JP2007231027A - 癌マーカー用生物合成結合蛋白質 - Google Patents
癌マーカー用生物合成結合蛋白質 Download PDFInfo
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Abstract
【解決手段】c−erbB−2またはc−erbB−2関連腫瘍抗原に結合する免疫グロブリンの免疫学結合特性を示す結合部位を特定する一本鎖Fv(sFv)ポリペプチドを開示する。sFvは、1つのドメインのC末端と他のドメインのN末端の間の距離をつなぐポリペプチドリンカーによって結合されている少なくとも2つのポリペプチドドメインを含む。ポリペプチドドメインのそれぞれのアミノ酸配列はフレームワーク領域の間の挿入された一組の相補的決定領域(CDRs)を含み、そのCDRsはc−erbB−2またはc−erbB−2関連腫瘍抗原に免疫学結合に関与する。
【選択図】なし
Description
(発明の分野)
本発明は、一般的には、新規な生物合成組成物に関し、特に生物合成抗体結合部位(BABS)の蛋白質とそれらの融合体に関する。本発明の組成物は、例えば薬剤や毒物を用いた種々の癌の免疫学的治療やターゲッティング、イメージングに有用であり、さらに特異的なバインディングアッセイ、アフィニティーによる精製法および生体触媒として有用である。
乳癌は、北米では女性の最も多い悪性疾患であり、1987年には130,000人の新患者が発生している。おおよそ女性は11人に1人の割合での一生の間に、乳癌が発生し、米国の女性にとっては、肺癌に次いで第2位の癌による死亡の原因となっている。乳癌女性の大多数は完全に切除可能疾患であったにもかかわらず、転移病巣が残存しており、完治させるためには障害となる。補助化学療法やホルモン療法は、病巣のない場合の延命と、完全切除の乳癌女性の特定の群の全体的な延命に対して明らかな有効性を示が、一般的な女性の場合は、未だに転移病巣によって悪い状態のままである(Fisher他,1986、J.Clin.Oncol.,4:929−941;”The Scottish trial”,Lancet,1987,2:171−175)。適切に選定された患者に対する化学療法やホルモン療法によって、正しく誘導性の目的とする応答が起こったとしても、転移性乳癌の完治は達成されない(Aisner他,1987、J.Clin.Oncol.,5:1523−1533)。この目的のために、新しい薬剤の使用、薬剤の併用、高容量療法(Henderson他 同上)や投与量増強療法(Kernan他、1988、Clin.Invest.259 :3154−3157)を含む革新的な治療計画が多用されている。改善は認められてはいるが、完治への最初のステップである転移病巣の完全な寛解の一般的な達成は未だ得られていない。治療のための新しいアプローチが求められている。
28:915)。
本発明は、一本鎖Fv(sFv)ポリペプチドとして公知であった蛋白質のクラスの新規合成物を特徴としている。このポリペプチドは、生物合成一本鎖ポリペプチドの結合部位(BABS)を含み、c−erbB−2あるいはc−erbB−2関連腫瘍抗原に結合する免疫グロブリン分子の免疫学的結合特性を示す結合部位を特定している。
は、上記c−erbB−2関連腫瘍抗原を有する細胞のイメージングを可能にするために遠隔的に検出可能な成分が結合している。
(a)上記DNAを宿主細胞にトランスフェクトして形質転換体を生産し、(b)上記形質転換体を培養して上記一本鎖ポリペプチドを生産する。
(a)上記ポリペプチドからなるイメージング剤を準備し、(b)イメージング剤が腫瘍に結合した後に上記腫瘍の体外検出を充分に可能にする量の上記イメージング剤を生理学的に受容可能なキャリアーとともに上記腫瘍をもつ哺乳動物に投与する、(c)上記対象における遠隔的に検出可能な成分の位置を検出して上記腫瘍の像を得る。
ながっている。本発明のsFvは、(VHn−リンカー−VLn)nで表すことのできる複数の結合部位を含むことができる(ここでnはn>1)。さらに、このドメインはn個の抗原結合部位とn×2個のポリペプチドドメインを有する連続したアミノ酸の一本鎖とすることもできる。
発現sFv融合蛋白質は結合性部位のポリペプチドにペプチド結合している補助的なポリペプチドを含んでいる。好ましい実例として、補助的ポリペプチドセグメントは、さらにまたc−erbB−2あるいは関連抗原に結合親和性を有しており、三番目あるいはさらに四番目のポリペプチドドメインを含んでいてもよい。これらのポリペプチドドメインはFRsの間に挿入されたCDRsを特定するアミノ酸配列から構成されており、そして上記の第一のポリペプチドに対すると同様な第二の一本鎖ポリペプチドの生物合成結合部位を一緒に形成する。
るその他の毒素蛋白質あるいはペプチド配列との融合によってターゲッティングへの応用が容易になる。さらに、本発明の幾つかのsFv誘導体または融合蛋白質は、細胞の表面にc−erbB−2あるいはその関連抗原と共通に結合した場合、腫瘍細胞の表面に発現したc−erbB−2あるいはその関連抗原の内在化を促進する作用を持つ。この方法は、適切なデザインの一本鎖−Fv−毒素の融合体を用いてこのような抗原の発現した細胞の選択的な死滅を可能にする。本発明のsFv −毒素融合蛋白質は、抗体全体あるいはFabと化学的に交差結合させた毒素を含む共有結合体と比べて15−200倍以上も高い殺腫瘍細胞活性を有している。
乳癌および卵巣癌細胞、さらには癌の形態が明らかに類似している腫瘍細胞に高いレベルで発現している、c−erbB−2関連抗原への親和性を有する一本鎖のFvとsFvの融合蛋白質が本発明で開示される。このポリペプチドは、生物合成した抗体結合部位として挙動する領域を構成する一つまたはそれ以上のアミノ酸配列によって特徴付けられる。図1に示したように、この部位は重鎖の可変領域(VH)10、軽鎖の可変領域(VL)14の一本鎖からなっている。ここでVH 10とVL 14はポリペプチドリンカー12により結合されている。結合ドメインは、分離した免疫グロブリンから得ることができるFRs32、34、36、38および32’、34’、36’、38’に結合した、c−erbB−2関連腫瘍抗原に結合することのできる免疫グロブリン分子由来のCDRs 2、4、6と2’、4’、6’を含む。図2A、図2B、図2Cに示したようにBABSの一本鎖ポリペプチド(VH 10、VL 14、リンカー12)は遠隔的に検出可能な成分および/またはその他のポリペプチド配列16、18又は22を含むことができ、これは酵素、毒素、結合部位、固定化マトリックスあるいは放射能活性原子に結合する部位などの機能を持っている。本発明は蛋白質の生産方法およびその使用方法を開示する。
−ン化されたオリゴヌクレオチドのライゲ−ションからなるまたはハイブリド−マのゲノム由来のフラグメントのライゲ−ションによる組み換えDNA、成熟B細胞クロ−ンまたは天然材料由来のcDNAライブラリ−、に一部基づいた遺伝子配列を含むプラスミドによってコ−ドされた蛋白質を発現させる宿主細胞中で合成され、再クロ−ン化されるという意味で生物合成される。
酸の少なくとも一部分と同一かまたは類似したアミノ酸配列を含んでいても良い。一方、CDRsを含むアミノ酸配列は、超可変領域由来のアミノ酸配列(そして明らかなフランキングアミノ酸配列)の一部分に類似する。この超可変領域はマウスまたはラット由来のc−erbB−2または関連抗原に対する抗体、あるいは特異的ヒト抗体または免疫グロブリンなどの公知の親和性と特異性を有する抗体のもので良い。
Hnatowich,米国特許第4,479,930)。また先行技術によって公知となっているアイソトープ結合のための標準的な方法であっても良い。
している。抗体はポリペプチドリンカー12ヘカルボキシル末端を介して結合しており、そして抗c−erbB−2モノクローナル抗体の軽鎖可変領域(VL)に類似のアミノ酸配列を有するポリペプチド14にリンカーが結合している。
特許第4,753,894号には、乳癌細胞上のc−erbB−2関連抗原を認識するモノクローナル抗体が開示されており、いかにしてこの抗体を得るか説明されている。この目的に特に有用なモノクローナル抗体は520C9である(Bjon他、1985,Cancer Res. 45 :124−1221;米国特許第4,753,894号)。この抗体は特異的に、種々の腫瘍セルラインの表面に発現しているc−erbB−2抗原を認識する。そして正常組織に結合することは非常にまれである。必要とする特異性を持つsFv配列の別の資源としては、ファージ抗体とコンビネーショナルライブラリーの進歩を利用できる。このような配列は、腫瘍細胞膜、c−erbB−2、c−erbB−2関連抗原フラグメントまたはペプチドによって予備免疫したマウスから得たcDNAに基づいて得られる(Clackson他、Nature 352 624−628(1991))。
配列の変更をもたらしているため可能である。
Hを合成し、次の制限酵素切断部位またがる5つのプライマリーなブロックとしてpUCでクローニングする。(1)EcoRI−第一のNarI、(2)第一のNarI−XbaI (3)XbaI−SalI (4)SalI−NcoI (5)NcoI−BamHI。これらのクローン化フラグメントは単離し、3フラグメントのライゲーション体を複数を集め、pUC8プラスミド中にクローニングする。PAGEで選別した必要なライゲーション体でE.coli JM8を形質転換させ、標準方法に従ってLBアンピシリン+Xgalプレートで培養する。遺伝子配列はサンガーのジデオキシ法(Molecular Cloning,1989,Sambrook et al.,eds.,2d
ed., Vol.2, Cold Spring Harbor Laboratory Press,NY)に従って、M13にクローニングするかサブクローニング後スーパーコイルシーケンシングによって確認する。
また毒素、酵素、サイトカイン、ホルモンなどの少なくとも一部分のような別のポリペプチドをコードする配列もまた含んでいる。遺伝子は既に確立された電気融合法またはプロトプラスト融合法でミエローマ細胞にトランスフェクトする。トランフェクト細胞はVH− リンカー− VLまたはVL − リンカー− VHの一本鎖Fvポリぺプチドを発現する。それぞれのポリペプチドは上記の種々の方法で別の機能を有する蛋白質ドメイン(細胞毒性物など)を結合している。
)をコードしているDNAの境界部位における切断部位が利用され、もしなければ創造される。発現プラスミドに集め、クローン化した遺伝子からさらに、単一の結合部位をコードするDNAをシャトルプラスミドにライゲーションし、クローン化する。目的のドメインは、多様化させ、そしてドメインの間のスペーサーは、ドメインのフォールディングを独立させるために必要なフレキシビリティー付与している。発現レベル、リフォールディング、機能活性に関する最適技術は経験的に決定される。二機能sFvを創造するためには、例えば、最初の結合部位をコードする遺伝子のストップコドンはオープンリーディングフレームに変え、そしてBamHI(Gly−Serをコード)またはXhoI(Gly−Ser−Serをコード)のような制限酵素切断部位になる、いくつかのグリシンにセリンを結合させるコドンは、他のコドン置き換える。第二のsFv遺伝子は、同じリーディングフレームの同じ制限酵素切断部位を確認して、その5’末端側を同様に改変する。遺伝子は、二機能性sFv遺伝子を調製するために、この部位に結合させる。
乳癌に対するモノクローナル抗体は、ヒト乳癌細胞またはマウスに免疫して得た細胞の膜抽出物を用いて、Frankel他の示した方法によって(Frankel et al.,1985, J.Biol.Resp.Modif.,4:273−286) 得た。文献は引用により発明と一体化している。ハイブリドーマを調製し、正常および乳癌細胞のパネルを用いて、抗体生産を選別した。8つの正常組織膜のパネル、線維芽細胞株、および乳癌細胞の凍結切片をスクリーニングに用いた。最初のスクリーニングを通過した候補は、さらに、16の正常組織切片、5つの正常血球タイプ、11の乳癌以外の腫瘍切片、21の乳癌切片、14の乳癌細胞株を用いて試験を行った。このセレクションにより127の抗体が選択された。不適切な抗体および乳癌以外の癌細胞株をコントロール実験に使用した。
ある一連の蛋白質、93KD、60KD、37KD;180KD(トランスフェリンレセプター);42KD;および55KD。抗原の5つのクラスに対して結合した抗体の最大の特異性は、200KDの物質に対するものであった。その抗原のクラスに代表的な抗体は520C9であった。520C9は少数の乳癌組織に反応する(分析条件に依存するが20−70%)。そして極わずかな正常組織に反応する。520C9は腎臓の細管に反応する(多くのモノクロナール抗体がそうであるように)。しかし、膵臓、食道、肺、大腸、胃、脳、扁桃、肝臓、心臓、卵巣、皮膚、骨、子宮、膀胱、正常な乳房組織には試験を行ったが反応しなかった。
ポリアデニレートRNAをInvitrogen(サンディエゴ、カリフォルニア)の”FAST TRACK”mRNAアイソレーションキットを使用して、約1×108個の細胞(520C9ハイブリドーマ)から分離した。免疫グロブリン重鎖RNAの存在は、重鎖の染色体DNAの種々のJ領域を含む組換えプローブを使用して、ノーザン分析で確認した(Molecular Cloning,1989,Sambrook et al.,eds.,2ded.,Vol.2, Cold Spring Harbor
Laboratory Press, NY)。それぞれ6μgのRNAを用いて、cDNAをインビトロージェンcDNA合成システムとランダムおよびオリゴdTプライマーの両方を使用して調製した。合成に引き続き、cDNAはアガロースゲル電気泳動で0.5−3.0キロベース(Kb)フラグメントを単離してサイズセレクションを行った。cDNAとベクターの比率の最適化を行ってこのフラグメントをインビトロージェン クローニング ベクターpCDNA IIにライゲーションした。
プラスミドライブラリーDNAを用いて細菌の形質転換後、コロニーハイブリダイゼションを、軽鎖または重鎖遺伝子のどちらかについて、抗体の定常(C)領域と結合(J)領域のプローブを使用して実施した。なおOrland et
al.,1989,Proc.Nat.Aca.Sci.86:3833を参照のこと。抗体定常領域のプローブは、公知の方法で免疫グロブリン遺伝子の重鎖または軽鎖のヌクレオチド配列から得ることができる。いくつかの可能性の高いクローンを重鎖および軽鎖遺伝子ともに特定し、精製後に第二のスクリーニングを行なって、この配列を決定した。一つのクローン(M207)は、保存されたシステインに代えてチロシンを有する非機能性κ鎖の配列を含んでおり、そしてさらに、これは可変J領域のジャンクションにはフレームシフトミューテーシヨンを誘導する4塩基の欠失があるために早期に終了している。第二の軽鎖のクローン(M230)は定常領域の最後の18残基のアミノ酸とシグナル配列の約半分を除いては、完全な520C9軽鎖の遺伝子を実質的含んでいた。520C9の重鎖の可変領域は、CH2 ドメインの末端付近で終了しているところの、約1100塩基対(F320)のクローン上に存在していた。
sFvを構築する目的で、重鎖と軽鎖両方の可変領域に適切な制限酵素切断部位を挿入するため変異させた(Kunkel,T.A.,1985,Proc.Nat.Acad.Sci.USA 82:1373)。重鎖クローン(F320)には、VH(F321)の5’末端にBamHIを挿入して変異を起こした。軽鎖にもまた5’末端にEcoRVと可変部位(M231)の3’末端に翻訳ストップコドンを含むPstIサイトを挿入して同時変異を起こさせた。
軽および重鎖をコードするcDNAクローンは、外来の標準pUCプライマーと複数の特異的内部プライマーを用いてシーケンシングを行なった。
c−erb−2関連腫瘍抗原を認識する一本鎖のFv結合部位を含む合成520C9 sFv領域をコードする核酸配列はCompugenソフトウェアーの手助けによってデザインした。その遺伝子は520C9抗体のVHおよびVL領域をコードする核酸配列を含んでおり、配列表配列番号3および4のアミノ酸残基番号116−133として配列を示したアミノ酸配列を持ったペプチドをコードする2本鎖の合成オリゴヌクレオチドが同時に結合している。このリンカーオリゴヌクレオチドはヘルパークローニングサイトEcoRIとBamHIを含んでいる。そしてそれぞれその5’と3’近傍のアセンブリーサイトSacIとEcoRVを含むようにデザインされている。これらのサイトはそれぞれ520C9のVHおよびVLの5’と3’末端をマッチアップしライゲーションすることを可能にしている。これらはまた、(VH − リンカー− VL)サイトを含んでいる。しかしオリゴヌクレオチドのリンケージの順序は、この例や発明のどのsFvでも(VL −リンカー−VH)のように逆転できることである。その他の制限酵素切断部位は、選択的なアッセンブリーサイトを提供できるようにデザインされている。プロテインAのフラグメントをコードする配列をリーダーとして使用した。
完成させるまで、FRを合成し、PCR−に基づいたリゲーションにより完全なV領域を連続的に調製するためにCDRに融合させる。例えば、マウス520C9抗体CDRsとヒトミエローマ蛋白質NEW FRsのハイブリッドであるヒト化sFvは、ヒトフレームワーク (FR1−CDR−FR2−CDR2−FR3−CDR3−FR4)のマウス結合部位をそれぞれの可変領域が保持するようにデザインされている。Fab NEWの結晶構造は(Saul etal.,1978,J.Biol.Chem.253:585−597)は可変領域のFRsの配置を予測するために使用できる。すでにこれらの領域は予測されており、領域のアミノ酸配列または対応する塩基配列が決定されており、配列は合成されて、シャトルプラスミドにクローン化されている。それらは集合させて、発現プラスミドでもクローン化されている。従って、520C9のsFvのFR配列は直接突然変異させて、変化は内部プライマーを使用してスーパーコイルシーケンシングで確認した(Che et al.,1985,DNA 4:165−170)。
A.インクルージョンボディーの溶解化
T7プロモータとベクターに基づいた520C9 sFvプラスミドの、配列表配列番号3として配列表を示した融合遺伝子をE.coli中で直接発現させた。2.01の培養液から得たインクルージョンボディー(15.8g)を25mM Tris、10mM
EDTA、pH8.0(TE)に1Mグアニジン塩酸塩(GuHCl)加えて洗浄した。インクルーションボディーはTE、6M GuHCl、10mM ジチオスレイトール(DTT)、pH9.0に溶解させ、3825 A280ユニットの物質を回収した。この物質はエタノール沈澱、TE、3M尿素洗浄、次いでTE、8M尿素、10mM DTT、pH8.0に再分散させた。この沈澱操作で、変成sFvのイオン交換の精製のための蛋白質を調製した。
sFvを再生する前に混入している核酸とE.coli蛋白質を除去するために、溶解したインクルージョンボディーをイオン交換クロマトグラフィにより処理した。8M尿素に溶解させたインクルージョンボディーをTEで希釈して、最終尿素濃度を6Mとして、ついでラジアル フロー カラム中のDEAE− セファロース ファースト フロー(100ml)を通過させた。sFvは、非結合画分に回収された(出発サンプルの69%)。
sFvの再生はジスルフィド開裂リフォールディングアプローチで行った。この方法では、sFvが完全に変成しているため、ジスルフィドを酸化して、変成を除去し次いでリフォールディングさせる。sFvサンプルの酸化はTE、6M
GuHCl、1mM 酸化グルタチオン(GSSG)、0.1mM還元グルタチオン(GSH)、pH9.0で行った。sFvは酸化緩衝液で希釈して4000mlの容量で、最終蛋白質濃度がA280=0.075にし、室温で一晩インキュベートした。
濃縮ステップに入る前に凝集したミスフォールディング物を除去する目的で、透析終了リフォールド520C9 sFv(5050ml)をミニタン ウルトラフィルトレーション 装置(ミリポア)を使用して100K MWCO膜(100,000mol.wt.カットオフ)(4 x 60cm2)を通して濾過した。このステップはかなりの長時間(9時間)が必要があったが、これは主として膜処理物中の沈澱形成と処理物中の蛋白質濃度の増加に伴う膜の汚れのためである。リフォールドしたサンプル中の蛋白質の95%は100Kの膜に不溶物の形の75%とともにと不溶解物の状態の79%は100Kの膜に保持された。100Kでの保持物は非常に低い活性であり、廃棄した。100Kの濾過液は、c−erbB−2に結合する活性を有して可溶性sFvの大部分を含んでいた。次にミニタンに取りつけた10KのMWCO膜(10,000 mol.wt.カットオフ)(4×60cm2)を使って100mlの容量(50×)に濃縮した。この物質は、さらに50mlのアミコンスティアードセルのYM10 10K MWCO膜を使用して、最終容量5.2mlまで濃縮した(1000×)。極わずかな沈澱が2回の10K濃縮操作で発生しただけだった。この濃縮物の比活性は、最初の透析リフォールディング物に対して相対的にみて有意に増加していた。
折り畳まれたsFvはサイズ排除クロマトグラフィーによって分画した時に、全ての520C9 sFv活性は、折り畳まれたモノマーの位置に溶出することが確認された。活性なモノマーを多く得るために、1000倍濃縮sFv試料を、0.5M尿素を加えたPBSA(2.7mM KCI,1.1mM KH2PO4,138mM NaCl,8.1mM Na2HPO4・ 7H2O,0.02%NaN3)中で、セファクリルS−200 HRカラム(2.5×40cm)で分画した。カラムからの溶出パターンとフラクションのSDS−PAGE分析は、二つのsFvモノマーのピークを示した。二つのsFvモノマーピークフラクションはプールして(全10ml)、c−erbB−2結合活性を拮抗分析で表示した。
c−erbB−2の細胞外ドメイン(ECD)はバキュラウイルス感染昆虫細胞で発現させた。この蛋白質(ECD c−erbB−2)はアガロースアフィニティーマトリックスに固定化させた。sFvモノマーのピークは尿素を除くためにPBSAに対して透析を行った。そして次いで、PBSAで0.7×4.5cm ECD c−erbB−2−アガロースアフィニティカラムに適用した。カラムはA280がベースラインになるまで洗浄し、PBSA+3M LiCl,pH=6.1で溶出した。ピークのフラクションを集め(4ml)、そしてPBSAに対して透析を行ってLiClを除去した。精製sFv
72μgが750μgのS−200モノマーフラクションから得られた。カラムフラクションでの活性測定は拮抗分析によって行った。簡潔に言えば、sFvアフィニティ精製フラクションとHRP−複合520C9FabフラグンメントはSK−BR−3の膜に対する結合に拮抗することが確認された。sFv調製物の充分な結合は、HRP−520C9Fabフラグメントの膜への結合を抑制した。さらにHRP基質の抑制と減少を行ったが色沢は変化しなかった(拮抗分析の詳細は以下を参照のこと)。その結果は、実際にはsFv活性の全てがカラムに結合し、溶出ピークに回収された(図4)。期待したように、溶出したピークの比活性はカラムのサンプルに対して相対的に増加していた。そしてこれらの測定の実験誤差の範囲内で、コントロールのペアレントFabと、必然的に同じ結
果を示した。
表Iに精製工程中の種々の520C9調製物の回収率を示した。蛋白質濃度(μg/ml)はバイオラッド プロテインアッセイで測定した。”全収量”の下の300AUは、0.41の培養液から3.15gのインクルージョンボディーが含まれている保有sFvを変成させたものである。酸化緩衝液は25mM Tris、10mM EDTA、6MGuHCl、1 mMGSSG、0.1mM
GSH、pH9.0を使用した。酸化は室温で一夜行った。酸化後のサンプルは、10mM リン酸ナトリウム、1mM EDTA、150mM NaCl、500mM尿素、pH 8.0の溶液に対して透析を行った。アフィニティクロマトグラフィーはPBSAで行ったが、それ以外の工程全ての緩衝液はこれを使用した。
リシンA−520C9 一本鎖融合イムノトキシン(配列表配列番号7)をコードする遺伝子は、pPL229(シータース エメリービル カリフォルニア)からHindIII−BamHI上のリシンA鎖をコードする遺伝子を単離し、図3に示したようにpH777の520C9の上流を使用して構築した。融合体はリシンのAドメインとBドメインの間に122アミノ酸の天然のリンカーを有している。しかし、オリジナルなpRAP299発現ベクター中を、リシンのアミノ酸268のコドンが、翻訳停止コドンTAAに変換していたため、得られた遺伝子の発現は、リシンAのみを生産していた。それ故、翻訳停止コドンを除去する目的で、部位直接突然変異を行ってTAAを除去し、天然型のセリンコドンに置き換えた。次いで完全なイムノトキシン遺伝子を連続させて、この遺伝子を翻訳させた。
レオチドアダプターが挿入された。BclIとBamHI末端は両立しており、ハイブリッドBclI/BamHI部位に重ねあわせることができた。BclIヌクレアーゼは、damメチレーションに感受性が高いため、構築にあたって最初に、プラスミドDNAをBclI(およびHindIII)で消化する目的で、dam(−)E.coli株Gm48に形質転換させた。次いでHindIII/BclIフラグメントバック上の完全なイムノトキシン遺伝子を、発現ベクターのHindIII/BclI分解位置に挿入した。
sFvは、sFvのC末端に結合したリシンA鎖と一緒に、Pe1Bシグナル配列を介して分泌される。これを構築するためには、PelB−シグナル配列、sFv、リシンをコードする配列をsFv (発現プラスミド中の)のすぐ後のHindIII部位を介してブルースクリプトプラスミドに結合させる。さらにHindIII部位は、3つの部分の集まり(RI−HindIII−BamHI)においてルシン遺伝子より先行する。リシン遺伝子に続く新しいPstIサイトは、ブルースクリプト ポリリンカーを介して得ることができる。このDNA変異は、sFvの末端でストップコドンとオリジナルのPstIサイトを除去し、幾つかのセリン残基をsFvとリシン遺伝子の間に置くところにある。この新しい融合遺伝子Pe1Bシグナル配列/ sFv /リシンAは発現ベクターのEcoRI/PstIフラグメントに挿入できる。
sFv −PE40は一本鎖Fv− トキシン融合蛋白質であり、蛋白質に最初から存在している18残基短いFBリーダーで構築する。この蛋白質のE.coliでの発現は、3M尿素 グルタチオン/レドックス緩衝液中でリフォールディングしたインクルージョンボディーを生産した。得られたsFv −PE40は、対応する架橋イムノトキシンと比べて、c−erbB−2保持細胞をより完全にかつ明らかにより強い細胞障害作用で、特異的に殺すことができた。741F8 sFvと同様に、sFv −毒素蛋白質は、この方法で効率良く調製できる。乳癌や卵巣癌などのc−erbB−2または関連抗原を保持する腫瘍に対する治療剤、診断剤として使用できる。
A.拮抗ELISA
SK−Br−3抽出物を以下のようなc−erbB−2抗原のソースとして調製した。SK−Br−3乳癌細胞(Ring et al.,1989, Cancer Research 49:3070− 3080)は、5%ウシ胎児血清と2mMグルタミン添加イソコブの培地(ギブコBRLゲイタースバーグMD)でコンフルエンスに近い状態まで培養した。培地を吸引除去して、細胞をカルシウムとマグネシウムを添加した10ml
のウシ胎児血清(FBS)ですすぎ洗い、ゴムの付いたガラス棒でカルシウムとマグネシウムを添加したFBSに取り出した。培養容器は新しいこの緩衝液5mlですすいだ。100rpmの遠心分離で細胞を回収した。上清を吸引除去し、細胞を10mMNaCl、0.5%NP40、pH8の緩衝液(TNN緩衝液)10mMを用いて107細胞/mlの密度になるように再分散させた。そしてピペッティングでアップダウンを行い、ペレットを溶解させた。溶液は1000rpmで遠心し、細胞核とその他の不溶解残渣を除去した。抽出物は0.45のマイレックスHAと0.2のマイレックスGvフィルターで濾過した。TNN抽出物はアリコートとして、ホエートン凍結用バイアルに入れて−70℃で保存した。
培養増殖する乳癌細胞に対して、強い蛋白質合成阻害を示すイムノトキシンは、インビボでその有効性を試験できる。インビボ分析は、ヒト乳癌細胞株MX−1を移植したヌードマウスモデルを使用して一般的に行うことができる。マウスにはPBS(コントロール)、種々の濃度のsFv −毒素のイムノトキシンを注射し、濃度依存的に腫瘍の増殖が抑制されることが観察される。より高い濃度のイムノトキシンの投与がより効果を示すこ
とが予測される。
Claims (1)
- c−erbB−2腫瘍抗原に結合する結合部位を特定する一本鎖Fv(sFv)ポリペプチドであって、該sFvポリペプチドは、ポリペプチドリンカーで連結された少なくとも2つのポリペプチドドメインを含み、該ポリペプチドリンカーは、1つのポリペプチドドメインのC末端と他のポリペプチドドメインのN末端との間の距離にわたっており、該ポリペプチドドメインのそれぞれのアミノ酸配列は、一組のフレームワーク領域の間に挿入された一組の相補性決定領域(CDRs)を含み、該CDRsは、該c−erbB−2抗原に対する免疫学的結合を与え、ここで、該ポリペプチドリンカーは、配列番号4のアミノ酸残基118〜133として示される配列、配列番号15のアミノ酸残基122〜135として示される配列、および配列番号12に示されているアミノ酸配列の群より選択されるアミノ酸配列からなる、一本鎖Fv(sFv)ポリペプチド。
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EP (3) | EP0625200B1 (ja) |
JP (8) | JPH08500962A (ja) |
AT (3) | ATE503496T1 (ja) |
AU (1) | AU675929B2 (ja) |
CA (2) | CA2129663C (ja) |
DE (3) | DE69333807T2 (ja) |
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CA2122732C (en) * | 1991-11-25 | 2008-04-08 | Marc D. Whitlow | Multivalent antigen-binding proteins |
US5932448A (en) * | 1991-11-29 | 1999-08-03 | Protein Design Labs., Inc. | Bispecific antibody heterodimers |
EP0654085B1 (en) * | 1992-01-23 | 1997-04-02 | MERCK PATENT GmbH | Monomeric and dimeric antibody-fragment fusion proteins |
ATE503496T1 (de) | 1992-02-06 | 2011-04-15 | Novartis Vaccines & Diagnostic | Biosynthetisches bindeprotein für tumormarker |
AU4025193A (en) * | 1992-04-08 | 1993-11-18 | Cetus Oncology Corporation | Humanized C-erbB-2 specific antibodies |
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1993
- 1993-02-05 AT AT08075574T patent/ATE503496T1/de not_active IP Right Cessation
- 1993-02-05 AU AU36122/93A patent/AU675929B2/en not_active Expired
- 1993-02-05 EP EP93904938A patent/EP0625200B1/en not_active Expired - Lifetime
- 1993-02-05 AT AT04078206T patent/ATE419355T1/de not_active IP Right Cessation
- 1993-02-05 CA CA002129663A patent/CA2129663C/en not_active Expired - Lifetime
- 1993-02-05 AT AT93904938T patent/ATE295420T1/de not_active IP Right Cessation
- 1993-02-05 CA CA002372813A patent/CA2372813A1/en not_active Withdrawn
- 1993-02-05 WO PCT/US1993/001055 patent/WO1993016185A2/en active IP Right Grant
- 1993-02-05 DE DE69333807T patent/DE69333807T2/de not_active Expired - Lifetime
- 1993-02-05 EP EP08075574A patent/EP1997894B1/en not_active Expired - Lifetime
- 1993-02-05 DE DE69334255T patent/DE69334255D1/de not_active Expired - Lifetime
- 1993-02-05 DE DE69334351T patent/DE69334351D1/de not_active Expired - Lifetime
- 1993-02-05 JP JP5514197A patent/JPH08500962A/ja not_active Withdrawn
- 1993-02-05 EP EP04078206A patent/EP1514934B1/en not_active Expired - Lifetime
- 1993-10-07 US US08/133,804 patent/US5534254A/en not_active Expired - Lifetime
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1994
- 1994-12-12 US US08/356,786 patent/US5877305A/en not_active Expired - Lifetime
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1995
- 1995-06-05 US US08/461,386 patent/US5837846A/en not_active Expired - Lifetime
- 1995-06-05 US US08/461,838 patent/US5753204A/en not_active Expired - Lifetime
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2001
- 2001-06-21 US US09/887,853 patent/US7138497B2/en not_active Expired - Fee Related
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2003
- 2003-03-24 JP JP2003081465A patent/JP4236493B2/ja not_active Expired - Lifetime
- 2003-10-10 US US10/684,237 patent/US20060147444A1/en not_active Abandoned
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2004
- 2004-06-16 JP JP2004178961A patent/JP2005104965A/ja not_active Withdrawn
- 2004-09-07 JP JP2004260280A patent/JP2005168489A/ja not_active Withdrawn
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2007
- 2007-06-20 JP JP2007163220A patent/JP2007231027A/ja not_active Withdrawn
- 2007-06-20 JP JP2007163221A patent/JP2007228979A/ja not_active Withdrawn
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2008
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- 2008-08-15 JP JP2008209384A patent/JP2009035558A/ja not_active Withdrawn
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