ
ーンＶＪに１４のＨｌｎｄｌｌ）挿入断片或はＯに領域
を含む３Ｋｂ　Ｈｉｎｄｌｌ−ＢａｍＨＩ断片（利根用
進氏より得た。
Ｎａｔｕｒｅ　　２８０２８８−２９４　（１９７９）
　　参照）に相当スるＣにプローブとのノーザンノーイ
ブリダイゼーションを示している。Ｊ９と０５の両プロ
ーブにより１．２Ｋｂの位置にバンドが見つかった。
クローンＶＪに１４は機能的なＶに−Ｊに構造を含んで
いる。
ノーザンハイプリダイゼーションの方法は免疫実験操作
法ＸＩＩ（１９８３）に記載されている。
また１図１＆（ｃ）は０．９ＫｂのＸｂａｉ　−Ｂｃｏ
Ｒ）断片に相当するＪＨゾローブ（Ｃｅ１ｌ　２４３５
３−３６５（１９８１）参照）とＢｃｏＲｌで切断した
ＤＮＡのサザンハイブリダイゼーションを示す。先に述
べた理由を基にＤ１０株ＤＮ＆にだけ探索される５、５
　ＫｂのＤＮＡ１機能的なＨ鎖のＶ領域遺伝子を含む断
片λフアージＥＣ０ＲＴベクターであるλｇｔＷＥｓ−
λＢ（Ｐ、Ｌｅａｄｅｒ、５ｃｉｅｎｃｅ　１９６１７
５−１７７（１９７７）参照）を用いてクローン化し、
クローンＶＪＨ２４３を得た。クローンＶＪＨ２４３と
ＭＢＰ２０３　（Ｐｒｏｃ、Ｎａｔｌ、　＆ｃａｄ、Ｓ
ｃｆ、　Ｕ　Ｓ　Ａ　７７２１３８−２１４２（１９８
０）参照）の１０ＫｂのＥｃｏ几■断片に相当する０μ
プローブを用いた。
Ｄ１０株のｍＲＮＡとノーザンブロツテングｋ　行ツ＊
結果、　２．４Ｋｂの位置にバンドを見つけた（図１ｋ
（ｄ）参照）。りｏ　　７　ＶＪ　ｃ　１４　（！：　
ＶＪＨ２４３に含まれる活性なＶ遺伝子が特異性の発現
に関与する。
ヒトＯ遺伝子の単離 ヒトの血漿の中で主要な免疫グロブリンクラスでらるＩ
ｇＧの定常領域の遺伝子を単離する。すなわちヒトの免
疫グロブリン遺伝子の塩基配列はマウスのそれと高い相
同性を示しているので、ヒトのゲノムに存在する例えば
ＣにとＣγ１遺伝子をそれに相当するマウスの遺伝子を
プローブとして用いて単離するのであって、その方法は
クローンＩｇ１４６（Ｐｒｏｃ、Ｎａｔｌ＋＋入ｃａｄ
、Ｓｃｉ、ＵＳＡ７５４７０９−４７１３（１９７８）
参照）からの３ＫｂのＨｉｎｄ［［−ＢａｍＨＩ断片と
クローンＭＰ！　Ｐ　１０　（Ｐｒｏｃ、　Ｎａｔｌ。
Ａｃａｄ、Ｓｃｉ、ＵＳＡ、　７８４７４−４７８　（
１９８１）参照）からの６．８ＫｂのＥｃｏＲＪ断片を
プローブとして用いヒトのラムダｃｈａｒｏｎ　４　Ａ
のＨａｅ　ＩＩＩ　−Ａｌ　ｕＩ遺伝子ライブラリー（
Ｔ、　Ｎａｎ１ａｔｉｓ　Ｃｅ１１．１５　１１５７−
１１７４（１９７８）参照）中からヒトＣに遺伝子を含
みエンハンサ−領域を保持している断片を単離する。０
γ１遺伝子はヒト胎子単細胞ＤＮん’１ｚＨｉｎｄｌｉ
で切断しアガロースゲル電気泳動で太きさにしたがって
分画したのち５．９　ＫｂのパンＰをλ７８８に挿入し
前記のプローブを用いてクローン化した。単離したクロ
ーンは図Ｉ　Ｂ（ｃ）のＨＣに２と（ｄ）のＨＧ１６３
である。
工／ハンサーを保持し氷ヒトＣ９遺伝子を含む１．９　
ＫｂのＰｖｕ　ｌ断片を図Ｉ　Ｂ（ｃ）に示すクローン
Ｈ０，２から単離し等量混合した川ｎｄ　ｌ［とＢａｍ
Ｈｌから単離した６、５　Ｋｂ　のＨｉｎｄ　ｌ［挿入
断片と結合し、　ＢａｍＨ１で切断する。得られた断片
を分別しアガロースゲル電気泳動によｊｌ）　５．９　
Ｋｂ　　の断片を単する。この断片ｋ　ｐＳＶ２ｇｐｔ
の１３ａｍＨ１部位に挿入する。挿入した遺伝子の方向
は、制限地図によシ決定する。（図２　ａ　　ｐＳＶ２
−Ｈｏ、ＶＤ、。参照）８．２　Ｋｂ　ＯＨｉ　ｎ　ｄ
　Ｉｌｌ挿入断片’１ｋＨＧ１６３クローンから単離し
、Ｋｌｅｎｏｖ　　酵素によシ両端の一本鎖部分を消化
し、その両端にＥｃｏＲＩ　　！Ｊンカー（全酒造■製
）を接続した。その断片ヲＢｃｏ几工とＢａｍＨＩで切
断しＥＣＯＲＩとＢ’ａｍ　ＨＩで開環したプラスミＰ
ｐ８Ｖ２ｇｐｔに挿入し、ヒトＣγ１遺伝子を含むｐＳ
Ｖ２−）ＩＧ　１４クローンを得る。５．５　ＫｂのＥ
ｃｏ　ＲＩｌ断片りｏ　　ｙ　Ｖ　ＪＨ２４３から単離
しｐＳＶ２−ＨＧＩ　４（７）Ｅｃ　ｏＲＩ切断位置に
挿入する。挿入した遺伝子の方向に制限地図によシ決定
した。（図２　ｂ　　ｐＳＶ２−ＨＧＩＶＤｌ。
参照） ｐＳ　Ｖ　２　ＨＯＡ：ＶＤｌｏ　（！：　ｐＳ　Ｖ２
−ＨＧｔ　ＶＤｌｏ）両Ｄ　Ｎ　Ａ　ヲカルシウム、リ
ン酸共沈降法（ｐｒｏｃ、Ｎａｔｌ、Ａｃａｄ。
Ｓｃｉ、ＵＳＡ７６　１３７３−１３７６（１９７９参
照）によシプラズマサイトーマ（形質細胞腫）Ｐ２Ｏ３
株（Ｈ鎖は合成しないがＬ鎖を生産する性質を持つ）に
導入した。その方法は次のとおシである。
１、　　Ａ溶液をそれと等量の２ｘＨｅＢＳ溶液に滴下
する。
２、室温で３０分間保温する。
３、　　Ｐ３Ｏ１株にトリプシン処理゛し、細胞をばら
ばらにしｆｃ後１０チ牛脂児血清を含むＲＰＭ１１６４
０培地を加えトリプシン処理を終了させる。
４、培養液を１．５００　ｒｐｍ５分間遠心して細胞を
集める。
５、　牛胎児血清を含まない培地に２　Ｘ　Ｉ　Ｏ’個
の細胞を滴下する。
５、　１．５０　Ｏｒｐｍで５分間遠心する。
７　直接、１の液１０―に浮遊する。
８、３７℃で３０分間保温する。
９．５−を別の試験管に移す。
１０．１０チ牛脂児血清を含むＲＰＭ１１６４０の培地
をそれぞれ４５−ずつ加える０ １１．９６穴プレートにそれぞれ０．１−ずつ、イス１
０４清培地で培養する。
１３、ソノ後５μｔ／Ｉ＋７！のきコツエノール酸とザ ２５０μむ−のキサンチンを含むＭＭ１１６４０−１０
％牛脂児血清培地にとシかえ、形質転換した細胞を選択
する。
しかして、Ａ溶液及び２ｘＨｅＢ８溶液は次のような組
成を有する。
Ａ溶液 ２ｘＨｅＢＳ溶液　　　　ｐＨ７，０５ＨＥＰＦｉ８　
　　１０Ｗ／１ ＮａＯＡ　　　　１６ｆ／１ ＫＯｔ　　　　　Ｏ，７４り／１ Ｎａ２ＨＰ０４・Ｈ２Ｏ０，２５ｔ／１ｄｅｘｉｔｒｏ
ｓｅ　　　　２　ｔ／Ｚ選別 キメラモノクローナル抗体産生形質転換細胞の選別には
酵素免疫、蛍光抗体法、或はセルンーター（ＦＡＣ８）
（ペクトン・デンキンソン社）ニよる解析な用いた。ミ
コフェノール酸を含む選択培地により１８の形質転換細
胞クローンが選別された。Ｐ３Ｕ１株とこれら１８の形
質転換細胞はプレート中に十分増殖するまで選択培地で
育てた。
これらの細胞の培養上清を酵素免疫蛍光抗体法（Ｍｅｔ
ｈ、Ｅｎｚｙｍｏｌ、７０４１９−４３９　（１９８０
）参照）に１って抗体の産生状態を試験した。
その結果を表１に示す。
表　　１ ＨＭ）（−８１− ＨＭＨ−８６− ＨＭＨ−８７＋　　　　＋ ＨＭＨ−８８− ＨＭＨ−８１８− ＨＭＨ−８７はＩ　Ｘ　１０７ｆｌｉｉｌの細胞が１０
−の培養上清Ｉｃ　約１０　Ｏｎｆ／ｖｄ！のマウス・
ヒトキメラモノクローナル抗体を産生じている。
抗ヒトＩ　ｇ（）’ｉ用いｆｃＨＭＨ細胞とＰ３Ｕｙ）
セルンーター解析 ＨＭＨ細胞とＰ３Ｕ１株Ｇｄ　Ｉ−Ｔ　ａ　ｎ、ｋ　’
　ｓの平衡塩類溶液（Ｇｉｂｃｏ）で２度洗浄し１０７
個の細胞を７５０μｔの染色緩衝液（１％、　Ｆｅ２−
ＲＰＭＩｏ　、１１６４０　）と２５０μｔのウサギ抗
ヒト免疫グロブリン抗体又は正常ウサギＩｇＧ（１μｒ
／＋７りの混合液に浮遊させ、１時間室温で保温した。
その後細胞を３度洗浄した。その後の手順はベクターラ
ゼラトリ社のアビジンビオチンキット（ａｖｉｄｌｒｉ
ｅ　　ｂｉｏｔｉｎｅＩｃｉｔ）に示されているものと
同様である。要領としては細胞を予めヒト　ＩｇＧで吸
収処理したビオチン結合抗ウサギＩｇＧ（１，５ｍｆ／
ｍ１）２００倍希釈溶液２５０μｔに浮遊し、１時間、
室温で保温した後、Ｈａｎｋ’　ｓ溶液で３度洗浄し、
２５０μｔの２０倍希釈アビジンＦＩＴＣ（５ｍｆ／／
ｖｔ１．）に浮遊させ室温で３０分間保温し、Ｈａｎｋ
’ｓ溶液で３度洗浄する。
最後に１０６個の細胞’Ｔｈ１ｍｇの培養液に浮遊させ
、対数増幅器付きのＦＡＯ８■（ペクトン・ディクソン
社）で解析した。その結果を図３に示す。図３（ａ）　
ｔ　（ｂ）　＃　（Ｃ）は標的細胞としてＨＭＨ細胞を
用いウサギＩｇＧの反応をコントロールとし、それぞれ
（、）はウサギの抗ヒトＩｇ抗体、（ｂ）はウサギの抗
ヒトに抗体、（Ｃ）はウサギの抗ヒトＩｇＧＦｃ抗体と
の反応を表わし、（ｄ）　ｔ　（ｅ）　ｌ　（ｆ）はＨ
ＭＨ細胞とＰ　３Ｕ１細胞に対するそれぞれ（ｄ）はウ
サギの抗ヒトＩｇ抗体、（ｅ）はウサギの抗ヒトに抗体
、（ｆ）はウサギの抗ヒト　ＩｇＧ、Ｆｃ抗体の反応を
表わす。
ＨＭＨ細胞から前述の方法によ、９ＤＮＡとポリ。
入構造金含むＲＮＡを単離する・ＨＭＨ細胞の９Ｎ”と
同様に単離し７’ＣＯ５７ＢＬ／６腎臓細胞とＰ３Ｕ１
細胞のＤ　Ｎ　Ａ　ｆ　ＢａｍＨ’Ｉで切断しＪｚ（マ
ウス）プローブ（表４Ａ−（ａ））、Ｏに（ヒト）プロ
ーブ（表４Ａ　−（ｂ））　、　ＪＨ（マウス）プロー
ブ（衣４　Ａ　−（ｃ）　）及び０γ（ヒト）プローブ
（表４　Ａ　−（ａ）　）　ｗ用いサザンハイプリダイ
ゼーションを行う。
ヒトＣにとマウ刀にプローブはｐＳＶ２−ＨｅにＶＤＩ
。
のＢａｍＨＩ挿入断片のサイズに相当する５、９　Ｋｂ
のバンドｉ　ＨＭ　ＨＩＶｆＩ胞のＤＮＡ中に探索した
。マウスＪＨ７’ロ２ハｐＳＶ２−ＨＧＩＶＤＩＯ（７
）ＶＨ遺伝子を含むＥｃｏ几Ｉ挿入断片に相当する５、
５　Ｋｂのノ々ンドをＨＭ）（細胞のＤＮＡ中に探索し
た。ヒト０γ１　）０−フハｐＳＶ２−ＨＧＩＶＤｔｏ
のＣγ蹟伝子を含むＥｃｏ几Ｉ　−Ｂ　ａ　ｍ　ＨＩ挿
入断片ｉＨＭＨ細胞のＤＮＡ中に探索した。これらによ
υＨＭＨ細胞にはゲノム中に完全なＨ鎖とＬ鎖のキメラ
遺伝子を保持していることが示された。
ＨＭＨ細胞よシ単離したボＩＪ　Ａ構造をもつｍ−ＲＮ
ＡとＰ３Ｕ１よシ単離したポリ入構造をもつｍＲＮＡを
それぞれＶＪに１４ゾローブ、ヒトＯＬゾロープ、ＶＪ
Ｈ２４３プローブ及びヒトＣγ１ゾローブと９間でノー
ザンブロツテングを行った。ＶＪに１４プローブとヒト
０にプローブによシ通常に鎖を生産している細胞にみら
れるのと同じサイズに相当する１、２Ｋｌ）のバンドが
キメ２抗体のＬ鎖のｍ　ＲＮ　Ａとして探索され、Ｉ−
Ｉ　Ｍ　Ｈ細胞のｍ　ＲＮ　Ａ中に最初に転写されたも
ので、またスプライシングされていないためイントロン
がとり除かれていないｍ　ＲＮ　Ａが５ＫｂのパンＰと
して探索される。（図４　Ｂ　（ａ）（ｂ）参照）　Ｖ
ＪＨ２４３として０γ１ゾローブによ、りＨＭＨ細胞の
ｍＲＮＡ中に３．５Ｋｂと７Ｋｂのバンドが探索され、
３．５Ｋｂのバンドは膜結合盤のγＨ鎖のｍＲＮＡのサ
イズに相当し、７Ｋｂのバンドは最初に転写されイント
ロンがとシ除かれていないｍＲＮＡに相当する。
以上によ、ｉ５ＨＭＨ，ＩＢ胞中でマウス由来のＶ−（
Ｄ）−Ｊエクソンとヒト由来Ｏエクソンの間で最初に転
写されｆｒニー　ｍ　ＲＮ　Ａのスプライシングが部分
的に起っていることが証明された。
【図面の簡単な説明】
図１人は活性なマウスＶ遺伝子とヒトの０遺伝子を単離
するためのサザンハイプリダイゼーション及びそれらの
ｍ　ＲＮ　Ａのノーザンブロツテングの解析結果を示す
Ｘ線写真 Ｂは単離しｍクローンの制限酵素地図 図中Ｅｎはエンハンサ−１ＨはＨｉ　ｎ　ｄ　■、プラ
スミド構造 ａ）プラスミドｐＳＶ２−ＨＯＩｃＶＤｌｏの構造ｂ）
プラスミドｐＳＶ２−ＨＧＩＶＤｔｏ（Ｄ構造図３はセ
ルンーター解析図 図４ＡはＨＭＨ細胞のＤＮＡのサザンハイプリダイゼー
ション Ｂ１１１．ＨＭＨ細胞のｍ　ＲＮ　Ａのノーザンブロツ
テング解析結果を示すＸ線写真

Claims (7)

    【特許請求の範囲】
  1. （１）ヒト以外の動物由来の可変領域とヒト由来の定常
    領域からなるキメラモノクローナル抗体
  2. （２）ヒト以外の動物としてマウスである特許請求の範
    囲第１項記載のキメラモノクローナル抗体
  3. （３）ヒト以外の動物としてラットである特許請求の範
    囲第１項記載のキメラモノクローナル抗体
  4. （４）ヒト以外の動物の抗体産生細胞から単離した活性
    なＶ＿ＨとＶ＿Ｌ遺伝子及びヒトＤＮＡから単離したＣ
    ＿ＨとＣ＿Ｌ遺伝子を発現ベクターに挿入し、動物培養
    細胞に導入してキメラモノクローナル抗体を生産するこ
    とを特徴とするヒト以外の動物由来の可変領域とヒト由
    来の定常領域とからなるキメラモノクローナル抗体の製
    造方法
  5. （５）抗体産生細胞としてハイブリドーマ、エプスタイ
    ンバールヴイルスによる形質転換Ｂ細胞またはクローン
    化Ｂ細胞を用いる特許請求の範囲第４項記載のキメラモ
    ノクローナル抗体の製造方法
  6. （６）ベクターとしてｐＳＶ２−ｇｐｔ、ｐＳＶ２−ｎ
    ｅｏ、ＳＶ４０からなる群から選ばれたベクターを使用
    することからなる特許請求の範囲第４項記載のキメラモ
    ノクローナル抗体の製造方法
  7. （７）動物培養細胞がヒト、サル、マウス等の動物に由
    来するリンパ腫、腎細胞、Ｌ細胞、 ＣｏＳ細胞、ＨｅＬａ細胞の何れか一種を使用する特許
    請求の範囲第４項記載のキメラモノクローナル抗体の製
    造方法
JP16937084A 1984-08-15 1984-08-15 キメラモノクロ−ナル抗体及びその製造法 Granted JPS6147500A (ja)

Priority Applications (5)

Application Number Priority Date Filing Date Title
JP16937084A JPS6147500A (ja) 1984-08-15 1984-08-15 キメラモノクロ−ナル抗体及びその製造法
DE1985102665 DE171496T1 (de) 1984-08-15 1985-03-08 Chimaerischer monoklonaler antikoerper und verfahren zu seiner herstellung.
DE19853587360 DE3587360T2 (de) 1984-08-15 1985-03-08 Verfahren zur Herstellung von chimärischen monoklonalen Antikörpern.
EP85102665A EP0171496B1 (en) 1984-08-15 1985-03-08 Process for the production of a chimera monoclonal antibody
CA 476731 CA1339201C (en) 1984-08-15 1985-03-18 Chimera monoclonal antibody and a production process thereof

Applications Claiming Priority (1)

Application Number Priority Date Filing Date Title
JP16937084A JPS6147500A (ja) 1984-08-15 1984-08-15 キメラモノクロ−ナル抗体及びその製造法

Publications (2)

Publication Number Publication Date
JPS6147500A true JPS6147500A (ja) 1986-03-07
JPH0373280B2 JPH0373280B2 (ja) 1991-11-21

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EP (1) EP0171496B1 (ja)
JP (1) JPS6147500A (ja)
CA (1) CA1339201C (ja)
DE (2) DE3587360T2 (ja)

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CA1339201C (en) 1997-08-05
EP0171496B1 (en) 1993-05-26
JPH0373280B2 (ja) 1991-11-21
DE171496T1 (de) 1986-07-03
DE3587360D1 (de) 1993-07-01
EP0171496A2 (en) 1986-02-19
DE3587360T2 (de) 1993-10-14
EP0171496A3 (en) 1987-11-25

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