JP5384338B2 - 単鎖Fcポリペプチド - Google Patents
単鎖Fcポリペプチド Download PDFInfo
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Description
驚くべきことに、本発明者らは現在、単鎖ポリペプチドとして機能的Fcドメインを作製することが可能であることを見出している。したがって本発明のポリペプチドは、多量に組換えにより作製することができ、任意の適切な手段により結合領域などのその他の分子に結合させることができるという利点を有する。さらに、抗体の定常領域は鎖内でFcドメインを形成するので、本発明のポリペプチドは二量体化しにくく、所望の場合には二価の結合領域を回避することができる。
−フェニルアラニン、チロシン及びトリプトファン(芳香族側鎖を有するアミノ酸);
−リシン、アルギニン及びヒスチジン(塩基性側鎖を有するアミノ酸);
−アスパラギン酸及びグルタミン酸(酸性側鎖を有するアミノ酸);
−アスパラギン及びグルタミン(アミド側鎖を有するアミノ酸);及び
−システイン及びメチオニン(硫黄を含む側鎖を有するアミノ酸)が含まれるが、これらに限定されない。
同一性と類似性の程度は、容易に算出することができる(Computational Molecular Biology、Lesk、A.M.編、Oxford University Press、New York、1988;Biocomputing.Informatics and Genome Projects、Smith,D.W.編、Academic Press、New York、1993;Computer Analysis of Sequence Data,Part 1,Griffin,A.M.と Griffin,H.G.編、Humana Press、New Jersey、1994;Sequence Analysis in Molecular Biology、von Heinje,G.、Academic Press、1987;及びSequence Analysis Primer、Gribskov,M.とDevereux,J.編、M Stockton Press、New York、1991)。一例では、変異体定常ドメインは、野生型定常ドメインと少なくとも60%同一であるか又は類似している。別の例では、変異体定常ドメインは、少なくとも70%同一であるか又は類似している。別の例では、変異体定常ドメインは、少なくとも80%同一であるか又は類似している。別の例では、変異体定常ドメインは、少なくとも90%同一であるか又は類似している。別の例では、変異体定常ドメインは、少なくとも95%同一であるか又は類似している。
N末端に、生物学的に活性な分子が抗体Fab断片である生物学的に活性な分子を含む、3つのマウスの単鎖Fcポリペプチドを設計した。Fab断片の可変領域は、細胞表面タンパク質抗原に結合するマウス抗体のMox46に由来した。Fcドメインは、マウスのIgG2aに由来し、これらのドメインの3つの異なるバージョンを以下に示す。リンカー配列には下線を付した。ヒンジ配列はイタリック体で示し、これらがリンカー配列の一部を構成する場合、ヒンジ配列はイタリック体で示し且つ下線を付した。
バージョン1 配列番号88(図2bに示した形式)。CH1とCH2間のヒンジのシステインが、セリンを置換している。
バージョン2 配列番号89(図2aに示した形式)
バージョン3 配列番号90(図1aに示した形式)。リンカーは、短縮したヒンジ’PCP’を含む。
抗原結合
抗原に結合する単鎖Fcポリペプチド(バージョン1及び3)の能力を、マウスIgG1骨格及び無関係なIgGで発現された同じ抗体可変領域(MOX46抗体由来の)と比較した。その表面上に抗原を発現する組換えNS0細胞(5×105)を、100μlの単鎖Fcポリペプチドと共に4℃で30分間インキュベートした。対照は、5μg/mlから下方へ1/3希釈で滴定したMOPC21であった。MOX46 IgG及び単鎖Fc構築物を、1/3希釈で滴定した。細胞を、5%のFCS及び0.1%アジ化ナトリウムを含むダルベッコ(Dulbecco)のPBSで2回洗浄し、次いで1/250希釈の抗マウスH鎖及びL鎖PE標識化(Jackson)抗体100μlを、4℃で30分間添加した。細胞を前述のように再度洗浄し、フローサイトメトリーによって分析した。
Fcレセプター結合
FcレセプターCD64(FcγRII)及びCD32(FcγRI)に結合する単鎖Fcバージョン1及び3の能力を、BIAcoreにより測定した。CD64及びCD32を、アミンカップリング化学により、標準的なCM5 Biacoreチップのフローセル2及び3(それぞれ)の上に固定(それぞれ約1000RU)した。フローセル1を、バックグラウンドの結合を調べるために参照フローセルとして設置した。次いで結合活性を探るため、単鎖Fcタンパク質を順番にチップ上に注入した。全てのサンプルは、原液、1:2希釈及び1:5希釈で流した。バックグラウンドの結合は、全てのサンプルでの有意でなかった。
組換えNS0細胞を用いる補体依存性細胞傷害アッセイ
単鎖Fcバージョン1及び3を、これらが結合した細胞で補体介在性細胞傷害を生じる能力に関して調べた。
活性化T細胞を用いる補体依存性細胞傷害アッセイ
(i)単鎖Fcバージョン1、2及び3を、その表面上でMOX46抗体により結合される抗原を発現する活性化T細胞の補体介在性細胞傷害を生じるこれら単鎖Fcバージョンの能力について試験した。使用した方法は、一次活性化T細胞をNS0細胞の代わりに使用した点を除けば、実施例4に記載したとおりであり、これらは実施例2に記載のように作製された。
実験条件におけるPI陽性細胞の% − PI陽性細胞のバックグラウンド%
PI陽性細胞の最大%(細胞溶解緩衝液) − PI陽性細胞のバックグラウンド%
受容体−scFc融合
ヒトgp130受容体ドメイン1を、図1aに示した単鎖Fc形式を用いて、単鎖Fc(マウスガンマ1)融合タンパク質としてクローニングした。融合タンパク質の配列を、以下に示す。
Claims (18)
- 2つのCH2ドメイン及び2つのCH3ドメインを含む単鎖Fcポリペプチドであって、該CH2及びCH3ドメインがポリペプチド鎖内で機能的Fcドメインを形成し、前記ポリペプチド鎖内で、第1のCH2ドメインが第2のCH2ドメインと二量体化され、第1のCH3ドメインが第2のCH3ドメインと二量体化されることを特徴とする単鎖ポリペプチド。
- N末端からC末端への配列において、第1のCH2ドメインが、そのC末端で第1のCH3ドメインのN末端と場合によってはリンカーを介して連結し、該第1のCH3ドメインが、そのC末端で第2のCH2ドメインのN末端とリンカーを介して連結し、該第2のCH2ドメインが、そのC末端で場合によってはリンカーを介して該第2のCH3ドメインのN末端と連結している、請求項1に記載のポリペプチド。
- N末端からC末端への配列において、第1のCH2ドメインが、そのC末端でリンカーを介して第2のCH2ドメインのN末端と連結し、該第2のCH2ドメインが、そのC末端で場合によってはリンカーを介して第1のCH3ドメインのN末端と連結し、該第1のCH3ドメインが、そのC末端でリンカーを介して第2のCH3ドメインのN末端と連結している、請求項1に記載のポリペプチド。
- 互いに二量体化される2つのCH4ドメインをさらに含む、請求項1に記載のポリペプチド。
- 配列番号8、配列番号9、配列番号10、配列番号11、配列番号12、配列番号13、配列番号21、配列番号22、配列番号23、配列番号24、配列番号25、配列番号26、配列番号34、配列番号35、配列番号36、配列番号37、配列番号38、配列番号39、配列番号47、配列番号48、配列番号49、配列番号50、配列番号51又は配列番号52に示す配列を含む、請求項1〜4までのいずれか一項に記載の単鎖Fcポリペプチド。
- 1つ又は複数の生物学的に活性な分子と連結している、請求項1〜5までのいずれか一項に記載の単鎖Fcポリペプチド。
- 前記生物学的に活性な分子が、抗体断片を含む、請求項6に記載の単鎖Fcポリペプチド。
- 前記抗体断片が、VHH、VH、VL、VH−CH1、VL−CL、Fab、Fab’又はscFvから選択される、請求項7に記載の単鎖Fcポリペプチド。
- 前記抗体断片がFabであり、前記FabのVH−CH1鎖のC末端が前記単鎖FcポリペプチドのN末端と遺伝子融合し、前記FabのVL−CL鎖がジスルフィド結合によって前記VH−CH1鎖と連結している、請求項8に記載の単鎖Fcポリペプチド。
- 前記生物学的に活性な分子が、ヒトgp130受容体の1つ若しくは複数のドメイン又はその断片を含む、請求項6に記載の単鎖Fcポリペプチド。
- 前記ヒトgp130受容体のドメイン1又はその断片を含む、請求項10に記載の単鎖Fcポリペプチド。
- 1つ又は複数のエフェクター分子が結合している、請求項1〜11までのいずれか一項に記載の単鎖Fcポリペプチド。
- 請求項1〜12までのいずれか一項に記載の単鎖Fcポリペプチドをコードする配列からなる、単離されたDNA分子。
- 請求項13に記載の1つ又は複数のDNA配列を含むクローニングベクター又は発現ベクター。
- 請求項14に記載の1つ若しくは複数のクローニングベクター又は発現ベクターを含む宿主細胞。
- 請求項1〜12までのいずれか一項に記載の前記単鎖Fcポリペプチドを産生する方法であって、請求項15に記載の宿主細胞を培養することと、前記単鎖Fcポリペプチドを分離することとを含む方法。
- 1つ又は複数の薬学的に許容し得る賦形剤、希釈剤又は担体と組み合わせて、請求項1〜12までのいずれか一項に記載の単鎖Fcポリペプチドを含む医薬組成物。
- 他の活性成分をさらに含む、請求項17に記載の医薬組成物。
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Application Number | Priority Date | Filing Date | Title |
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GB0614780.5 | 2006-07-25 | ||
GBGB0614780.5A GB0614780D0 (en) | 2006-07-25 | 2006-07-25 | Biological products |
PCT/GB2007/002842 WO2008012543A1 (en) | 2006-07-25 | 2007-07-24 | Single chain fc polypeptides |
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JP2009544300A JP2009544300A (ja) | 2009-12-17 |
JP5384338B2 true JP5384338B2 (ja) | 2014-01-08 |
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JP2009521344A Expired - Fee Related JP5384338B2 (ja) | 2006-07-25 | 2007-07-24 | 単鎖Fcポリペプチド |
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CA (1) | CA2658542C (ja) |
ES (2) | ES2564389T3 (ja) |
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ES2564389T3 (es) | 2016-03-22 |
CA2658542C (en) | 2017-10-31 |
EP2046832A1 (en) | 2009-04-15 |
CN104744587A (zh) | 2015-07-01 |
CN104744587B (zh) | 2019-01-11 |
GB0614780D0 (en) | 2006-09-06 |
CA2658542A1 (en) | 2008-01-31 |
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