JP2978210B2 - 二特異性およびオリゴ特異性の一価およびオリゴ価リセプター、それらの調整および使用 - Google Patents

二特異性およびオリゴ特異性の一価およびオリゴ価リセプター、それらの調整および使用

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JP2978210B2
JP2978210B2 JP2165485A JP16548590A JP2978210B2 JP 2978210 B2 JP2978210 B2 JP 2978210B2 JP 2165485 A JP2165485 A JP 2165485A JP 16548590 A JP16548590 A JP 16548590A JP 2978210 B2 JP2978210 B2 JP 2978210B2
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クラウス、ボスレット
ペーター、ヘルメンツィン
ゲルハルト、ジーマン
ルートウィッヒ、クールマン
アレックス、シュタインシュトレーサー
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Description

【発明の詳細な説明】 ＜発明の分野＞ 本発明は、適当なリンカーによって、二つまたはそれ
以上の異なる特異性の抗体のＦ（ab）断片をコードする
DNAの融合による遺伝子操作によって調製される、二特
異性（bispecific）およびオリゴ特異性（oligospecifi
c）の一価（monovalent）およびオリゴ価（oligovalen
t）リセプターに関する。これに関して、一つの特異性
は、好ましくは、細胞膜上または間隙に位置している腫
瘍関連抗原（TAA）のエプトープに向けられるかまたは
腫瘍内皮（TE）のエピトープに向けられるが、その他の
特異性は高分子量または低分子量のリガンド（ligand）
に関連して、例えば、キレートのエチレンジアミン四酢
酸塩（ethylenediaminetetra−acetate）およびジエチ
レントリアミン五酢酸塩（diethylenetriaminepenta−a
cetate）のY90複合型（各々、EDTA−Y90およびDTPA−Y9
0）と反応する。特に好ましい態様においては、キレー
トとの結合は、fos−jun相互作用（または他にはアビデ
ィン−ビオチン（avidin−biotin）相互作用）を介し
て、キレートリセプターの腕部（arm）上で起きる。他
の好ましい特異性は、触媒的な性質を有する、あるいは
同じ腫瘍細胞上の他のTAAとまたはリンパ球細胞上のリ
セプターと結合する。
＜従来の技術＞ 二特異性抗体は、今日まで、次の方法で調製されてき
た。
異種二機能性（heterobifunctional）リンカーを介す
る多種（diverse）特異性の抗体の化学的結合（H.Paulu
s:Behring lnst.Mitt.78、118−132、1985） 既に入手可能で、種々のモノクローナル抗体（MAb）
を分泌するハイブリドの融合、および二特異性の一価の
部分の単離（U.S.StaerzおよびM.J.Bevan:Proc.Natl.Ac
ad.Sci.USA 83,1453−1457,1986） 二つの異なるMAbの重鎖および軽鎖遺伝子（４個の遺
伝子）のネズミミエローマ細胞または他の真核細胞発現
系へのトランスフェクション、および二特異性一価部分
の単離（U.Zimmermann:Rev.Physio.Biochem.Pharmacol.
105、176−260、1986、J.van Dijkら:lnt.J.Cancer 4
3、344−349、1989） この型の二特異性抗体は、悪性腫瘍の治療および診断
に用いられる。方法の原理は、第一段階において、長期
にわたって大量投与量で二特異性巨大分子（macromolec
ule）を注射することによって、標的細胞上で二つの特
異性の中の一つによって認識されるエピトープの飽和を
達成することからなる。
数日間の治療の中断からなる第二段階において、非特
異的に吸着した二特異性抗体の非標的組織からの自己除
去（autoelimination）がある。この自己除去は、糖残
基、好ましくはガラクトース、に結合している抗イディ
オタイプ抗体の注射によって加速することができ、二特
異性リセプターの抗腫瘍腕部に対して向けられる。
方法の第三段階は放射性同位元素で標識した親水性低
分子量リガンドの静脈内注射からなるが、このリガンド
は、細胞内で蓄積せず、体内停留時間が短く、90Y、186
Re、188Re、189Re、99mTcまたは111Inなどのβ−および
γ−エミッターの複合定数（complexing constant）が
高く、かつ二特異性リセプターの第二の特異性に高い親
和性で結合する。この段階の結果、標的組織上での保持
が延長されるとともに放射性リガンドの濃縮が行われ、
その結果、標的組織の選択的崩壊がなされて、例えば、
転移（metastases）の診断が可能になる。
発明の具体的説明 本発明は、要求に応じて、特定のエピトープとの一価
またはオリゴ価結合部位を有しており、適当なリンカー
による遺伝子操作によって産生される、二特異性および
オリゴ特異性リセプターを今提供する。すなわち、抗体
ａおよびｂのVHおよびCH1部分をコードする遺伝子断片
を、例中の表１に示されるような適当な合成オリゴヌク
レオチドを用いて、MAbbのVHドメイン（domain）のＮ末
端をポリペプチドスペーサーを介してMAb aのCH1ドメイ
ンのＣ末端に共有結合で結合させるようにして、連結さ
せる（第１図）。VHaCHla−ポリペプチドスペーサー−V
HbCH1b遺伝子構築物を、抗体ａおよびｂの軽鎖の遺伝子
とともに真核細胞（例えばマウスミエローマ細胞）にト
ランスフェクト（transfect）させる。CH1a、CH1b、CKa
およびCKbドメインを、反対荷電が定常ドメイン（CH1a
（＋）CKa（−）、CH1b（−）CKb（＋））（＋＝陽性、
−＝陰性）と接触領域で合わさるように、または、接触
の反対領域が各場合に疎水性または各場合に親水性であ
るようにして、修飾する。これは、トランスフェクトさ
れたもの（形質転換体、transfectomas）が、重鎖およ
び軽鎖の正しい対合を有するハイブリド分子を選択的に
発現することを意味する（第２図）。
ここで、抗体ａは抗腫瘍抗体の代表的な例で、抗体ｂ
は低分子量リガンド、好ましくはキレートDTPA−Y90ま
たはEDTA−Y90、に対する抗体を表すものである。
従って、二特異性またはオリゴ特異性リセプターは、
適当なリンカーを介しての、多種特異性の抗体のVHおよ
びCH1ドメインの遺伝子工学的な構築を意味し、これに
よれば、対応する軽鎖との結合のための要求される移動
性（mobility）が存在して、抗原結合が妨げられない。
抗原結合部位は、結合価（vanlencies）または結合部
位と呼ばれる。二特異性一価リセプターは、したがっ
て、二つの特異性がある場合には各場合に一つの抗原結
合部位を有する。したがって、二特異性三価リセプター
は、一つの特異性のための一つの抗原結合部位を、他の
特異性のために二つの抗原結合部位を各々有する。
腫瘍抗原（MAb ａ）に対して二価であってEDTA−Y90
（MAb ｂ）に対して一価である二特異性リセプター
を、上記のオリゴヌクレオチドリンカーを用いて、上記
の重鎖遺伝子構築物をMAb ａのVHおよびCH1ドメインを
コードする遺伝子部分に連結させることによって調製し
て（第３図）、ポリペプチドスペーサーによってMAb
ｂのCH1ドメインのＣ末端をMAb ａのVHドメインのＮ−
末端に連結するようにする。これらの遺伝子構築物を、
MAb ａおよびｂに属する軽鎖の遺伝子とともに真核細
胞（例えばミエローマ細胞）にトランスフェクトさせ
る。上記のようにして、CH1およびCKドメインは、相補
的な荷電または各場合に疎水性または親水性である接触
領域とともに提供される。形質転換体は、MAb ａの二
つのＦ（ab）断片およびMAb ｂの一つのＦ（ab）断片
（第４図）を含む融合分子を選択的に発現する。ペプチ
ドリンカーの移動性は、MAb ａの二つのＦ（ab）腕部
の腫瘍細胞に対する整列（alignment）、同時に、細胞
間空間に対するMAb ｂのＦ（ab）腕部の整列を可能に
する。同様に、同一または異なる特異性のさらなる結合
部位を加えることが可能である。さらに、構築物中の特
異性の配列（sequence）を自由に組み合わせることが可
能である。
したがって、本発明は、例えばTAAまたはTEのよう
な、細胞膜上または間隙中に位置するエピトープのため
の特異性と、細胞外空間にのみ分布する低分子量または
高分子量リガンドのための特異性とを共に有する、二特
異性またはオリゴ特異性、一価またはオリゴリセプター
に関する。これに関連して、一つの特異性は、独国特許
出願第p 39 09 799.4号明細書において提示されたよう
に、好ましくは腫瘍特異性抗体によって形成され、他の
特異性は、好ましくは、DTPA−Y90またはEDTA−Y90に対
して向けられる。特に好ましい態様においては、結合は
キレートと、fos−jun相互作用（例５を参照されたい）
を介してキレートリセプター腕部上で起きる。他の好ま
しい本発明の変形は、触媒的活性を有する特異性の組み
入れからなる。さらに、二つの特異性を有する三価の第
４図の例で示されるように、特異性の配列または結合価
の選択に制限はない。
本発明の特に好ましい構築物は、表２、３、４および
／または５のＶ遺伝子を含むものである。これらの配列
有する抗体およびそれらの性質は、独国特許出願第p 39
09 799.4号明細書に記載されている。さらに、相補性
決定領域（CDR）は、KabatおよびWu（Sequences of Pro
teins of lmmunological lnterest、US Dept.of Health
and Human Services、US Government Printing Offic
e、1987）の方法によって同定することができる。同様
に好ましい構築物は、上記のモノクローナル抗体によっ
て定義されたエピトープに対する特異性を含むものであ
る。
加えて、本発明は、上記の構築物の調製のための遺伝
子工学的方法、および標的細胞の抑制および診断のため
の医薬物の調製のための上記構築物の使用に関する。す
なわち、第一の段階において、構築物を注射した後に標
的細胞上で関連エピトープを飽和させて、次いで、非特
異的に吸着したあるいは非結合の構築物を除去する。こ
れに続く次の段階は、注射および次いでの低または高分
子量リガンドの特異的結合からなるが、このリガンド
は、細胞内に蓄積されず、本質的に細胞毒性（cytotoxi
c）または適宜に他の段階において身体外（extracorpor
eal）の影響によって細胞毒性に「活性化」されるもの
である。この型の方法の例は、酵素的活性化、プロドラ
ッグのマイクロ波照射による活性化またはレーザー光線
による活性化などがある。
本発明は、さらに諸例および特許請求の範囲に示され
る通りである。
例1:抗−DTPA−Y90またはEDTA−Y90MAbの調製 イソチオシアネートベンジル−DTPA（化学式２）を、
N.W.Brechbielら（lnorganic Chemistry25、2772−278
1、1986）による記載の方法によってヒト血清アルブミ
ン（HSA、キャリアとして）に、HSA分子当り19個のベン
ジル−DTPAの誘導化（derivatization）率で、ハプテン
として共有結合させた。冷却したＹを中に複合させてお
いたこのハプテン−キャリア複合体の20μｇを、０日目
にフロイントのアジュバントとともに、７日および14日
目に不完全フロイントアジュバントとともに、および21
日目にPBSとともに、Balb/cマウスに皮下注射した。24
日目に、最高値の抗−DTPA抗体タイマーを示すマウスの
脾臓を、SP2/0−Ag14ミエローマ細胞系（Shulmanら:Nat
ure276、269、1978）と融合させた。得られるハイブリ
ドーマを、DTPAおよびEDTAに対する高親和性のMAbの産
生についてDTPA−特異性ELISA中で試験した。ELISAは、
HSA−ベンジル−DTPA−Ｙを含む溶液を負荷した固相か
らなる。試験されるMAbを含む上清を遊離のキレートま
たはその金属イオン複合体と予備インキュベートしてか
ら、特異的固相との結合を測定した。抗−マウス免疫グ
ロブリン抗体と結合している酵素増幅系を、この目的の
ために用いた。これらの方法の詳細は付録1aおよび1bに
記載の通りである。
付録1eに記載の性質を有するMAbは、この分析系を用
いて得られた。
他の多くの抗−DTPA/EDTA MAbと対照的に、これらMA
bは、APAAP技法（Cordellら:J.Histochem.Cytochem.3
2、219、1984）を用いて見出されたように、冷温保存さ
れた（cryopreserved）組織上で正常ヒト組織と結合し
ない。したがって、これらのMAbをインビボで診断およ
び治療に用いることが可能である。
用いるコンペティター（competitors）は、キレートD
TPAおよびEDTAの非−複合および複合型（付録1c）であ
る。
加えて、構造的に関連した化合物トランスアコニット
酸および1,2−ジアミノエタンをインヒビターとして用
いた（付録1eを参照されたい）。MAbBW2050/174はイン
ビボ使用に特に適しており、他のMAb全てと対照的に、E
DTA−Ｙへの選択的結合を示す（付録1e、EDTA−Ｙの低
いコンペティター過剰量（100×）と他のEDTA複合体の
より高い過剰量、を参照されたい）。ハイブリド2050/1
74を、したがって、安定化させて、二特異性リセプター
におけるEDTA−Ｙ腕部を作出するのに用いた。
例2:VH1a CH1−リンカー−VH1b CH1遺伝子構築物の調
製および発現 ここで用いた技法は、特に記載がない限り、Molecula
r Cloning、A Laboratory Manual、Sambrook、Fritsc
h、Maniatis、Cold Spring Harbor Laboratory、1982
（pp.11−44、51−127、133−134、141、146、150−16
7、170、188−193、197−199、248−255、270−294、31
0−328、364−401、437−506）およびMolecular Clonin
g、A Laboratory Manual、Second Edition、Sambrook、
Fritsch、Maniatis、Cold Spring Harbor Laboratory P
ress、1989（pp.16.2−16.22、16.30−16.40、16.54−1
6.55）から採用した。
ヒトIgG3C遺伝子を、EMBL3ファージ（A.M.Frischauf
ら:J.Mol.Biol.170、827−842、1983およびG.H.A.Seema
nnら:The EMBO Journal 5、547−552、1986）中のヒト
遺伝子バンクから単離した。
一方でCH1エクソンおよびヒンジエキソンのみを含み
（第５図）、他方でCH1エクソンおよびHLA B27遺伝子
の３′NT領域を含む（第６図、プラスミドＭ中の断片
Ｍ）、構築物をこのIgG3C遺伝子から独国特許出願第P 3
8 25 615.0号明細書に記載のようにして調製した。
VHaおよびVHb遺伝子を、ハイブリドクローンａおよび
ｂのmRNAからOrlandiら（Proc.Natl.Acad.Sci.USA 86、
3833−3837、1989）による記載のようにして増幅させ
て、M13ベクター中でクローニングした（VHa PCRおよ
びVHb PCR）（第７図）。VHa遺伝子をHind III−BamH
I断片として真核細胞発現ベクターpEVH（Simonら:Nucl.
Acids Res.16、354、1988）中でクローニングした（第
８図）。その結果、プラスミドpEVHaCが得られた。
CH1および一つのヒンジエクソンを有するヒトIgG Ｃ
遺伝子サブクローン（第５図）は、CH1エクソンとヒン
ジエクソンとの間にPst I切断部位を含む。VH遺伝子
は、５′末端にPst I切断部位を含む。リンカーオリゴ
ヌクレオチドは、それが５′末端でIgG Ｃ遺伝子のCH1
＋1Hサブフラグメント上のPat I切断部位領域および
３′末端でVHb遺伝子のPst I切断部位と、重複（overla
p）するように設計されている。リンカーオリゴヌクレ
オチドは、そのPstI切断部位によってPUC18プラズミド
のPst I切断部位にクローニングされる（第９図）。結
果としてプラスミドクローンＬが得られる。
CH1エクソンおよびヒンジエクソンを有するIgG3C遺伝
子サブフラグメントを有するプラスミドを、Pst Iおよ
びBamH Iで切断して、VHbPCRからPst I−BamH I断片と
して切り出したVHb遺伝子断片に連結させる（第10
図）。その結果、プラスミドＸが得られる。
プラスミドＸをPst Iで切断して、プラスミドＬから
同様にPst Iで切り出しておいたリンカー断片に連結さ
せる（第11図）。核酸配列分析を用いて、リンカーが、
正しい位置方向でCH1とVHbとの間にイントロン３とリン
カーエクソン間のイントロン／エクソン結合部を損なわ
ず、かつ、リンカーとVHb遺伝子間の結合部における解
読枠を損なわずにクローニングされている、クローンＺ
を同定する。
プラスミドpEVa ＣをBamH Iで切断して、プラスミド
ＭからBamH Iで切り出しておいた断片Ｍと連結させる。
制限酵素分析を用いて、断片Ｍを正しい位置方向で含ん
でいるクローンＹを同定する（第12図）。
プラスミドＹをBamH Iで部分的に切断して、全ての末
端を埋填した後に、プラスミドＸからHind IIIおよびBa
mH I切断によって切り出した断片（CH1−リンカー−V
Hb）に連結する。ヌクレオチド配列分析および制限地図
作出を用いて、全てのエクソンを正しい位置方向で有す
る融合遺伝子VHa CH1−リンカー−VHb CH1を含むプラ
スミドクローンPEVTを同定する（第13図）。
プラスミドPEVTを、抗体aF（ab）抗体bF（ab）融合タ
ンパク質を発現させるために、抗体ａおよびｂの軽鎖の
遺伝子を有するプラスミドとともに適当な真核発現細胞
にトランスフェクトさせる。
例3:二つの異なるMAbの軽鎖および重鎖遺伝子（４遺伝
子）のトランスフェクション 免疫グロブリン遺伝子の単離は、独国特許出願第P 39
09 799.4号明細書に記載されている。
ベクターにクローニングされた遺伝子を、ベクターを
線状にした後にエレクトロポレーション（electroporat
ion）によってX63Ag8.653ミエローマ細胞（H.Stopper
ら:Biochem.Biophys.Acta900、38−44、1987）中にトラ
ンスフェクトさせた。選択培地中で増殖した形質転換体
を、特異的RIA中で二特異性一価MAbの産生について試験
した。このRIAは、カゼインによる非特異的部位のブロ
ックの後、分析される形質転換体上清を上に位置させた
固相上に吸着させたTAAからなった。90Yまたは99mTcと
複合しているDTPAまたはEDTAを加えてから過剰分を洗い
流した後、二特異性一価抗−TAA×抗−EDTA MAbを分泌
したこれら形質転換体を、固相上の増加した放射性シグ
ナルによって検出することが可能であった。
形質転換体９を、制限希釈クローニングによって安定
化させて細胞培養中に広げた。細胞培養上清を、10×に
濃縮して、MAb画分をタンパク質Ａクロマトグラフィー
（P.L.Eyら:lmmunochemistry15、429、1978）によって
精製し、二特異性一価MAbを含む画分をアニオン交換ク
ロマトグラフィー（Ｊ・Van Dijkら:lnt.J.Cancer 43、
344−349、1989）によって精製した。
例4:生物学的有効性 二特異性一価MAb（BW431/26×BW2050/174）を含む精
製タンパク質を、500μｇの投与量で０、３、５、８、1
0および12日目にヒト腫瘍異種移植片（xenografts）（C
oCa4）を有するヌードマウスに静脈内注射した。27〜30
日目の各動物にEDTA−Y90の50μCiを静脈内注射した。
第二のグループの動物には同じ日に二特異性MAbの代わ
りに500μｇのMAb BW431/26、およびEDTA−Y90注射を
上記のように行った。
第三の腫瘍を有するグループには、MAbおよびEDTA−Y
90の代わりにPBS（腫瘍増殖コントロールとして）を注
射した。腫瘍の増殖を６週間追跡した。EDTA−Y90の注
射の結果、二特異性一価MAbを注射されたグループにお
いて腫瘍の増殖の有意の阻害が認められたが、一方、MA
b BW431/26を注射して、EDTA−Y90で処理した動物で
は、PBSのみを注射された動物と同じく、腫瘍増殖の阻
害がみられなかった。
これらのデータは、毒性素因（principle）としてEDT
A−Y90と組合せて二特異性一価MAbの選択的腫瘍治療効
果を示す。
さらにより好ましい腫瘍治療効果はオリゴ価／二特異
性またはオリゴ特異性リセプターによって得られる。な
ぜならば、これらはTAAとの二価結合のために腫瘍上に
より長く保持され、したがって、リガンドが同様に腫瘍
上により長く、より高濃度で保持されるからである。
例5:抗−キレート腕部の強い要求性（avidity）を増加
させることによる、二特異性またはオリゴ特異性巨大分
子の生物学的有効性の最適化 細胞外分布をしている親水性キレートのオリゴ特異性
巨大分子の抗−キレート腕部への効果的な付着に影響す
る決定的な因子は、キレートへのこの腕部の強い要求性
である。モノクローナル抗体のそれらの対応するエピト
ープへの強い要求性は、105〜1011l/molの範囲である。
これらの結合強度は、効果的なラジオイムノセラピー
（radioimmunotherapy）に必要な量のキレートを腫瘍上
に位置させるにはあるいは不十分であることから、次の
例においては、fos−ロイシン−ジッパー（zipper）ペ
プチド（fos−ペプチド）とjun−ロイシン−ジッパーペ
プチド（jun−ペプチド）（Erin k.O′Sheraら:Scienc
e、245、1989）とのきわめて強い相互作用を用いて、キ
レートをできるだけ強固に抗−キレート腕部上に固定化
した。この強力なfos−jun相互作用を利用することがで
きるように、好ましくは、fos−ペプチドを共有結合で
キレート（DTPA）に連結させることが必要である。この
目的のために、第一の手段においてイソチオシアネート
ベンジル−DTPAをヒドラジン（またはジアミノアルカ
ン）と反応させることが可能である。このようにして産
生されたDTPA−ベンジルチオカルバジドを、第二段階に
おいて、Ｎ−（γ−マレイミドブチリルオキシ）サクシ
ニミドまたは類似体と反応させて、DTPA−ベンジル−
（γ−マレイミドブチリル）チオカルバジドを得ること
ができる。次いで、第三の段階で、この化合物をグリシ
ン−グリシン−システイン（第１図）によって広げてお
いたfos−ペプチドに、アミノ末端のシステインの遊離
のSH基を介して連結させる。このようにして産生された
fos−ペプチド−DTPA抱合体（conjugate）を、第四段階
において、塩化イットリウム（yttrium）と複合化させ
る。このようにして産生されたfos−ペプチド−DTPA−
Ｙ抱合複合体を、次いで二−またはオリゴ特異性巨大分
子のjun−ペプチド腕部へのインビボ添加に用いること
ができる。以上略述した例の合成を以下に詳述する。
Ａ）fos−EDTA−Ｙ抱合複合体の調製 段階1: EDTA−ベンジルチオカルバジドの合成 イソチオシアネートベンジル−EDTA（SCN−Bn−EDT
A）（30mg、54μmol）を10％（v/v）水成ヒドラジン中
で１時間攪拌した。次いで、溶媒を高真空下で除去し
て、残留物を五酸化リン上で高真空下で乾燥させて、最
後に凍結乾燥した。産生物をDOWEX WX2（H+型）で中和
して、再び凍結乾燥した（収量28mg）。
段階2: DETA−ベンジル（γ−マレイミドブチリル）チオカルバ
ジドの合成 段階１で調製されたEDTA−ベンジルチオカルバジド
（20mg、34μmol）およびＮ−（γ−マレイミドブチリ
ルオキシ）サクシニミド（8mg、29μmol＝0.9等量）を
無水ジメチルフォルムアミド中で１時間攪拌した。混合
物を、次いで、蒸発させて乾燥して、残留物を高真空下
で乾燥した。
段階3: EDTA−ベンジル（γ−マレイミドブチリル）チオカルバ
ジドの、fos−ペプチド中のアミノ末端システインへの
カップリング fos−ペプチド（4.8mg、１μmol）（段階3.1を参照さ
れたい）の燐酸緩衝生理食塩水（2ml）を、段階２で得
られた産生物混合物（4mg）のジメチルフォルムアミド
（400μｌ）懸濁液と混合して、室温で１時間インキュ
ベートした。反応混合物を、次いで、燐酸緩衝生理食塩
水中でセファデックスG15カラム上でのゲル濾過に供し
た。タンパク質を含む溶出液を集めて−30℃で保存した
（収量4.2mg）。
段階3.1: Ｎ−末端GGC延長を有するfos−ペプチド（｜ ｜）のア
ミノ酸配列 各アルファベット文字は次のアミノ酸を表す。Ａ＝ア
ラニン、Ｃ＝システイン、Ｄ＝アスパラギン酸、Ｅ＝グ
ルタミン酸、Ｇ＝グリシン、Ｉ＝イソロイシン、Ｋ＝リ
ジン、Ｌ＝ロイシン、Ｍ＝メチオニン、Ｎ＝アスパラギ
ン、Ｑ＝グルタミン、Ｒ＝アルギニン、Ｓ＝セリン、Ｔ
＝スレオニン、Ｖ＝バリン、Ｙ＝チロシン。
オリゴペプチドを、自動ペプチド合成機（Applied Bi
osystems Model 430A）を用いてタート−ブチルオキシ
カルボニル保護基を用いるMerrifield固相法（Stewart
およびYoung:Solid Phase Synthesis、Pierce Chemical
Company、第二版Rockford lll.）によって合成した。
オリゴペプチドを、フェニルアセタミドメチル−ポリス
チレン支持体から切り出した。保護基（Tomら:J.Am.Che
m.Soc.105、6442−6455、1983）を除去した後、オリゴ
ペプチドをRivierら（J.Chromatography 288、303−32
8、1984）による記載の逆相クロマトグラフィー（PepRP
Cカラム、Pharmacia社製）によって精製した。
段階4: 段階３において調製されるfos−ペプチド−EDTA抱合体
を有する、fos−ペプチド−EDTA−イットリウムキレー
トの調製 段階３のようにして調製されたfos−ペプチド−EDTA
抱合体（4.2mg）を、等張生理食塩水/0.1Mクエン酸ナト
リウム（pH7.0）に対して、分子量1,000の排除限界（ex
clusion limit）を有する透析チューブ（スペクトラ
ム）中で透析して、3mlの等張生理食塩水/0.1Mクエン酸
ナトリウム（pH7.0）に溶解した6mgの塩化イットリウム
と混合した。１時間後、燐酸緩衝生理食塩水に対して逆
透析を行って、キレート溶液を−30℃で保存した。上記
の例に記載したfos−ペプチド−EDTA−イットリウムキ
レートを次いで、高い要求性で二特異性またはオリゴ特
異性巨大分子のjun−ペプチド腕部と結合させるため
に、リガンドとして用いる。特にこの相互作用に適して
いる二特異性巨大分子の構築は、次の例に記載されてい
る。
Ｂ）MAb−jun融合分子の構築 ここで用いる技法は、特に記載がない限り、Maniatis
ら（Laboratory Manual EMBL、1982、Heidelberg）およ
びSambrook（Molecular Cloning:A Laboratory Manua
l）から採用した。
段階1: ヒトIgG3C遺伝子を、EMBL3ファージ（A.M.Frischauf
ら:J.Mol.Biol.170、827−842、1983およびG.H.A.Seema
nnら:The EMBO Journal 5、547−552、1986）中のヒト
遺伝子バンクから単離した。IgG3C遺伝子のCH1エクソン
および最初のヒンジエクソンのみを含む構築物（Ｄ）
（第14図）を、このIgG3C遺伝子から独国特許出願第P 3
825615.0号明細書に記載のようにして調製した。
ヒトHLA B27k遺伝子を、同じ遺伝子バンクから同じ
く独国特許出願第P 3825615.0号明細書に記載のように
して調製した。C3エクソンおよびHLA B27k遺伝子の
３′NT領域のみを含む構築物（Ｅ）（第15図）を、この
HLA B27k遺伝子から調製した。
段階2: C1エクソンおよびHLA B27k遺伝子の３′NT領域をプ
ラスミドＥからXbaIで切り出して、断片を単離して、構
築物ＤのXbaI切断部位にクローニングした。制限酵素分
析および核酸配列分析を用いて、C3エクソンおよびHLA
B27k遺伝子の３′NT領域を正しい５′−３′の位置方
向で含む、３′がIgG3C遺伝子断片からである、クロー
ンＦを同定した（第16図）。
段階3: クローンＦの挿入物を、エンドヌクレアーゼHind III
およびEcoR Iを用いてプラスミドから切り出して、M13m
p18二本鎖（DS）ファージのHind IIIとEcoR I切断部位
間にクローニングする。抗体/HLA融合遺伝子断片を含む
ファージクローンＧを単離する（第17図）。
段階4: ウラシル一本鎖を、ファージクローンＧからT.A.Kunk
el（Proc.Natl.Acad.Science、U.S.A、82、488−492、1
985）の方法で調製する。一本鎖ファージを、突然変異
誘導性（mutagenic）オリゴヌクレオチド１および２
（表６）とハイブリダイズさせて、オリゴヌクレオチド
間の間隙をクレノウDNAポリメラーゼおよびT4リガーゼ
で閉環させた。大腸菌（E.coli）中での形質転換の後、
制限酵素分析および核酸配列分析を用いて、ヒンジエク
ソンの５′末端におけるSst I制限酵素切断部位が除去
されたファージクローン（Ｇ）を同定した。同時に、Ss
t IおよびSph I制限酵素切断部位を、ヒンジエクソンの
３′末端に導入した（第18図）。Sst I切断部位を除去
するためにヒンジエクソンの第二のコドンの３番目の塩
基をＣからＧに変換して、SstI およびSph I切断部位を
導入するために塩基群５′GAGCTCGGGGCA3′をヒンジエ
クソンの15番目と16番目のコドンの間に導入した（表
７）。
段階5: ファージクローンＧ′の二本鎖DNAを、Shp Iで完全に
Sst Iで部分的に切断する。合成オリゴヌクレオチドJun
IおよびJun II（表８）を合わせて、その各末端にSph
IおよびSst I制限酵素切断部位の切断部を含み、Junロ
イシンジッパー（０′Sheaら:Science、245、646−64
8、1989）を含むペプチドをコードする、二本鎖DNA断片
が得られる。
二本鎖DNA断片をＦ′ファージクローンのSst Iおよび
Sph I制限酵素切断部位にクローニングして、ヒンジエ
クソン中にJunジッバーペプチドのための配列が挿入さ
れた遺伝子構造物を含むファージクローンＨを同定する
（第19図）。
段階6: DSファージＨの挿入物を、制限エンドヌクレアーゼHi
nd IIIおよびEco RIで切り出して、末端をT4ポリメラー
ゼで埋填して、SmaI−切断KsFベクター（Stratagene、1
1099 North Torrey Pines Road、La Jolla California
92037）中にクローニングした。抗体/Jun/HLA融合遺伝
子をその両側をBamH I切断部位で挟むように位置して含
む、プラスミドクローンＩを同定した（第20図）。
段階7: 抗体/Jun/HLA融合遺伝子を、KSクローンＩからBamH I
で切り出して、特異的機能性免疫グロブリンＶ遺伝子を
含む発現プラスミドpABStop（Behringwerke AG）中にク
ローニングした。特異的Ｖ遺伝子を、特許出願第P 3909
799.4号明細書に記載のようにして得る。抗体/Jun/HLA
融合遺伝子構築物を正しい位置方向でVH遺伝子の下流に
含む発現プラスミドＫを、同定した（第21図）。
プラスミドＫと特異的MAbの軽鎖のための遺伝子を含
むプラスミドおよび耐性（resistance）遺伝子を有する
プラスミドの共形質転換（cotransformation）によっ
て、ヒンジ領域に二つのJunジッパーペプチドを含み、
もはやいかなるホモダイマー（homodimer）（Jun/Jun）
形成のないようにJunジッパーペプチドが修飾されてい
る、特異的抗体Ｆ（ab′）２断片の発現が導かれる。
例6: 腫瘍上の二特異性またはオリゴ特異性リセプターの量の
最適化、および血液および正常組織中でのそれらの最少
化 他者による科学的な研究調査は、巨大分子（＞50k D
a）による固体腫瘍の浸透（penetration）は緩慢に起
き、通常、縁辺領域または腫瘍の少ない領域のみに達す
ることを示している。これらの研究調査は、少量の巨大
分子の一回の注射からなる実験に基づいている。これに
対して、本発明者らは、ヌードマウス異種移植片におけ
る全腫瘍体の実質的な侵透が多量の二特異性またはオリ
ゴ特異性リセプターの反復的な静脈内注射（10×250μ
ｇリセプター／マウス、10日間）によって可能であるこ
とを見出した。さらに、これらのTAAへの特異的結合の
故に二特異性またはオリゴ特異性リセプターは、腫瘍細
胞膜上および腫瘍間隙中で長期の間（＞20日）大量に付
着したままで保持される。これらの結果は、ヒト直腸お
よび膵臓腫瘍異種移植片の冷温保存された（cryopreser
ved）薄切片に間接的アルカリフォスファターゼ技法を
用いて得られた。
この間（わずか10日後）に二特異性およびオリゴ特異
性リセプター分子は、崩壊および排除によってTAA−陰
性正常組織および血液から既に除去されていた。この除
去期間を短縮するために非結合の二特異性またはオリゴ
特異性リセプター分子の抗−TAA腕部とのみ反応する抗
−イディオタイプMAb（抗Id）を二−またはオリゴ特異
性リセプターの10回の注射の完了後24時間に静脈内注射
した。この一回の注射は非結合二−またはオリゴ特異性
リセプター分子の血液からの除去を速めて、肝臓および
脾臓における代謝率を高めた。
この操作に基づいて、キレート（EDTA−Y90）を二−
またはオリゴ特異性リセプターの浸透および結合相の完
了後わずか４日後に注射することが可能である。次の治
療方法（ヌードマウス用）は、これらの知見から導かれ
たものである。
ａ） １〜10日目、各回１×250μｇの二−またはオリ
ゴ特異性リセプターの静脈内注射 ｂ） 11日目、１×50μｇの抗Idの静脈内注射 ｃ） 14日目、治療的投与量のEDTA−Y90の静脈内注射 ヌードマウスと腫瘍患者における比較的免疫シンチグ
ラフ（immunoscintigraphic）データに基づいて、この
方法は、ヒトにおいても腫瘍治療に適していると考えら
れる。しかし、ヒト系において注射されるべき量は、範
囲が異なる（10×５〜10gの二特異性リセプター、１×1
gの抗I d）。抗I dの注射は、治療には必ずしも必須で
はない。
付録1a DTPAまたはEDTA複合体による、MAbの定量的阻害ELISA 材料：分割可能な96−ウェルポリスチレンマイクロタイ
タープレート（Ｕ型）タイプＢ、Nunc社製、No.4−6044
5 １） １μｇ抱合体/mlPBS（pH7.2）の濃度の50μｌの
Ｙ−ベンジル−DTPA−HSA19抱合体を、各ウェルにピペ
ットで入れて、室温で一晩インキュベートする。
２） 上清を吸引によって取り除いて、３回0.05Mトリ
スクエン酸塩緩衝液（pH7.4）（洗浄溶液１）で洗浄す
る（１回洗浄＝250μl/ウェルの洗浄液をウェルに入れ
て２分間靜間してから吸引によって除去する）。
３） マイクロタイタープレートがすぐに必要でない場
合には、それをセルロース上に室温で一晩置く（開口部
を下にして）。次いでプレートを、乾燥カートリッジ
（Gaplast社製、postrach529、8100Garmisch−Partenki
rchen）とともにフィルムに密閉する。プレートを、＋
４℃でこれらの条件化で少なくとも８週間保存すること
ができる。
４） 250μｌのブロッキング溶液を各ウェルに入れ
て、37℃で30分間インキュベートする。
５） 希釈されたハイブリドーマ上清とコンペティター
との予備インキュベーションをブロッキングの間に行う
（付録２を参照されたい）。
６） 50μｌの適宜に予備希釈して予備インキュベート
した試験すべきハイブリドーマ上清を、各ウェルに入れ
て、室温で30分間インキューベートする。
７） 洗浄溶液２で３回洗浄を続いて行う。
８） 次いで、アルカリフォスファターゼで標識してか
らブロッキング溶液で1:500に希釈しておいたヤギ抗−
マウスIgG1抗体50μｌを各ウェルに入れて、室温で30分
間インキュベートする。
９） 次いで、Enzygnostのための洗浄溶液で３回洗浄
を行う。
10） 次いで、50μｌの0.1mM NADPを加える。
11） 室温でのインキュベーションを次いで30分間行
う。
12） NADPとのインキュベーションの間に、増幅系を次
のようにして作る。
プレート当り２部のINTと１部のPBS（pH7.2）を混合
して、１部のジアホラーゼ（diaphorase）と１部のADH
をピペットで入れる。
13） この系の50μｌを各ウェルに入れる。
14） 透明から赤へと色に明確な変化が起きたとき、ウ
ェル当り100μｌの0.1NH2SO4溶液によって反応を停止さ
せる。
15） TITERTEKR MULTISCAN中で492nmで吸光度（extinc
tion）を測定する。50μｌのNADPと50μｌの溶液および
1200μｌの0.1N H2SO4をブランクとして用いる。
ブロッキング溶液： PBS（pH7.2）に、カゼインを加えて30分間攪拌してカ
ゼイン３％濃度にして、pHを7.4に調整する。次いで4,0
00rpmで10分間遠心分離して粒子を除去する。
希釈ヤギ抗−マウスIgG1抗体をアルカリフォスファタ
ーゼ（Southern Biotechnology Associates社製、カタ
ログ番号1080−04）で標識する。
0.1mM NADPの調製： 7.65mgのNADPを、100mlの20mMトリス、0.1mM MgSO
4（pH9.5）に溶解する。この溶液は−20℃で数カ月保存
できる。
INT（Ｐ−IODONITROTETRAZOLIUM Violet）の調製： 2.5mg/mlの30％エタノールを超音波槽で溶解する。常
に新鮮なものを調製する。
ジアホラーゼの調製： 1mgジアホラーゼ/mlPBS（pH7.2）を少量づつに分けて
−20℃で保存する。
アルコールデヒドロゲナーゼの調製： 0.5mgADH/mlPBS（pH7.2）を少量づつに分けて−20℃
で保存する。
付録1b ハイブリドーマ上清の、コンペティターとの予備インキ
ュベーション ハイブリドーマ上清中のマウスIgG濃度を、市販の定
量ELISA系を用いて決定することができる。
ELISA濃度決定に基づいて、ハイブリドーマ上清をCa
++およびMg++を含まないPBS中で1.25μg/mlに希釈す
る。
グラムからモル（mol）への変換： 150,000g −１モルのMAb 1.25×10-6g −ｘモル 1.25μg ＝ｘ＝8.33×1012モル MAbとインヒビターの１＋１比を得るために、8.33×1
0-12モル/200μｌ（これは５の係数（factor）で増え
る）の濃度のインヒビターの10μｌを、8.33×10-12モ
ル/mlの濃度のハイブリドーマ上清の50μｌに加える。
ハイブリドーマ上清を、コンペティターの100,000
倍、50,000倍、10,000倍、5,000倍、1,000倍および100
倍の濃度で室温で30分間インキュベートする。この50μ
ｌを、ピペットでELISA（付録1aのno.6を参照された
い）に入れる。
付録1c DTPAおよびEDTA複合体の産生 表Ｉに示したDTPAまたはEDTAの金属イオンとの複合定
数は著しく高いために、これら金属イオンとのDTPAまた
はEDTAの等モル混合では完全な飽和が期待されねばなら
ない。このために、対応する金属イオンを、DTPAまたは
EDTAと３倍モル過剰量でインキュベートした。例とし
て、170μｌの10mM硫酸カドミウム溶液（二度蒸留水溶
液）（付録1dを参照されたい）を30μｌの0.028モルDTP
A保存溶液（二度蒸留水溶液）と室温で５分間インキュ
ベートした。このコンペティター溶液10μｌをハイブリ
ドーマ上清と混合することによって、コンペティターは
ハイブリドーマ上清中に含まれるMAbの100,000倍過剰と
なる。より低いコンペティターとMAb比は、コンペティ
ター溶液を特別な塩イオン溶液で所望のモル過剰に適宜
に希釈することによって達成された（付録1bを参照され
たい）。
付録1d 用いる金属イオンの入手元および関連物理化学的パラメ
ーター 次の金属イオンの10ミリモル溶液を、二度蒸留水中に
調製した。
塩化マンガン 分子量 161.88 メルク社製 No.5934 Mnイオン半径:80pm 硫酸カドミウム 分子量 256.5 Riedel de Haen No.31145 Cdイオン半径:97pm 塩化亜鉛 分子量 136.28 メルク社製 No.8816 Znイオン半径:74pm 硫酸銅 分子量 159.61 Riedel de Haen No.31294 Cuイオン半径:96pm 塩化イッテリウム 分子量 303.36 Aldrich No.20,491−９ Ｙイオン半径:92pm 硝酸（II）鉛 分子量 331.20 Riedel de Haen No.311.37 Pbイオン半径:120pm 付録1e DTPAおよびEDTAによるMAbの阻害の定量的分析 固相抗原との結合の50％阻害を起こすコンペティター
の過剰モル
【図面の簡単な説明】
第１図および第３図は、重鎖遺伝子部分のポリペプチド
スペーサーによる結合構造を示す説明図である。 第２図および第４図は、それぞれ第１図および第３図の
ものに軽鎖が対合した構造を示す説明図である。 第５図〜第13図はＶH 1a ＣH 1−リンカーＶH 1b ＣH
1遺伝子構築物の構築を示す説明図である。 第14図〜第21図はMab−jun融合分子のためのプラスミド
Ｋの構築を示す説明図である。
───────────────────────────────────────────────────── フロントページの続き (51)Int.Cl.6 識別記号 ＦＩ // Ｃ１２Ｎ 5/10 Ｃ１２Ｎ 5/00 Ｂ (Ｃ１２Ｐ 21/08 Ｃ１２Ｒ 1:91） (72)発明者 ルートウィッヒ、クールマン ドイツ連邦共和国フレールシャイム、ア ム、マイン、ベルリナー シュトラー セ、57 (72)発明者 アレックス、シュタインシュトレーサー ドイツ連邦共和国リーデルバッハ、ツー ム、モルゲングラーベン、26

Claims (8)

    (57)【特許請求の範囲】
  1. 【請求項１】二つまたはそれ以上の異なる特異性の抗体
    のVHおよびCH1領域をコードするDNAの適当なリンカーに
    よる融合、およびそれらに属する軽鎖のための遺伝子部
    分と合わせての発現系における続いての発現による遺伝
    子操作によって得ることができる、二特異性またはオリ
    ゴ特異性の一価またはオリゴ価リセプターであって、一
    つの特異性がfos−jun相互作用を介して複合体に向けら
    れている、リセプター。
  2. 【請求項２】他の特異性が動物またはヒト腫瘍関連抗原
    に対して向けられている、請求項１に記載のリセプタ
    ー。
  3. 【請求項３】他の特異性が表２、３、４または５に示さ
    れる可変領域を有するモノクローナル抗体に由来する、
    請求項１または２に記載のリセプター。
  4. 【請求項４】三つの結合部位が二つの特異性の場合に存
    在する、請求項１〜３のいずれか１項に記載のリセプタ
    ー。
  5. 【請求項５】四つの結合部位が二つの特異性の場合に存
    在する、請求項１〜３のいずれか１項に記載のリセプタ
    ー。
  6. 【請求項６】三つの特異性の場合、一つが腫瘍に向けら
    れており、他の二つが異なるやり方でDTPAまたはEDTAに
    向けられている、請求項１〜５のいずれか１項に記載の
    リセプター。
  7. 【請求項７】重鎖抗体部分をコードするDNA断片を適当
    なリンカーを用いて連結して、軽鎖のための遺伝子とと
    もに発現系で発現することからなる、請求項１〜６のい
    ずれか１項に記載のリセプターの製造法。
  8. 【請求項８】請求項１〜６のいずれか１項に記載のリセ
    プターを含む腫瘍の治療のための医薬物であって、該リ
    セプターが二特異性であり、かつ一方の特異性が細胞膜
    上または間隙に位置している腫瘍関連抗原または腫瘍内
    皮のエピトープに向けられ、他方の特異性はキレートに
    関連する二特異性リセプターである、医薬物。
JP2165485A 1989-06-22 1990-06-22 二特異性およびオリゴ特異性の一価およびオリゴ価リセプター、それらの調整および使用 Expired - Lifetime JP2978210B2 (ja)

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DE59010480D1 (de) 1996-10-10
CA2019559C (en) 2002-01-08
IE902254L (en) 1990-12-22
KR910001057A (ko) 1991-01-30
US5591828A (en) 1997-01-07
KR0183980B1 (ko) 1999-04-01
ATE142230T1 (de) 1996-09-15
IE902254A1 (en) 1991-01-16
CA2019559A1 (en) 1990-12-22
EP0404097A2 (de) 1990-12-27
DK0404097T3 (ja) 1997-02-10
DE3920358A1 (de) 1991-01-17
EP0404097B1 (de) 1996-09-04
JPH0348699A (ja) 1991-03-01
ES2093623T3 (es) 1997-01-01
PT94443A (pt) 1991-02-08
AU5762190A (en) 1991-01-03
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RU2096459C1 (ru) 1997-11-20
IE76715B1 (en) 1997-10-22

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