JP2022176971A - IgE Fc受容体のアルファサブユニットの細胞外ドメイン、その物を含む医薬組成物、およびその物を製造する方法 - Google Patents
IgE Fc受容体のアルファサブユニットの細胞外ドメイン、その物を含む医薬組成物、およびその物を製造する方法 Download PDFInfo
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- polypeptide dimer
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Abstract
Description
Arg Asn Thr Gly Arg Gly Gly Glu Glu Lys Lys Xaa1 Xaa2 Lys Glu Lys Glu Glu Gln Glu Glu Arg Glu Thr Lys Thr Pro Glu Cys Pro(配列番号:17)(配列中、Xaa1はLysまたはGlyであってもよく、Xaa2はGlu、GlyまたはSerであってもよい)。具体的には、該ヒンジは配列番号:3または配列番号:19のアミノ酸配列を有してもよく、それによりタンパク質を産生する工程の間にて末端切断された形態の生成を最小限とする。
Ala Gln Pro Gln Ala Glu Gly Ser Leu Ala Lys Ala Thr Thr Ala Pro Ala Thr Thr Arg Asn Thr Gly Arg Gly Gly Glu Glu Lys Lys Xaa3 Xaa4 Lys Glu Lys Glu Glu Gln Glu Glu Arg Glu Thr Lys Thr Pro Glu Cys Pro(配列番号:18)(配列中、Xaa3はLysまたはGlyであってもよく、Xaa4はGlu、GlyまたはSerであってもよい)。具体的には、該ヒンジは配列番号:4のアミノ酸配列を有してもよく、それによりタンパク質を産生する工程の間にて末端切断された形態の生成を最小限とする。
もまた、医薬組成物に配合されてもよい。
次に、該形質転換細胞を培養する工程を行う。
ここで、該ポリペプチド二量体はシアル酸含有量が高く、かくして理論上のpI値と比べて酸性タンパク質の含有量が極めて高い。
IgE Fc受容体のアルファサブユニットの細胞外ドメイン(FcεRIα-ECD)のC-末端修飾ポリペプチドを、米国特許第7,867,491号に開示される方法に従って製造した。
上記した実施例1にて選択された細胞株の中で、i)FcεRIαECD-Fc3,ii)FcεRIαECD-Fc3ST、およびiii)FcεRIαECD-Fc2STをバッチ培養法により60mlのスケールで培養した。得られた培養物をタンパク質Aアフィニティカラムを用いて精製し、次に精製したタンパク質をSDS-PAGEおよびサイズ排除HPLC(SE-HPLC)に供し、そのタンパク質の純度を同定した。
IgEとの結合能を、上記した実施例2の方法を通して精製された、4種のタンパク質、i)FcεRIαECD-Fc2、ii)FcεRIαECD-Fc2ST、iii)FcεRIαECD-Fc3、およびiv)FcεRIαECD-Fc3ST、ならびに市販の抗IgE抗体であるオマリズマブ(商品名:ゾーレア)について比較して測定した。具体的には、IgEとの結合能は、タンパク質GLCセンサーチップ(Bio-Rad Laboratories, Inc.、カタログ番号176-5011)のチャンネルでIgEをコーティングし、オマリズマブまたは各FcεRIαECD-Fcタンパク質を種々の濃度にて30μl/分の速度で流れるようにすることにより測定された。
IgETRAPおよびオマリズマブのIgG受容体との結合度は、Octet RED384システム(ForteBio, CA, USA)を用いて同定された。FcγRI、 FcγRIIA、FcγRIIb、FcγRIIIA、およびFcγRIIIB組換えタンパク質(R & D Systems Inc.、5μg/ml)を300mMの酢酸緩衝液(pH5)中にて活性化AR2Gバイオセンサー上で固定した。ランニング緩衝液として、0.1%ツィーン20および1%ウシ血清を含有するPBSを用いた。すべての実験は、30℃でサンプルプレート振盪器を用いて1,000rpmの速度で実施された。結果を図5A~5Eに示し、オマリズマブおよびIgETRAPのIgG受容体との結合能を定量し、図6に示す。
ベータヘキソサミニダーゼアッセイを、本発明のFcεRIαECD融合タンパク質のインビトロでの活性分析について行った。具体的には、本発明の実施態様に係るFcεRIαECD-Fc2タンパク質を、各濃度で、マウスIgE(1μg/mL)と混合し、室温(20℃)で30分間インキュベートし、サンプルを調製した。脂肪細胞を活性化するための培養液中にあるマウス骨髄由来の脂肪細胞をハンクス平衡塩溶液(HBSS)の緩衝液で洗浄し、培地を除去し、細胞の数を測定した。次に、5x105個の細胞が40μLのHBSS緩衝液に注入されるように調整を行った。
β-ヘキソサミニダーゼアッセイを行い、インビトロ活性分析を介してゾレアと比較したFcεRIα ECD融合タンパク質の優位性を同定した。各薬物の、FcεRIαECD-Fc2ST(IgETRAP)およびゾレアを各濃度で製造し、次にヒトIgE(1μg/mL)と混合した。次に、インキュベーションを室温で30分間行った。薬物のプレインキュベーションの間に、ヒトFcεRI遺伝子を導入し、マウス骨髄から誘導され、分化した、マウスFcεRI遺伝子が除去された、脂肪細胞を調製した。調製した脂肪細胞をHBSS緩衝液で洗浄し、次に5x105細胞を60μLのHBSS緩衝液中に注入した。20μLのプレインキュベートしたサンプルを調製した脂肪細胞に添加し、ついで5%CO2インキュベーター中、37℃で30分間にわたってインキュベートした。
50μgのオマリズマブ(OVA)および1mgのアルム(alum)をBalb/cマウス(Orientbio Inc.)に14日間の間隔で2回腹腔内投与に付し、感作を誘発させた。その後で、50mgのOVAを第28日、30日、32日、34日および36日に合計で5回経口投与に付し、腸において食物アレルギーを誘発した。
Claims (19)
- 2つの単量体(その各々がIgE Fc受容体のアルファサブユニットの細胞外ドメイン(FcεRIa-ECD)を含有する)を含む、ポリペプチド二量体であって、
ここで、該単量体が修飾Fc領域を含有し、
該修飾Fc領域およびFcεRIa-ECDがヒンジを介して連結される、
ポリペプチド二量体。 - IgE Fc受容体のアルファサブユニットの細胞外ドメインが配列番号:1のアミノ酸配列またはそのフラグメントを有する、請求項1に記載のポリペプチド二量体。
- 修飾Fc領域が配列番号:2で示される、請求項1に記載のポリペプチド二量体。
- ヒンジがイムノグロブリンIgDより誘導されるヒンジ領域またはその変種である、請求項1に記載のポリペプチド二量体。
- イムノグロブリンIgDより誘導されるヒンジ領域またはその変種が少なくとも1個のシステインを含有する、請求項4に記載のポリペプチド二量体。
- イムノグロブリンIgDより誘導されるヒンジ領域またはその変種が
Arg Asn Thr Gly Arg Gly Gly Glu Glu Lys Lys Xaa1 Xaa2 Lys Glu Lys Glu Glu Gln Glu Glu Arg Glu Thr Lys Thr Pro Glu Cys Pro(配列番号:17)であり、
Xaa1がLysまたはGlyであって、
Xaa2がGlu、GlyまたはSerである、
請求項4に記載のポリペプチド二量体。 - イムノグロブリンIgDより誘導されるヒンジ領域またはその変種が
Ala Gln Pro Gln Ala Glu Gly Ser Leu Ala Lys Ala Thr Thr Ala Pro Ala Thr Thr Arg Asn Thr Gly Arg Gly Gly Glu Glu Lys Lys Xaa3 Xaa4 Lys Glu Lys Glu Glu Gln Glu Glu Arg Glu Thr Lys Thr Pro Glu Cys Pro(配列番号:18)であり、
Xaa1がLysまたはGlyであって、
Xaa2がGlu、GlyまたはSerである、
請求項4に記載のポリペプチド二量体。 - ヒンジが、配列番号:3、配列番号:4および配列番号:19からなる群より選択されるいずれか1つのアミノ酸配列を有する、請求項1に記載のポリペプチド二量体。
- IgE Fc受容体のアルファサブユニットの細胞外ドメイン(FcεRIa-ECD)を含有する、請求項1に記載の単量体をコードする、ポリヌクレオチド。
- 請求項9に記載のポリヌクレオチドでロードされる、発現ベクター。
- 請求項10に記載の発現ベクターが導入される、宿主細胞。
- 活性成分として、請求項1~8のいずれかに記載のポリペプチド二量体を含む、アレルギー疾患を治療または予防するための医薬組成物。
- アレルギー疾患が、食物アレルギー、アトピー性皮膚炎、喘息、アレルギー性鼻炎、アレルギー性結膜炎、アレルギー性皮膚炎、慢性特発性蕁麻疹、およびアレルギー性接触皮膚炎からなる群より選択されるいずれかの疾患である、請求項12に記載の医薬組成物。
- 活性成分として、請求項1~8のいずれかに記載のポリペプチド二量体を含む、アレルギー症状を改善または緩和するための食品組成物。
- 請求項9に記載のポリヌクレオチドおよびシアル酸トランスフェラーゼ遺伝子が導入される細胞を培養する工程;および
ポリペプチド二量体を回収する工程
を含む、ポリペプチド二量体を生成する方法。 - 請求項15にて得られるポリペプチド二量体。
- 活性成分として、請求項16に記載のポリペプチド二量体を含む、アレルギー疾患を治療または予防するための医薬組成物。
- 活性成分として、請求項16に記載のポリペプチド二量体を含む、アレルギー症状を改善または緩和するための食品組成物。
- 請求項1および/または請求項16に記載のポリペプチド二量体を対象に投与する工程を含む、アレルギー疾患を治療または予防するための方法。
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