JP6178349B2 - 抗pd−l1抗体およびt細胞機能を増強するためのそれらの使用 - Google Patents
抗pd−l1抗体およびt細胞機能を増強するためのそれらの使用 Download PDFInfo
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Description
本願は、2008年12月9日に出願された米国仮出願第61/121092号の35 USC 119(e)の下で優先権の利益を主張し、その開示が参照によりその全体が本明細書に組み入れられる。
本発明は、一般的に、免疫機能およびT細胞機能を増強すること(細胞媒介性免疫応答のアップレギュレーションを含む)およびT細胞機能障害性障害の処置に関する。
T細胞に対する同時刺激または2つの別々のシグナルの提供は、抗原提示細胞(APC)による休止Tリンパ球のリンパ球活性化の広く受け入れられたモデルである。Lafferty et al., Aust. J. Exp. Biol. Med. Sci. 53: 27-42 (1975)。このモデルは、さらに、非自己から自己の識別および免疫寛容を提供する。Bretscher et al., Science 169: 1042-1049 (1970); Bretscher, P. A., P. N. A. S. USA 96: 185-190 (1999); Jenkins et al., J. Exp. Med. 165: 302-319 (1987)。一次シグナル、または抗原特異的シグナルが、主要組織適合複合体(MHC)に関連して提示される外来抗原ペプチドの認識に続いてT細胞受容体(TCR)を通じて伝達される。二次または同時刺激シグナルが、抗原提示細胞(APC)上で発現される同時刺激分子によりT細胞に送達され、T細胞のクローン増殖、サイトカイン分泌物、およびエフェクター機能の促進を誘導する。Lenschow et al., Ann. Rev. Immunol. 14: 233 (1996)。同時刺激の非存在において、T細胞は抗原刺激に抵抗性になりうる、効果的な免疫応答を開始しない、さらに外来抗原に対する消耗または寛容を招きうる。
ネガティブの二次シグナルがT細胞寛容の誘導のために必要と思われ、一方ではポジティブのシグナルがT細胞活性化を促進する。簡単な2シグナルモデルが依然としてナイーブリンパ球についての妥当な説明を提供する一方で、宿主の免疫応答は動的なプロセスであり、同時刺激シグナルは抗原に暴露されたT細胞に対しても提供されうる。
本発明は、抗PD−L1抗体(そのような抗体をコードする核酸およびそのような抗体を含む組成物を含む)、および細胞媒介性免疫応答をアップレギュレーションするためにT細胞機能を増強させるためのそれらの使用およびT細胞機能障害性障害(感染(例、急性および慢性)および腫瘍免疫を含む)の処置を提供する。
(a)HVR−H1配列がGFTFSX1SWIH(配列番号1)であり;
(b)HVR−H2配列がAWIX2PYGGSX3YYADSVKG(配列番号2)であり;
(c)HVR−H3配列がRHWPGGFDY(配列番号3)であり;
さらに、それにおいて:X1がDまたはGであり;X2がSまたはLであり;X3がTまたはSである。1つの特定の局面において、X1がDであり;X2がSであり、およびX3がTである。別の局面において、ポリペプチドは、さらに、以下の式のHVRの間に並置された重鎖可変領域フレームワーク配列:(HC−FR1)−(HVR−H1)−(HC−FR2)−(HVR−H2)−(HC−FR3)−(HVR−H3)−(HC−FR4)を含む。さらに別の局面において、フレームワーク配列は、ヒトコンセンサスフレームワーク配列に由来する。さらなる局面において、フレームワーク配列は、VHサブグループIIIコンセンサスフレームワークである。さらなる局面において、フレームワーク配列の少なくとも1つは以下:
HC−FR1はEVQLVESGGGLVQPGGSLRLSCAAS(配列番号4)であり;
HC−FR2はWVRQAPGKGLEWV(配列番号5)であり;
HC−FR3はRFTISADTSKNTAYLQMNSLRAEDTAVYYCAR(配列番号6)であり;
HC−FR4はWGQGTLVTVSA(配列番号7)
である。
さらなる局面において、重鎖ポリペプチドは、さらに、HVR−L1、HVR−L2、およびHVR−L3を含む軽鎖可変領域と組み合わされ、それにおいて:
(a)HVR−L1配列はRASQX4X5X6TX7X8A(配列番号8)であり;
(b)HVR−L2配列はSASX9LX10S(配列番号9)であり;
(c)HVR−L3配列はQQX11X12X13X14PX15T(配列番号10)であり;
さらに、それにおいて:X4はDまたはVであり;X5はVまたはIであり;X6はSまたはNであり;X7はAまたはFであり;X8はVまたはLであり;X9はFまたはTであり;X10はYまたはAであり;X11はY、G、F,またはSであり;X12はL、Y、FまたはWであり;X13はY、N、A、T、G、FまたはIであり;X14はH、V、P、TまたはIであり;X15はA、W、R、PまたはTである。
さらなる局面において、X4はDであり;X5はVであり;X6はSであり;X7はAであり;X8はVであり;X9はFであり;X10はYであり;X11はYであり;X12はLであり;X13はYであり;X14はHであり;X15はAである。さらなる局面において、軽鎖は、さらに、以下の式のHVRの間に並置された軽鎖可変領域フレームワーク配列:(LC−FR1)−(HVR−L1)−(LC−FR2)−(HVR−L2)−(LC−FR3)−(HVR−L3)−(LC−FR4)を含む。さらなる局面において、フレームワーク配列は、ヒトコンセンサスフレームワーク配列に由来する。さらなる局面において、フレームワーク配列は、VLカッパIコンセンサスフレームワークである。さらなる局面において、フレームワーク配列の少なくとも1つは以下:
LC−FR1はDIQMTQSPSSLSASVGDRVTITC(配列番号11)であり;
LC−FR2はWYQQKPGKAPKLLIY(配列番号12)であり;
LC−FR3はGVPSRFSGSGSGTDFTLTISSLQPEDFATYYC(配列番号13)であり;
LC−FR4はFGQGTKVEIKR(配列番号14)
である。
(a)重鎖は、HVR−H1、HVR−H2、およびHVR−H3を含み、それにおいて、さらに:
(i)HVR−H1配列はGFTFSX1SWIH(配列番号1)であり;
(ii)HVR−H2配列はAWIX2PYGGSX3YYADSVKG(配列番号2)であり;
(iii)HVR−H3配列はRHWPGGFDY(配列番号3)であり;そして
(b)軽鎖はHVR−L1、HVR−L2、およびHVR−L3を含み、それにおいて、さらに:
(i)HVR−L1配列はRASQX4X5X6TX7X8A(配列番号8)であり;
(ii)HVR−L2配列はSASX9LX10S(配列番号9)であり;および
(iii)HVR−L3配列はQQX11X12X13X14PX15T(配列番号10)である。
HC−FR1 EVQLVESGGGLVQPGGSLRLSCAAS(配列番号4)
HC−FR2 WVRQAPGKGLEWV(配列番号5)
HC−FR3 RFTISADTSKNTAYLQMNSLRAEDTAVYYCAR(配列番号6)
HC−FR4 WGQGTLVTVSA(配列番号7)
である。
LC−FR1 DIQMTQSPSSLSASVGDRVTITC(配列番号11)
LC−FR2 WYQQKPGKAPKLLIY(配列番号12)
LC−FR3 GVPSRFSGSGSGTDFTLTISSLQPEDFATYYC(配列番号13)
LC−FR4 FGQGTKVEIKR(配列番号14)
である。
(a)重鎖は、さらに、GFTFSDSWIH(配列番号15)、AWISPYGGSTYYADSVKG(配列番号16)、およびRHWPGGFDY(配列番号3)と少なくとも85%の配列同一性をそれぞれ有するHVR−H1、HVR−H2、およびHVR−H3配列を含み、または
(b)軽鎖は、さらに、RASQDVSTAVA(配列番号17)、SASFLYS(配列番号18)、およびQQYLYHPAT(配列番号19)と少なくとも85%の配列同一性をそれぞれ有するHVR−L1、HVR−L2、およびHVR−L3配列を含む。
HC−FR1 EVQLVESGGGLVQPGGSLRLSCAAS(配列番号4)
HC−FR2 WVRQAPGKGLEWV(配列番号5)
HC−FR3 RFTISADTSKNTAYLQMNSLRAEDTAVYYCAR(配列番号6)
HC−FR4 WGQGTLVTVSA(配列番号7)
である。
LC−FR1 DIQMTQSPSSLSASVGDRVTITC(配列番号11)
LC−FR2 WYQQKPGKAPKLLIY(配列番号12)
LC−FR3 GVPSRFSGSGSGTDFTLTISSLQPEDFATYYC(配列番号13)
LC−FR4 FGQGTKVEIKR(配列番号14)
である。
(a)重鎖は、以下:
EVQLVESGGGLVQPGGSLRLSCAASGFTFSDSWIHWVRQAPGKGLEWVAWISPYGGSTYYADSVKGRFTISADTSKNTAYLQMNSLRAEDTAVYYCARRHWPGGFDYWGQGTLVTVSA(配列番号20)の重鎖配列と少なくとも85%の配列同一性を有し、または
(b)軽鎖は、以下:
DIQMTQSPSSLSASVGDRVTITCRASQDVSTAVAWYQQKPGKAPKLLIYSASFLYSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQYLYHPATFGQGTKVEIKR(配列番号21)
の軽鎖配列と少なくとも85%の配列同一性を有する。
HC−FR1 EVQLVESGGGLVQPGGSLRLSCAAS(配列番号4)
HC−FR2 WVRQAPGKGLEWV(配列番号5)
HC−FR3 RFTISADTSKNTAYLQMNSLRAEDTAVYYCAR(配列番号6)
HC−FR4 WGQGTLVTVSA(配列番号7)
である。
LC−FR1 DIQMTQSPSSLSASVGDRVTITC(配列番号11)
LC−FR2 WYQQKPGKAPKLLIY(配列番号12)
LC−FR3 GVPSRFSGSGSGTDFTLTISSLQPEDFATYYC(配列番号13)
LC−FR4 FGQGTKVEIKR(配列番号14)
である。
(a)重鎖は、さらに、GFTFSDSWIH(配列番号15)、AWISPYGGSTYYADSVKG(配列番号16)、およびRHWPGGFDY(配列番号3)と少なくとも85%の配列同一性をそれぞれ有するHVR−H1、HVR−H2、およびHVR−H3配列を含み、そして
(b)軽鎖は、さらに、RASQDVSTAVA(配列番号17)、SASFLYS(配列番号18)、およびQQYLYHPAT(配列番号19)と少なくとも85%の配列同一性をそれぞれ有するHVR−L1、HVR−L2、およびHVR−L3配列を含む。
HC−FR1 EVQLVESGGGLVQPGGSLRLSCAAS(配列番号4)
HC−FR2 WVRQAPGKGLEWV(配列番号5)
HC−FR3 RFTISADTSKNTAYLQMNSLRAEDTAVYYCAR(配列番号6)
HC−FR4 WGQGTLVTVSA(配列番号7)
である。
LC−FR1 DIQMTQSPSSLSASVGDRVTITC(配列番号11)
LC−FR2 WYQQKPGKAPKLLIY(配列番号12)
LC−FR3 GVPSRFSGSGSGTDFTLTISSLQPEDFATYYC(配列番号13)
LC−FR4 FGQGTKVEIKR(配列番号14)
である。
本明細書で言及した全ての参考文献が、参照により具体的に組み入れられる。
本発明の実行は、特記なき場合、当技術分野の技能の範囲内にある分子生物学(組換え技術を含む)、微生物学、細胞生物学、生化学、および免疫学の従来の技術を用いる。そのような技術は文献において十分に説明される。例えば、Molecular Cloning: A Laboratory Manual, second edition (Sambrook et al., 1989); Oligonucleotide Synthesis (M.J. Gait, ed., 1984); Animal Cell Culture (R.I. Freshney, ed., 1987); Methods in Enzymology (Academic Press, Inc.); Current Protocols in Molecular Biology (F.M. Ausubel et al., eds 1987, and periodic updates); PCR: The Polymerase Chain Reaction, (Mullis et al., ed., 1994); A Practical Guide to Molecular Cloning (Perbal Bernard V., 1988); Phage Display: A Laboratory Manual (Barbas et al., 2001)。
A.リンパ球の発生および活性化
ヒトにおける2つの主な型のリンパ球はT(胸腺由来)およびB(骨髄由来)である。これらの細胞は、リンパ系発生経路にコミットした骨髄および胎児肝臓中の造血幹細胞に由来する。これらの幹細胞の子孫は、BまたはTリンパ球中に成熟する多岐にわたる経路に従う。ヒトBリンパ球の発生は、完全に骨髄内で起こる。T細胞は、他方で、骨髄を離れ、血流を通じて胸腺まで移動する未成熟な前駆体から発生し、そこで、それらは、増殖し、成熟Tリンパ球に分化する。
Tリンパ球は免疫グロブリンを発現せず、しかし、代わりに、T細胞受容体(TCR)と呼ばれる表面タンパク質により外来物質の存在を検出する。これらの受容体は、直接的な接触によりまたは他の免疫細胞の活性に影響を与えることを通じて抗原を認識する。マクロファージと一緒に、T細胞は細胞媒介性免疫に関与する一次細胞型である。
他の身体の防御から区別される哺乳動物の免疫系の3つの一次機能特性は、以下:(1)特異性 − 大多数の標的分子の間で個別に認識するおよび応答するまたは応答しない能力、(2)識別 − 非自己から自己を決定するための能力(全ての無数のタンパク質および他の有機物質と穏やかに共存し、依然として身体に導入される外来物質に対してウイルス学的に応答するようにする)、および(3)記憶 − 経験により形成される能力(特定の外来病原体との後の遭遇が、最初の遭遇で生じたよりも迅速で活発な応答を惹起する)を含む。これらの機能の1つまたは複数が失敗している場合、病理学的状態がもたらされる。
1.B7.1/B7.2 − CD28/CTLA−4
恐らく、最も良く特徴付けられているT細胞同時刺激経路は、B7.1(CD80)/B7.2(CD86) − CD28/CTLA−4(CD152)を通じてシグナル伝達する経路である。このシグナル伝達経路はT細胞の活性化および寛容に決定的である。Karandikar et al., J. Neuroimmunol. 89: 10-18 (1998); Oosterwegal et al., Curr. Opin. Immunol. 11: 294-300 (1999); Salomon et al., Annu. Rev. Immunol. 19: 225-252 (2001); Sansom, D. M., Immunol. 101: 169-177 (2000); Chambers et al., Annu. Rev. Immunol. 19: 565-592 (2001)。
APCとT細胞の間での相互作用の別の経路は、ICOS(CD278)およびICOSL(B7−H2、CD275)を通じて生じる。ICOS/ICOSLシグナル伝達は、Tヘルパー細胞分化およびエフェクター機能を促進し、特にインターロイキン10(IL−10)産生のために重要であるが、しかし、T細胞増殖およびIL−2産生(調節性T細胞を含む)、T細胞寛容、および自己免疫を調節する際により適度な役割を果たす。
T細胞活性化を調節する重要なネガティブ同時刺激シグナルが、プログラム死1受容体(PD−1)(CD279)、ならびにそのリガンド結合パートナーPD−L1(B7−H1、CD274)およびPD−L2(B7−DC、CD273)により提供さる。PD−1のネガティブな調節的役割が、PD−1ノックアウト(Pdcd1−/−)により明らかにされ、それは自己免疫の傾向がある。Nishimura et al., Immunity 11: 141-51 (1999); Nishimura et al., Science 291: 319-22 (2001)。PD−1はCD28およびCTLA−4に関連するが、しかし、ホモ二量体化を可能にする膜近位システインを欠く。PD−1の細胞質ドメインは、免疫受容体チロシンベースの阻害モチーフ(ITIM、V/IxYxxL/V)を含む。PD−1はPD−L1およびPD−L2だけに結合する。Freeman et al., J. Exp. Med. 192: 1-9 (2000); Dong et al., Nature Med. 5: 1365-1369 (1999); Latchman et al., Nature Immunol. 2: 261-268 (2001); Tseng et al., J. Exp. Med. 193: 839-846 (2001)。
同時刺激シグナルは、また、B7−H3(B7RP−2、CD276、PRO352)を通じて提供され、それは広くリンパ系および非リンパ系組織において発現される。Chapoval et al., Nat. Immunol. 2: 269-74 (2001)。ヒトにおいて、B7−H3は4Igおよび2Igバリアントの両方を有し、4Ig形態が優勢であり、2Igバリアントがマウスにおいて優勢である。Sun et al., J. Immunol. 168: 6294-97 (2002); Steinberger et al., J. Immunol. 172: 2352-59 (2004); Ling et al., Genomics 82: 365-77 (2003)。
B7ファミリーへの最も最近の追加はB7−H4(B7x、B7−S1、B7−H.5、VTCN1、PRO1291)であり、それはT細胞応答のネガティブレギュレーターである。Zang et al., Proc. Natl. Acad. Sci. U.S.A. 100 (18), 10388-10392 (2003); Watanabe et al., Nat. Immunol. 4 (7), 670-679 (2003); Prasad, et al., Immunity 18(6), 863-873 (2003); Sica et al., Immunity 18 (6), 849-861 (2003)。ヒトおよびマウスの両方のB7−H4が、リンパ系器官(脾臓および胸腺)および非リンパ系器官(肺、肝臓、精巣、卵巣、胎盤、骨格筋、膵臓、および小腸を含む)において広く発現される。B7−H4は、正常ヒト組織において、IHCまたはB7−H4の翻訳レベルでの調節により検出されない。IHCでは、B7−H4が肺および卵巣の腫瘍において高度に発現されることが示され、リアルタイムポリメラーゼ連鎖反応(PCR)分析では、マウスB7−H4が前立腺、肺、および結腸の癌細胞株においても高度に発現されることが示される。B7−H4は、活性化T細胞(しかし、ナイーブT細胞ではない)上の未知の受容体に結合し、それはCTLA−4、ICOS、PD−1、およびB7−H3についての受容体とは別々である。BTLAがB7−H4についてのリガンドであると最初に報告されたが、野生型細胞(しかし、BTLA−/−細胞ではない)へのB7−H4/Ig融合物の報告された結合によって、HVEM(BTLAではない)がB7−H4についての固有のリガンドであるという結論に説得力がある。Sedy et al., Nat. Immunol. 6: 90-98 (2004)。
B7ファミリーメンバーBTLA(CD272、BTLA−1)は、PD−1およびCTLAと機能的に類似している。Th1細胞用の選択マーカーとして最初に同定され、BTLAはリンパ球だけで発現される。CTLA−4、ICOS、およびPD−1と同様に、BTLAは活性化の間にT細胞上で誘導される。しかし、ICOS(Th2細胞では上昇したままであるが、しかし、Th1細胞ではダウンレギュレーションされる)とは対照的に、BTLAはTh1細胞(しかし、Th2細胞ではない)では発現されたままである。PD−1と同様に、BTLAは、B細胞上でも発現される。Gavrieli et al., Biochem. Biophys. Res. Commun. 312: 1236-43 (2003)。しかし、BTLAは休止中のB細胞および活性化B細胞の両方で発現されるのに対し、PD−1は活性化B細胞でアップレギュレーションされる。BTLAは2つのITIMモチーフを有する。
1.OX40/OX40L(CD134)
OX40(CD134、TXPG1L、TNFRSF4)およびOX40L(CD134L、CD252、GP34、TNFSF4、TXGP1)欠損マウスは、ウイルス抗原および一般的なタンパク質抗原の両方に対しておよび接触過敏反応において低下した一次CD4+T細胞応答を有する。Chen et al., Immunity 11: 689-698 (1999); Kopf et al., Immunity 11: 699-708 (1999); Murata et al., J. Exp. Med. 191: 365-374 (2000); Gramaglia et al., J. Immunol. 165: 3043-3050 (2000)。より低い頻度の抗原特異的エフェクターT細胞が、一次応答における後期に生成され、より少ない記憶T細胞が発生する。Gramaglia et al., supra。CD27を欠損したT細胞とは対照的に、初期増殖は、OX40を欠損したナイーブCD4+T細胞集団において損なわれていない。しかし、低下した増殖および顕著なアポトーシス細胞死が活性化後4−5日目に生じ、結果としてわずかなT細胞しか長期間生存しない。Rogers et al., Immunity 15: 445-455 (2001)。OX40欠損CD8+T細胞を用いて、最初の細胞分裂は影響されず、しかし、一次エフェクター細胞の蓄積が抗原との遭遇後3−6日目に顕著に低下する。Croft et al., Nat. Immunol. 3: 609-620 (2003)。
OX40/OX40Lと同様に、4−1BB(CD137、TNFRSF9)および4−1BBL(TNFSF9)を欠くT細胞では、より少ない抗原反応性CD8+T細胞が、4−1BBLが存在しない場合に一次応答において蓄積し、より少ない記憶T細胞が発生することが示される。DeBenedette et al., J. Immunol. 163: 4833-4841 (1999); Tan et al., J. Immunol. 163: 4859-4868 (1999); Tan et al., J. Immunol. 164: 2320-2325 (2000)。また、4−1BBLを遮断することによって、CD8+T細胞の最初の増殖性応答は変化しないが、しかし、数回に分割された細胞のアポトーシスのため、3−6日後の一次応答のピークでエフェクターCTLの蓄積が抑制される。Cooper et al., Eur. J. Immunol. 32: 521-529 (2002)。アゴニスト抗4−1BB抗体および抗4−1BBL−トランスフェクトAPCも同様の結果を産生している:CTLおよびCD4+T細胞応答がin vivoで顕著に増加される。Melero et al., Nature Med. 3: 682-685 (1997); Melero et al., Eur. J. Immunol. 28: 1116-1121 (1998); Takahashi et al., J. Immunol. 162: 5037-5040 (1999); Guinn et al., J. Immunol. 162: 5003-5010 (1999); Halstead et al., Nature Immunol. 3: 536-541 (2002); Takahashi et al., Immunol. Lett. 76: 183-191 (2001); Bansal-Pakala et al., J. Immunol. 169: 5005-5009 (2002)。4−1BB−特異的抗体は最初の増殖性応答を変化させず、4−1BBL遮断実験からの結論を支持し、細胞−生存シグナルを供給する際での4−1BBの後期活性を指し示す。
T細胞応答の最初の段階におけるCD27(TNFRSF7、S152)およびCD27L(CD70、TNFSF7)シグナル伝達の重要性がin vitroでの遮断試験において実証されており、それにおいてCD27/CD70相互作用が破壊された。Oshima et al., Int. Immunol. 10: 517-526 (1998); Agematsu et al., J. Immunol. 153: 1421-1429 (1994); Hintzen et al., J. Immunol. 154: 2612-2623 (1995)。CD27を欠くT細胞は最初は正常に分裂するが、しかし、次に、活性化後3日目またはそれ以降に不良に増殖する。Hendriks et al., Nature Immunol. 1: 433-440 (2000)。これは、CD27が、T細胞死の早期抑制によりまたは細胞周期に作用することにより、ナイーブT細胞集団の最初の増殖の促進に関与し、活性化後2〜3日間持続的な分裂を可能にすることを示す。これはCD27欠損マウスでのin vivo試験により裏付けられ、それにおいて、より低い数の抗原特異的応答(4〜8日目)およびより少ない記憶T細胞が3週間またはそれ以上にわたり発生する。Hendriks et al., supra。CD27の発現は、T細胞活性化後、早期にアップレギュレーションされ、それが、エフェクター応答のピーク前に、早期増殖を保持するシグナルを主に送達することを示唆する。
CD30(TNFRSF8、Ki−1)およびCD30L(CD153、TNFSF8)シグナル伝達は、in vitroでのいくつかのT細胞機能について同時刺激的である。Del Prete et al., J. Exp. Med. 182: 1655-1661 (1995), Bowen et al., J. Immunol. 156: 442-449 (1995)。CD30Lに対する遮断試薬は、Th2細胞の発生を抑制し、in vitroでTh1細胞の発生を増強した。この活性は、CD30がTh2細胞および2型細胞傷害性Tc2細胞により優先的に発現されることを示すデータと一致する。Del Prete et al., supra, Nakamura et al., J. Immunol. 158: 2090-2098 (1996)。CD30は、非極性化された一次応答においてナイーブT細胞の活性化後3〜4日目に発現される。Nakamura et al., supra(その役割が2型サイトカイン支配的応答に制限されないことを示す)。
T細胞同時刺激に対するHVEM(HVEA、ATAR、LIGHTR、TNFRSF14、PRO509)およびLIGHT(CD258、HVEML、TR2、TNFSF14、PRO726)の効果は、1)LIGHTがリンホトキシンβ受容体(LTβR)にも結合する能力および2)HVEMが可溶性LTα3に結合する能力により複雑化される。このように、HVEM/LIGHTの効果の任意の試験では、また、このシグナル伝達系についての他の結合パートナーの効果を考慮に入れるべきである。LIGHTの遮断によって、同種混合リンパ球反応(MLR)において早期T細胞増殖およびサイトカイン分泌を阻害することができる。Tamada et al., J. Immunol. 164: 4105-4110 (2000), Kwon et al., J. Biol. Chem. 272: 14272-14276 (1997); Harrop et al., J. Immunol. 161: 1786-1794 (1998); Tamada et al., Nature Med. 6: 283-289 (2000)。炎症性サイトカインの産生は、LIGHTがMHC不適合心臓同種移植片において遮断される場合に抑制される。Ye et al., J. Exp. Med. 195: 795-800 (2002)。さらに、同種皮膚移植片が、LIGHTおよびCD28の両方を欠損するレシピエントにおいて遅延した動態で拒絶される。Scheu et al., J. Exp. Med. 195: 1613-1624 (2002)。遅延された移植片拒絶がT細胞クローン増殖またはサイトカイン産生の早期抑制を示しうるとの示唆。この結論は、(i)同種抗原に応答するLIGHT欠損脾細胞が、TH1およびTH2の両方のサイトカインの低下した産生ならびに細胞傷害性Tリンパ球活性(CTL)活性の弱い生成を有することを示すin vitro試験[Sheu et al., supra.]ならびに(ii)LIGHTの遮断がアロ反応性CTLの生成を低下させることを示すin vivo試験により裏付けられる。Tamada et al., Nature Med. 6: 283-289 (2000)。
「アレルゲン」または「免疫原」は、免疫応答を誘発することができる任意の分子である。本明細書で使用する通り、この用語は、抗原分子自体、またはその供給源(例えば花粉粒、動物のフケ、昆虫毒、または食物産物など)のいずれかを対象とする。これは抗原という、免疫グロブリンまたはT細胞受容体により特異的に認識されることができる分子を指す用語と対比される。免疫応答を誘導することが可能である任意の外来物質が、潜在的なアレルゲンである。天然および合成由来の多くの異なる化学物質が、アレルゲン性であることが公知である。複雑な天然有機化学物質、特にタンパク質が、抗体媒介性アレルギーを起こす可能性が高いのに対し、単純な有機化合物、無機化学物質、および金属はT細胞媒介性アレルギーをより優先的に起こす。一部の場合において、同じアレルゲンは1を上回る型のアレルギーに関与しうる。アレルゲンへの暴露は、吸入、注射、注射、または皮膚接触を通じうる。
siRNAは、上昇したインターフェロン合成、非特異的タンパク質合成阻害、およびRNA分解(哺乳動物細胞においてRNAiの使用に関連する細胞の自殺または死をしばしばもたらす)により特徴付けられる抗ウイルス応答を特異的に回避するよう設計される。Paddison et al., Proc Natl Acad Sci USA 99(3):1443-8.(2002)。
ループ Kabat AbM Chothia 接触
---- ----- --- ------- -------
L1 L24-L34 L24-L34 L26-L32 L30-L36
L2 L50-L56 L50-L56 L50-L52 L46-L55
L3 L89-L97 L89-L97 L91-L96 L89-L96
H1 H31-H35B H26-H35B H26-H32 H30-H35B
(Kabatナンバリング)
H1 H31-H35 H26-H35 H26-H32 H30-H35
(Chothiaナンバリング)
H2 H50-H65 H50-H58 H53-H55 H47-H58
H3 H95-H102 H95-H102 H96-H101 H93-H101
100×分数X/Y
(式中、Xは、AおよびBのそのプログラムのアラインメントにおける配列アラインメントプログラムALIGN−2による同一のマッチとしてスコア化されるアミノ酸残基の数であり、式中、YはBにおけるアミノ酸残基の総数である)の通りに算出する。アミノ酸配列Aの長さがアミノ酸配列Bの長さとは等しくない場合、AのBに対する%アミノ酸配列同一性は、BのAに対する%アミノ酸配列同一性とは等しくないと理解されるであろう。
特に腫瘍免疫の処置において、本発明の抗PD−L1抗体との組み合わせで有用な特に好ましい化学療法剤は、ゲムシタビンである。
A.ファージディスプレイを使用したヒト化
本明細書に記載する超可変領域を移植したバリアントは、各超可変領域について別々のオリゴヌクレオチドを使用して、ヒト受容体配列をコードする核酸のKunkel突然変異誘発により生成した。Kunkel et al., Methods Enzymol. 154: 367-382 (1987).適切な変化を、通常の技術を使用してフレームワークおよび/または超可変領域中に導入し、適した超可変領域−抗原相互作用を補正および再確立することができる。
本発明は、また、抗PD−L1抗体をコードする単離核酸、そのような核酸を含むベクターおよび宿主細胞、ならびに抗体の産生のための組換え技術を提供する。
a)ベクター構築
本発明の抗体のポリペプチド成分をコードするポリヌクレオチド配列を、標準的な組換え技術を使用して得ることができる。所望のポリヌクレオチド配列を、抗体産生細胞(例えばハイブリドーマ細胞など)から単離し、配列決定してもよい。あるいは、ポリヌクレオチドをヌクレオチドシンセサイザーまたはPCR技術を使用して合成することができる。一旦得られると、ポリペプチドをコードする配列を、原核生物宿主において異種ポリヌクレオチドを複製および発現することが可能な組換えベクター中に挿入する。当技術分野において利用可能で公知の多くのベクターを、本発明の目的のために使用することができる。適切なベクターの選択は、ベクター中に挿入される核酸のサイズおよびそのベクターを用いて形質転換される特定の宿主細胞に主に依存するであろう。各ベクターは、その機能(異種ポリヌクレオチドの増幅または発現、あるいは両方)およびそれが存在する特定の宿主細胞とのその適合性に依存して、種々の成分を含む。ベクター成分は、一般的に、限定はされないが、以下:複製起点、選択マーカー遺伝子、プロモーター、リボゾーム結合部位(RBS)、シグナル配列、異種核酸インサート、および転写終結配列を含む。
本発明の抗体を発現させるために適した原核生物宿主細胞は、古細菌と真正細菌、例えばグラム陰性またはグラム陽性生物などを含む。有用な細菌の例は、エシェリキア属(例、E.coli)、バシラス属(例、B. subtilis)、腸内細菌、シュードモナス属(例、P. aeruginosa)、サルモネラ・チフィリウム(Salmonella typhimurium)、セラチア・マルセッセンス(Serratia marcescans)、クレブシエラ属、プロテウス属、シゲラ属、根粒菌、ビトレオシラ属、またはパラコッカス属を含む。一実施態様において、グラム陰性細胞を使用する。一実施態様において、E.coli細胞を本発明のための宿主として使用する。E.coli株の例は、W3110株(Bachmann, Cellular and Molecular Biology, vol. 2 (Washington, D.C.: American Society for Microbiology, 1987), pp.1190-1219; ATCC Deposit No. 27,325)およびその派生体を含み、遺伝子型W3110 yfhuA (ytonA) ptr3 lac Iq lacL8 yompTy(nmpc−fepE) degP41 kanR(米国特許第5,639,635号)を有する33D3株を含む。他の株およびその派生体、例えばE.coli 294(ATCC 31,446)、E.coli B、E.coli 1776(ATCC 31,537)およびE.coli RV308(ATCC 31,608)なども適する。これらの例は、限定的よりも、むしろ説明的である。定義された遺伝子型を有する上記の最近のいずれかの派生体を構築するための方法が、当技術分野において公知であり、例えば、Bass et al., Proteins, 8:309-314 (1990)に記載される。一般的に、細菌の細胞におけるレプリコンの複製能を考慮に入れて適切な細菌を選択することが必要である。例えば、E.coli、セラチア属、またはサルモネラ属が、周知のプラスミド(例えばpBR322、pBR325、pACYC177、またはpKN410など)を、レプリコンを供給するために使用する場合、宿主として使用するのに適しうる。
宿主細胞を上記の発現ベクターを用いて形質転換し、プロモーターを誘導し、形質転換体を選択し、または所望の配列をコードする遺伝子を増幅するために適宜改変された従来の栄養培地中で培養する。形質転換はDNAを原核生物宿主中に導入し、DNAが、染色体外エレメントとしてまたは染色体組み込み体のいずれかとして複製可能であることを意味する。使用する宿主細胞に依存して、形質転換は、そのような細胞に適切である標準的な技術を使用して行う。塩化カルシウムを用いたカルシウム処理は、実質的な細胞壁バリアを含む細菌細胞のために一般的に使用される。形質転換のための別の方法ではポリエチレングリコール/DMSOを用いる。使用されるさらに別の技術は、エレクトロポレーションである。
本明細書において産生される抗体タンパク質をさらに精製し、さらなるアッセイおよび使用のための実質的に均質である調製物を得る。当技術分野において公知の標準的なタンパク質精製方法を用いることができる。以下の手順:免疫親和性カラムまたはイオン交換カラム上での分画、エタノール沈殿、逆相HPLC、シリカ上または陽イオン交換樹脂(例えばDEAEなど)上でのクロマトグラフィー、クロマトフォーカシング、SDS−PAGE、硫安塩析、およびゲルろ過(例えば、Sephadex G-75を使用)は、適した精製手順の例示である。
真核生物での発現のために、ベクター成分は、一般的に、限定はされないが、以下:シグナル配列、複製起点、1つまたは複数のマーカー遺伝子、ならびにエンハンサーエレメント、プロモーター、および転写終結配列の1つまたは複数を含む。
真核生物宿主における使用のためのベクターは、また、成熟タンパク質またはポリペプチドのN末端に特定の切断部位を有するシグナル配列または他のポリペプチドをコードするインサートを含んでもよい。選択される異種シグナル配列は、宿主細胞により認識され、プロセシングされる(即ち、シグナルペプチダーゼにより切断される)ものである。哺乳動物細胞での発現において、哺乳動物シグナル配列ならびにウイルス分泌リーダー、例えば、単純ヘルペスgDシグナルを利用可能である。
一般的に、複製起点成分は、哺乳動物発現ベクターのために必要とされない(SV40起点を典型的に使用してもよい。なぜなら、ただ、それは初期プロモーターを含むからである)。
発現ベクターおよびクローニングベクターは、選択遺伝子(選択可能マーカーとも呼ばれる)を含んでもよい。典型的な選択遺伝子は、(a)抗生物質または他の毒素(アンピシリン、ネオマイシン、メトトレキサート、またはテトラサイクリン)に対して耐性を付与する、(b)栄養要求性欠損を補完する、または(c)複雑な培地から利用可能ではない決定的な栄養分を供給するタンパク質をコードする(例、バシラス属についてのDアラニンラセマーゼをコードする遺伝子)。
発現ベクターおよびクローニングベクターは、通常、宿主生物により認識され、所望の抗体配列をコードする核酸に機能的に連結されたプロモーターを含む。事実上、全ての真核生物遺伝子が、転写が開始される部位から約25〜30塩基上流に位置付けられるATリッチ領域を有する。多くの遺伝子の転写の開始から70〜80塩基上流に見出される別の配列は、CNCAAT領域であり、そこでNは任意のヌクレオチドでありうる。大半の真核生物の3’末端は、AATAAA配列であり、それはコード配列の3’末端へのポリAテールの付加のためのシグナルでありうる。これらの配列の全てを、真核生物発現ベクター中に挿入してもよい。
より高い真核生物による本発明の抗体をコードするDNAの転写は、しばしば、ベクター中にエンハンサー配列を挿入することにより増加される。多くのエンハンサー配列が、現在、哺乳動物遺伝子から公知である(グロビン、エラスターゼ、アルブミン、α−フェトプロテイン、およびインスリン)。典型的に、しかし、真核細胞ウイルスからのエンハンサーが使用されうる。例は、複製開始点の後期側のSV40エンハンサー(bp 100−270)、サイトメガロウイルス初期プロモーターエンハンサー、複製開始点の後期側のポリオーマエンハンサー、およびアデノウイルスエンハンサーを含む。また、真核生物プロモーターの活性化のための増強エレメントに関するYaniv, Nature 297: 17-18 (1982)を参照のこと。エンハンサーは、抗体コード配列に対する位置5’または3’でベクター中にスプライシングされうるが、しかし、好ましくはプロモーターから部位5’に位置付けられる。
真核生物宿主細胞(酵母、真菌、昆虫、植物、動物、ヒト、または他の多細胞生物からの有核細胞)において使用される発現ベクターは、また、転写の終結のためにおよびmRNAを安定化させるために必要な配列を含みうる。そのような配列は、一般に、真核生物またはウイルスのDNAまたはcDNAの5’および、時には3’の非翻訳領域から利用可能である。これらの領域は、、抗体をコードするmRNAの非翻訳部分におけるポリアデニル化フラグメントとして転写されるヌクレオチドセグメントを含む。1つの有用な転写終結成分は、ウシ成長ホルモンポリアデニル化領域である。WO94/11026およびその中で開示される発現ベクターを参照のこと。
本明細書におけるベクター中でDNAをクローン化または発現するための適した宿主細胞は、本明細書に記載するより高い真核細胞(脊椎動物宿主細胞を含む)を含む。培養(組織培養)における脊椎動物細胞の増殖は、通常の手順になっている。有用な哺乳動物宿主細胞株の例は、以下:SV40により形質転換されたサル腎臓CV1株(COS−7, ATCC CRL 1651);ヒト胚腎臓株(293細胞または浮遊培養中での増殖のためにサブクローン化された293細胞、Graham et al., J. Gen Virol. 36: 59 (1977));仔ハムスター腎細胞(BHK, ATCC CCL 10);チャイニーズハムスター卵巣細胞/−DHFR(CHO, Urlaub et al., Proc. Natl. Acad. Sci. USA 77: 4216 (1980));マウスセルトリ細胞(TM4, Mather, Biol. Reprod. 23: 243-251 (1980) );サル腎臓細胞(CV1 ATCC CCL 70);アフリカミドリザル腎臓細胞(VERO−76, ATCC CRL−1587);ヒト子宮頚癌細胞(HELA, ATCC CCL 2);イヌ腎臓細胞(MDCK, ATCC CCL 34);バッファローラット肝細胞(BRL 3A, ATCC CRL 1442);ヒト肺細胞(W138, ATCC CCL 75);ヒト肝細胞(Hep G2, HB 8065);マウス乳癌(MMT 060562, ATCC CCL51);TRI細胞(Mather et al., Annals N.Y. Acad. Sci. 383: 44-68 (1982));MRC5細胞;FS4細胞;およびヒト肝細胞癌株(Hep G2)である。
本発明の抗体を産生するために使用される宿主細胞を、種々の培地中で培養してもよい。商業的に利用可能な培地、例えばHam’s F10(Sigma)、最小必須培地((MEM)、(Sigma)、RPMI−1640(Sigma)、およびダルベッコ改変イーグル培地((DMEM)、Sigma)などが、宿主細胞を培養するために適する。また、Ham et al., Meth. Enz. 58: 44 (1979)、Barnes et al., Anal. Biochem. 102: 255 (1980)、米国特許第4,767,704号;第4,657,866号;第4,927,762号;第4,560,655号;または第5,122,469号;WO90/03430;WO87/00195;またはU.S. Patent Re.30,985に記載される培地のいずれかを宿主細胞用の培養液として使用してもよい。これらの培地のいずれかに、必要に応じて、以下を補給してもよい:ホルモンおよび/または他の増殖因子(例えばインスリン、トランスフェリン、または上皮増殖因子など)、塩(例えば塩化ナトリウム、カルシウム、マグネシウム、およびリン酸など)、緩衝剤(例えばHEPESなど)、ヌクレオチド(例えばアデノシンおよびチミジンなど)、抗生物質(例えばGENTAMYCIN(商標)薬物など)、微量元素(通常マイクロモル範囲の最終濃度で存在する無機化合物と定義される)、およびグルコースまたは等価のエネルギー供給源。任意の他の必要な補給剤を、また、当業者に公知でありうる適切な濃度で含めてもよい。培養条件、例えば温度、pHなどは、発現のために選択された宿主細胞と共に以前に使用されたものであり、当業者に明らかであろう。
組換え技術を使用する場合、抗体は、細胞内に、ペリプラズム間隙中に産生されうる、または培地中に直接的に分泌されうる。抗体が細胞内に産生される場合、最初の工程として、微粒子細片、宿主細胞または溶解フラグメントを、例えば、遠心分離または限外ろ過により除去する。Carter et al., Bio/Technology 10: 163-167 (1992)には、E.coliのペリプラズム間隙に分泌される単離抗体のための手順が記載される。簡単に説明すると、細胞ペーストを、酢酸ナトリウム(pH3.5)、EDTA、およびフェニルメチルスルホニルフルオリド(PMSF)の存在において約30分にわたり溶解させる。細胞片を遠心分離により除去することができる。抗体が培地中に分泌される場合、そのような発現系からの上清を、一般的に、商業的に利用可能なタンパク質濃縮フィルター、例えば、AmiconまたはMillipore Pellicon限外ろ過ユニットを使用して最初に濃縮する。プロテアーゼ阻害剤、例えばPMSFなどを、先の工程のいずれかに含め、タンパク質分解を阻害してもよく、抗生物質を含め、外来性混入菌の増殖を予防してもよい。
1)ポリクローナル抗体
ポリクローナル抗体は、一般的に、関連抗原およびアジュバントの複数回の皮下(sc)または腹腔内(ip)注射により動物において産生される。関連抗原を、免疫化される種において免疫原性であるタンパク質、例えば、キーホールリンペットヘモシアニン(KLH)、血清アルブミン、ウシサイログロブリン、または大豆トリプシン阻害剤に、二官能性薬剤または誘導体化薬剤、例えば、マレイミドベンゾイルスルホスクシンイミドエステル(システイン残基を通じた抱合)、Nヒドロキシスクシンイミド(リジン(lysien)残基を通じて)、グルタルアルデヒド、無水コハク酸、SOCl2、またはR1N=C=NR(式中、RおよびR1は非依存的により低いアルキル基である)を使用して抱合することが有用でありうる。用いてもよいアジュバントの例は、フロイント完全アジュバントおよびMPL−TDMアジュバント(モノホスホリル脂質A、合成トレハロースジコリノミコラート)を含む。免疫化プロトコールは、過度の実験なしに当業者により選択されうる。
モノクローナル抗体を実質的に均質な抗体の集団から得る。即ち、その集団を含む個々の抗体は、少量で存在しうる、起こりうる天然突然変異および/または翻訳後修飾(例、異性化、アミド化)を除いて同一である。このように、修飾語「モノクローナル」は、別々の抗体の混合物ではないとして抗体の特徴を示す。
本発明の抗体は、さらに、ヒト化抗体またはヒト抗体を含みうる。非ヒト(例、マウス)抗体のヒト化形態は、非ヒト免疫グロブリンに由来する配列を最小に含む、キメラ免疫グロブリン、免疫グロブリン鎖、またはそのフラグメント(例えばFv、Fab、Fab’、F(ab’)2、または抗体の他の抗原結合サブ配列など)である。ヒト化抗体はヒト免疫グロブリン(レシピエント抗体)を含み、それにおいてレシピエントの相補性決定領域(CDR)(本明細書で使用されるHVR)からの残基が、非ヒト種(例えば所望の特異性、親和性、および能力を有するマウス、ラット、またはウサギなど)(ドナー抗体)のCDRからの残基により置換される。一部の例において、ヒト免疫グロブリンのFvフレームワーク残基は、対応する非ヒト残基により置換される。ヒト化抗体は、また、レシピエント抗体においてまたは移入されたCDRまたはフレームワーク配列において見出されない残基を含みうる。一般的に、ヒト化抗体は、少なくとも1つ、典型的には2つの可変ドメインの実質的に全てを含みうるが、それにおいてCDR領域の全てまたは実質的に全てが非ヒト免疫グロブリンのものに対応し、FR領域の全てまたは実質的に全てがヒト免疫グロブリンコンセンサス配列のものである。ヒト化抗体は、最適にはまた、免疫グロブリン定常領域(Fc)の少なくとも部分、典型的にはヒト免疫グロブリンのそれを含む。Jones et al., Nature 321: 522-525 (1986); Riechmann et al., Nature 332: 323-329 (1988)およびPresta, Curr. Opin. Struct. Biol. 2: 593-596 (1992)。
ヒト化に対する代替物として、ヒト抗体を生成することができる。例えば、免疫化時に、内因性の免疫グロブリン産生の非存在においてヒト抗体の完全レパートリーを産生することが可能であるトランスジェニック動物(例、マウス)を産生することが現在可能である。例えば、キメラマウスおよび生殖系列突然変異マウスにおける抗体重鎖連結領域(JH)遺伝子のホモ接合性欠失が、内因性の抗体産生の完全な阻害をもたらすことが記載されている。そのような生殖系列突然変異マウスにおけるヒト生殖系列免疫グロブリン遺伝子アレイの移入は、抗原攻撃時でのヒト抗体の産生をもたらす。例えば、Jakobovits et al., Proc. Natl. Acad. Sci. USA, 90: 2551 (1993); Jakobovits et al., Nature, 362: 255-258 (1993); Bruggermann et al., Year in Immuno., 7: 33 (1993);米国特許第5,591,669号およびWO97/17852を参照のこと。
特定の状況において、抗体全体よりむしろ抗体フラグメントを使用することに利点がある。より小さなフラグメントサイズは迅速なクリアランスを可能にし、固形腫瘍に対する改善されたアクセスに導きうる。
本発明の抗体を、また、ADEPTにおいて、プロドラッグ(例、ペプチジル化学療法剤、WO81/01145を参照のこと)を活性な抗癌薬物に変換するプロドラッグ活性化酵素に抗体を抱合させることにより使用してもよい。例えば、WO88/07378および米国特許第4,975,278号を参照のこと。
二特異性抗体(BsAb)は、少なくとも2つの異なるエピトープ(同じまたは別のタンパク質上のものを含む)について結合特異性を有する抗体である。あるいは、1つのアームは標的抗原に結合することができ、別のアームは、白血球上の誘発分子、例えばT細胞受容体分子(例、CD3)、またはIgGについてのFc受容体(FcγR)、例えばFcγR1(CD64)、FcγRII(CD32)、およびFcγRIII(CD16)などに結合するアームと組み合わせることができ、細胞防御機構を標的の抗原発現細胞に集中させ、局在化する。そのような抗体は、全長抗体または抗体フラグメント(例、F(ab’)2二特異性抗体)に由来しうる。
多価抗体は、抗体が結合する抗原を発現する細胞により、二価抗体よりも速くインターナリゼーションされうる(および/または異化されうる)。本発明の抗体は、3つまたはそれ以上の抗原結合部位(例、四価抗体)を伴う多価抗体(それはIgMクラス以外のものである)でありうるが、それは、抗体のポリペプチド鎖をコードする核酸の組換え発現により容易に産生することができる。多価抗体は、二量体化ドメインおよび3つまたはそれ以上の抗原結合部位を含むことができる。好ましい二量体化ドメインは、Fc領域またはヒンジ領域を含む(またはそれからなる)。このシナリオにおいて、抗体は、Fc領域およびFc領域のアミノ末端に3つまたはそれ以上の抗原結合部位を含みうる。本明細書における好ましい多価抗体は、3〜約8、しかし好ましくは4つの抗原結合部位を含む(またはそれからなる)。多価抗体は、少なくとも1つのポリペプチド鎖(および好ましくは2つのポリペプチド鎖)を含み、それにおいてポリペプチド鎖は2つまたはそれ以上の可変ドメインを含む。例えば、ポリペプチド鎖はVD1−(X1)n−VD2−(X2)n−Fcを含みうるが、それにおいてVD1は第1の可変ドメインであり、VD2は第2の可変ドメインであり、FcはFc領域の1つのポリペプチド鎖であり、X1およびX2はアミノ酸またはポリペプチドを表し、nは0または1である。例えば、ポリペプチド鎖は以下を含みうる:VH−CH1フレキシブルリンカーVH−CH1−Fc領域鎖;またはVH−CH1−VH−CH1−Fc領域鎖。本明細書における多価抗体は、好ましくは、少なくとも2つの(好ましくは4つの)軽鎖可変ドメインポリペプチドをさらに含む。本明細書における多価抗体は、例えば、約2〜約8つの軽鎖可変ドメインポリペプチドを含みうる。本明細書で検討する軽鎖可変ドメインポリペプチドは、軽鎖可変ドメインを含み、場合により、CLドメインをさらに含む。
ヘテロコンジュゲート抗体も本発明の範囲内にある。ヘテロコンジュゲート抗体は、2つの共有結合的に連結された抗体で構成される。例えば、ヘテロコンジュゲート中の抗体の1つをアビジンに、他をビオチンに共役することができる。そのような抗体は、例えば、免疫系細胞を不要な細胞に対して標的化すること(U.S.P.4,676,980)およびHIV感染の処置のために提案されている。WO91/00360、WO92/200373、およびEP0308936.抗体を、合成タンパク質化学において公知の方法(架橋薬剤を含むものを含む)を使用してin vitroで調製されうることが検討される。例えば、免疫毒素を、ジスルフィド交換反応を使用してまたはチオエーテル結合を形成することにより構築してもよい。この目的のための適した試薬の例は、イミノチオラート(iminothiolate)およびメチル−4−メルカプトブチルイミデートならびに、例えば、米国特許第4,676,980号に開示されるものを含む。ヘテロコンジュゲート抗体は、任意の便利な架橋方法を使用して作製してもよい。適した架橋薬剤は当技術分野において周知であり、米国特許第4,676,980号において、多くの架橋技術と共に開示される。
本発明の抗体を、Fcエフェクター機能に関して改変し、例えば、抗体の抗原依存性細胞媒介性細胞傷害(ADCC)および/または補体依存性細胞傷害(CDC)を改変する(例、増強または除去する)ことが望まれうる。好ましい実施態様において、抗PD−L1抗体のFcエフェクター機能を低下または除去する。これは、抗体のFc領域において1つまたは複数のアミノ酸置換を導入することにより達成されうる。あるいはまたは加えて、システイン残基をFc領域中に導入してもよく、それによりこの領域における鎖間ジスルフィド結合形成を可能にする。このようにして生成されたホモ二量体抗体は、改善されたインターナリゼーション能力および/または増加した補体媒介性細胞殺傷および抗体依存性細胞傷害(ADCC)を有しうる。Caron et al., J. Exp Med. 176: 1191-1195 (1992)およびShopes, B. J. Immunol. 148: 2918-2922 (1992)を参照のこと。増強した抗腫瘍活性を伴うホモ二量体抗体は、また、Wolff et al., Cancer Research 53: 2560-2565 (1993)に記載されるヘテロ二官能性架橋剤を使用して調製されうる。あるいは、二重Fc領域を有し、それにより増強した補体溶解およびADCC能力を有しうる抗体を操作することができる。Stevenson et al., Anti-Cancer Drug Design 3: 219-230 (1989)を参照のこと。
本明細書に記載する抗体のアミノ酸配列の改変を検討する。例えば、抗体の結合親和性および/または他の生物学的特性を改善することが望まれうる。抗体のアミノ酸配列バリアントを、抗体核酸中へ適切なヌクレオチド変化を導入することによりまたはペプチド合成により調製する。そのような改変は、例えば、抗体のアミノ酸配列内の残基からの欠失、および/またはその中への挿入、および/またはその置換を含む。欠失、挿入、および置換の任意の組み合わせを作製し、最終産物に達する(最終的な構築物が所望の特徴を保有するという条件で)。アミノ酸変化は、また、抗体の翻訳後プロセスを変化させうる(例えばグリコシル化部位の数または位置を変化させるなど)。
(1)疎水性:ノルロイシン、met、ala、val、leu、ile;
(2)中性疎水性:cys、ser、thr;
(3)酸性:asp、glu;
(4)塩基性:asn、gln、his、lys、arg;
(5)鎖の方向に影響を与える残基:gly、pro;および
(6)芳香族:trp、tyr、phe
本発明の抗体をさらに改変し、当技術分野において公知であり、容易に利用可能な追加の非タンパク質成分を含むことができる。好ましくは、抗体の誘導体化のために適した成分は、水溶性ポリマーである。水溶性ポリマーの非限定的な例は、限定はされないが、以下を含む:ポリエチレングリコール(PEG)、エチレングリコール/プロピレングリコールのコポリマー、カルボキシメチルセルロース、デキストラン、ポリビニルアルコール、ポリビニルピロリドン、ポリ−1,3−ジオキソラン、ポリ−1,3,6−トリオキサン、エチレン/無水マレイン酸コポリマー、ポリアミノ酸(ホモポリマーまたはランダムコポリマーのいずれか)、およびデキストランまたはポリ(n−ビニルピロリドン)ポリエチレングリコール、ポリプロピレングリコールホモポリマー、ポリプロピレンオキシド/酸化エチレンコポリマー、ポリオキシエチル化ポリオール(例、グリセロール)、ポリビニルアルコール、およびその混合物。ポリエチレングリコールプロピオンアルデヒドは、水中でのその安定性のため、製造において利点を有しうる。ポリマーは、任意の分子量でありうる、分岐または非分岐でありうる。抗体に付着するポリマーの数は変動しうるが、1つを上回るポリマーが付着する場合、それらは同じまたは異なる分子でありうる。一般的に、誘導体化のために使用されるポリマーの数および/または型は、抗体誘導体が限定条件下での治療において使用されるか否かなどにかかわらず、考察(限定はされないが、改善される抗体の特定の特性または機能を含む)に基づいて決定することができる。そのような技術および他の適した製剤が、Remington: The Science and Practice of Pharmacy, 20th Ed., Alfonso Gennaro, Ed., Philadelphia College of Pharmacy and Science (2000)に開示される。
治療用製剤は、保存のために、所望の程度の純度を有する活性成分を、任意の医薬的に許容可能な担体、賦形剤、または安定剤と混合することにより調製する(Remington: The Science and Practice of Pharmacy, 20th Ed., Lippincott Williams & Wiklins, Pub., Gennaro Ed., Philadelphia, PA 2000)。許容可能な担体、賦形剤、または安定剤は、用いられる投与量および濃度でレシピエントに対して無毒性であり、バッファー、抗酸化剤(アスコルビン酸を含む)、メチオニン、ビタミンE、メタ重亜硫酸ナトリウム;保存剤、等張剤、安定剤、金属複合体(例、Zn−タンパク質複合体);キレート剤(例えばEDTAおよび/または非イオン界面活性剤など)を含む。
疾患の予防または処置のために、活性薬剤の適切な投与量は、処置される疾患の型(上で定義する)、疾患の重症度および経過(薬剤が予防的または治療的な目的のために投与されるか否かにかかわらず)、過去の治療、患者の臨床歴および薬剤に対する応答、ならびに主治医の判断に依存しうる。薬剤は、患者に対して、1回でまたは一連の処置にわたり適切に投与される。
PD−1およびそのリガンド(「PD−1:PD−L」)は、急性および慢性感染を起こす病原体に対する免疫防御を調節する際に重要な役割を果たす。PD−1:PD−Lシグナル伝達は、効果的な抗菌免疫防御と免疫媒介性組織損傷の間でのバランスを調節する際に重要な役割を果たす。例えば、PD−1ノックアウトマウスは、それらの野生型の対応物よりも迅速にアデノウイルス感染を除去し、それらはより重度の肝細胞傷害を発生する。Iwai et al., J. Exp. Med. 198: 39-50 (2003)。ヘルペス間質性角膜炎のマウスモデルにおいて、抗PD−L1抗体の遮断は角膜炎を悪化させ、HSV−1特異的エフェクターCD4 T細胞増殖およびIFN−γ産生および生存を増加させた。Jun et al., FEBS Lett. 579: 6259-64 (2005)。
腫瘍免疫についての経験的な証拠は以下を含む:(i)自然寛解の観察、(ii)腫瘍に対する検出可能であるが、しかし、無効である宿主免疫応答の存在、(iii)免疫不全患者における原発および二次悪性腫瘍の増加した羅患率、(iv)腫瘍患者における増加レベルの抗体およびTリンパ球の検出、ならびに(v)試験動物を種々の腫瘍型に対して免疫化することができるとの観察。
試験では、大半のヒト腫瘍が、T細胞により認識されることができ、このように免疫応答を誘導することが潜在的に可能である腫瘍関連抗原(TAA)を発現することが示されている。Boon et al., Immunol. Today 16: 334-336 (1995)。初期段階の臨床試験が、TAAまたはTAAを用いてパルスされた専門の抗原提示細胞を用いて癌患者にワクチン接種することにより開始されている。Dudley et al., Science 298: 850-854 (2002); Gajewski et al., Clin. Cancer Res. 7: 895s-901s (2001); Marincola et al., Adv. Immunol. 74: 181-273 (2000); Peterson et al., J. Clin. Oncol. 21: 2342-2348 (2003)。腫瘍抗原特異的CD8+T細胞の誘導が、これらの試験の多くにおいて達成されている。Mackensen et al., Eur. Cytokine Netw 10: 329-336 (1999); Peterson et al., supra。腫瘍抗原特異的T細胞の患者中への養子移入も追求されており、増殖した細胞傷害性T細胞(CTL)の腫瘍部位への帰巣が明らかになっている。Meidenbauer et al., J. Immunol. 170: 2161-2169 (2003)。しかし、免疫エフェクター細胞の腫瘍浸潤にもかかわらず、腫瘍増殖はほとんど制御されなかった。
本発明の方法を、慢性感染または癌の処置の公知の方法と組み合わせることができる(組み合わせもしくは追加の処置工程としてまたは治療用製剤の追加成分として)。
腫瘍と戦うために宿主の免疫機能を増強することが、増加する興味の対象である。従来の方法は以下を含む:(i)APC増強、例えば(a)外来MHC同種抗原をコードするDNAの腫瘍中への注射、または(b)腫瘍の免疫抗原認識(例、免疫刺激性サイトカイン、GM−CSF、同時刺激分子B7.1、B7.2)の確率を増加させる遺伝子を用いた生検腫瘍細胞のトランスフェクション、(iii)活性化した腫瘍特異的T細胞を用いた養子細胞免疫療法、または処置。養子細胞免疫療法は、腫瘍浸潤宿主Tリンパ球を単離すること、in vitroで集団を増殖すること(例えばIL−2もしくは腫瘍または両方による刺激を通じて)を含む。加えて、機能障害性である単離T細胞を、また、本発明の抗PD−L1抗体のin vitro適用により活性化してもよい。そのようにして活性化されたT細胞を次に宿主に再投与してもよい。
感染(例、急性および/または慢性)の処置において、本発明の抗PD−L1抗体の投与を、感染に対する自然宿主免疫防御の刺激に加えてまたはその代わりに、従来の処置と組み合わせることができる。感染に対する自然宿主免疫防御は、限定はされないが、炎症、発熱、抗体媒介性宿主防御、Tリンパ球媒介性宿主防御(リンホカイン分泌および細胞傷害性T細胞(特にウイルス感染の間)を含む)、補体媒介性溶解およびオプソニン作用(食作用を促進)、ならびに食作用を含む。反応性機能障害性T細胞に対する本発明の抗PD−L1抗体の能力が、慢性感染、特に細胞媒介性免疫が完全回復のために決定的であるものを処置するために有用でありうる。
細菌感染に起因する感染のために、本発明の抗PD−L1抗体を、細菌感染を処置するための標準治療と同時の、その前の、またはそれに続く投与と組み合わせてもよい。細菌感染が、今日、抗菌抗生物質を用いて最も一般的に処置されるが、しかし、免疫化宿主からの病原体特異的抗体を含む血清も効果的でありうる。
ウイルスの原因に起因する感染について、本発明の抗PD−L1抗体を、ウイルス感染を処置するための標準的な治療の適用と同時の、その前の、またはそれに続く適用と組み合わせてもよい。そのような標準的治療は、ウイルスの型に依存して変動するが、ほぼ全例において、ウイルスに特異的なヒト血清含有抗体(例、IgA、IgG)の投与が効果的でありうる。
インフルエンザ感染は、発熱、咳、筋肉痛、頭痛、および倦怠感をもたらし、それらはしばしば季節的流行において生じる。インフルエンザは、また、多くの感染後障害、例えば脳炎、心筋心膜炎、グッドパスチャー症候群、およびライ症侯群などに関連する。インフルエンザ感染は、また、正常な肺の抗細菌防御(例えば患者のインフルエンザからの回復など)を抑制し、細菌性肺炎が発生する増加リスクを有する。
9〜11日間のインキュベーション後、麻疹ウイルスに感染した宿主は、発熱、咳、鼻感冒、および結膜炎を発生する。1〜2日間以内に、紅斑性、斑点状丘疹が発生し、急速に全身にわたり広がる。感染は、また、細胞性免疫を抑制するため、宿主には、細菌重複感染(中耳炎、肺炎、および感染後脳脊髄炎を含む)を発生するより大きなリスクがある。急性感染は、特に栄養不良の思春期の若者において、重大な罹患および死亡に関連する。
B型肝炎ウイルス(HB−V)は、最も感染性の高い公知の血液由来病原体である。それは、急性および慢性肝炎および肝臓癌、ならびに一生の慢性感染の主要な原因である。感染に続き、ウイルスが肝細胞において複製し、また、次に表面抗原HBsAgを放出する。血清中の過剰レベルのHBsAgの検出は、B型肝炎感染を診断するための標準的方法として使用される。急性感染は消散しうる、または、それは慢性の持続的感染に発生しうる。
C型肝炎ウイルス(HC−V)感染が、肝炎の慢性形態に導き、肝硬変(cirrosis)をもたらしうる。症状はB型肝炎に起因する感染と類似し(HB−Vとは明確に異なる)、感染宿主は10〜20年間にわたり無症候性でありうる。HC−V感染のための処置が、α−インターフェロンおよびリバビリンの組み合わせの投与を含む。HC−V感染についての有望な潜在的治療は、プロテアーゼ阻害剤テラプレビル(VX−960)である。追加の処置は以下を含む:抗PD−1抗体(MDX−1106、Medarex)、バビツキシマブ(bavituximab)(B2−糖タンパク質I依存的な様式で陰イオンリン脂質ホスファチジルセリンに結合する抗体、Peregrine Pharmaceuticals)、抗HPVウイルスコートタンパク質E2抗体(例、ATL 6865 − Ab68 + Ab65,XTL Pharmaceuticals)、およびCivacir(登録商標)(ポリクローナル抗HCVヒト免疫グロブリン)。本発明の抗PD−L1抗体は、治療的利点のためにC型肝炎感染のためのこれらの処置の1つまたは複数と組み合わせてもよい。
HIVはCD4+細胞(Tリンパ球、単球−マクロファージ、濾胞樹状細胞、およびランゲルハンス細胞を含む)を攻撃し、CD4+ヘルパー/誘導細胞が枯渇される。結果として、宿主は細胞媒介性免疫における重度の欠損を獲得する。HIV感染は、個人の少なくとも50%においてAIDSをもたらし、性的接触、感染した血液または血液産物の投与、感染した精液を用いた人工受精、血液を含む針またはシリンジへの暴露、および感染した母親から新生児への出産の間での伝達を介して伝達される。
サイトメガロウイルス(CMV)感染は、しばしば、持続的で、潜在的で、および再発性の感染に関連する。CMVが、単球および顆粒球−単球前駆細胞において感染し、潜在性のままである。CMVの臨床症状は、単核球症様症状(即ち、発熱、肥大した腺、倦怠感)および抗生物質に対するアレルギー性皮膚発疹を発生する傾向を含む。ウイルスは直接接触により広がる。ウイルスが、尿、唾液、精液、およびより少ない程度で他の体液に放出される。伝達は、また、感染した母親から彼女の胎児または新生児に、輸血および臓器移植により生じうる。CMV感染は細胞性免疫の全身損傷をもたらし、非特異的マイトジェンおよび特異的CMV抗原に対する損なわれた幼若化応答、細胞傷害能力の減弱、およびCD4+リンパ球のCD8リンパ球数の上昇により特徴付けられる。
エプスタイン・バーウイルス(EBV)は、持続的で潜在的な感染を確立することができ、主にB細胞を攻撃する。EBV感染は、感染性単核球症の臨床状態(発熱、咽頭炎(しばしば浸出物を伴う)、全身性リンパ節腫脹、および脾腫大を含む)をもたらす。肝炎も存在し、それは黄疸を発生しうる。
単純ヘルペスウイルス(HSV)は感染宿主との直接接触により伝達される。直接感染は無症候性でありうるが、しかし、典型的に、感染粒子を含む水疱をもたらす。疾患は疾患の活動期間のサイクルとして発現し、それにおいて病変は、ウイルスが続く大流行のために神経節に潜在的に感染するにつれて出現し消滅する。病変は、顔、生殖器、眼および/または手にありうる。一部の場合において、感染は脳炎も起こすことができる。
ヒトTリンパ向性ウイルス(HTLV−1、HTLV−2)は性的接触、授乳、または汚染血液への暴露を介して伝達される。ウイルスはTH細胞(Th1細胞と呼ばれる)のサブセットを活性化し、それらの過剰増殖およびTh1関連サイトカイン(例、IFN−γおよびTNF−α)の過剰産生をもたらす。これは、次に、Th2リンパ球の抑制およびTh2サイトカイン産生(例、IL−4、IL−5、IL−10、およびIL−13)の低下をもたらし、クリアランスのためにTh2依存性応答を必要とする侵入生物に対する適切な免疫応答を高める感染宿主の能力における低下を起こす(例、寄生虫感染、粘膜抗体および液性抗体の産生)。
ヒトパピローマウイルス(HPV)は主にケラチノサイトに影響を与え、2つの形態で生じる:皮膚および生殖器。伝達は、直接接触および/または性的活動を通じて生じると考えられる。皮膚および生殖器の両方のHPV感染は、疣贅および潜在的感染および時には再発性感染をもたらしうるが、それらは症状を制御し、疣贅の出現を遮断するが、しかし、感染を他に伝達することが可能である宿主を残す宿主免疫により制御される。
真菌感染、または真菌症は、一次感染または内因性微生物叢による免疫系低下を伴う宿主での日和見コロニー形成をもたらす。真菌症に対する免疫は主に細胞性であり、好中球、マクロファージ、リンパ球、および恐らくはナチュラルキラー(NK)細胞を含む。真菌症は、典型的に、抗体および補体による直接的な殺傷に感受性ではない。一次感染に起因する全身の非侵襲性真菌症は、ブラストミセス症、コクシジオイデス症(coccidioiodomycosis)、ヒストプラスマ症、およびパラコクシジオイデス症を含む。真菌感染に起因する慢性感染のために、本発明の抗PD−L1抗体を、これらの真菌症のための従来から公知の処置のいずれかの前に、それと同時に、またはそれに続いて投与してもよい。
寄生虫障害(例えばマラリア、住血吸虫症、およびレーシュマニア症など)に起因する疾患が、開発途上国において最も流行しており、重要な健康問題になっている。これらの疾患は特定の攻撃を引き起こす。なぜなら、それらは以下を含む種々の手段を通じて宿主免疫を回避しうるからである:1)宿主細胞内での生存(例、リーシュマニア属)、2)迅速に変化する表面抗原(例、トリパノソーマ)、および3)宿主抗原を提示することによりそれら自身を宿主細胞として「偽る」(例、住血吸虫症)。癌の処置における臓器移植と併用した免疫抑制薬物の使用、ならびにAIDの世界的な罹患率は、プラスモジウム属、トキソプラズマ属、リーシュマニア属、クリプトスポリジウム属、トリパノソーマ属、および蠕虫からの潜在的または無症状性感染を復活させることができる。
ワクチン接種または疾患に対して免疫を誘導するための抗原材料の投与を定期的に使用し、病原体による感染の効果を妨げる、または改善する。宿主免疫の増強は、感染性の病原体だけでなく、罹患した(例、癌性)宿主組織でも見出される非所望の抗原に使用することができる。従来、ワクチンは、弱められたまたは死んだ病原体の全体に由来するが、しかし、それらは、また、ヒトのクラスIまたはクラスII主要組織適合複合体(MHC)分子により特異的に認識されるインタクトな病原体上のペプチド提示エピトープでありうる。特定の目的のペプチド抗原は、T細胞により特異的に認識されるものである。
本発明の医薬的組成物の投与量および所望の濃度は、想定される特定の使用に依存して変動しうる。適切な投与量または投与経路の決定は、当業者の能力の十分に範囲内である。動物実験は、ヒトの治療のための有効量の決定のための信頼できるガイダンスを提供する。有効量の種間スケーリングは、Mordenti, J. and Chappell, W. "The Use of Interspecies Scaling in Toxicokinetics," In Toxicokinetics and New Drug Development, Yacobi et al., Eds, Pergamon Press, New York 1989, pp.42-46に定められる原理に従って実施することができる。
本発明の製剤は、限定はされないが、再構成された液体製剤を含み、抗PD−L1抗体を用いた処置を必要とする哺乳動物、好ましくはヒトへ、公知の方法に従って(例えばボーラスとしての静脈内投与、あるいはある期間にわたる持続的注入により、筋肉内、腹腔内、脳脊髄内、皮下、関節内、滑液内、髄腔内、経口、局所、または吸入経路により)投与される。
本発明の別の実施態様において、製造品が提供され、それは製剤を含む、好ましくはその使用のための説明書を提供する。製造品は容器を含む。適した容器は、例えば、ボトル、バイアル(例、二重チェンバーバイアル)、シリンジ(例えば一重または二重チェンバーシリンジなど)、および試験管を含む。容器は、種々の材料(例えばガラスまたはプラスチックなど)から形成されうる。容器は製剤を保持する。容器上にある、またはそれに関連するラベルは、再構成および/または使用のための指示を示しうる。ラベルは、さらに、製剤が皮下投与のために、および/またはT細胞機能障害性障害の処置のために有用である、または意図されることを示しうる。製剤を保持する容器は、再構成製剤の反復投与(例、2〜6回投与)を可能にする複数回使用バイアルでありうる。製造品は、さらに、適した希釈剤(例、BWFI)を含む第2の容器を含みうる。希釈剤および凍結乾燥製剤の混合時、再構成製剤中の最終的なタンパク質濃度は、一般的に、少なくとも50mg/mlでありうる。製造品は、さらに、市販のユーザーの見地から望ましい他の材料を含みうる(他の緩衝剤、希釈剤、フィルター、針、シリンジ、および添付文書(使用説明書を伴う)を含む)。
ファージライブラリーにおける抗PD−L1抗体の同定
抗PD−L1抗体を同定するためのライブラリー選別およびスクリーニング
ヒト(R&D Systems,cat# 156-B7)およびマウス(R&D Systems,cat# 1019-B7)PD−L1−Fc融合体を、代替ライブラリー選別のための抗原として使した。具体的には、ファージライブラリーを、最初にヒト抗原、続く3ラウンドにおいてマウス、ヒト、およびマウス抗原に対して選別した。Nunc 96 well Maxisorp(登録商標)を標的タンパク質(10μg/ml)と4℃で一晩コートし、室温で1時間にわたりファージブロッキングバッファーPBST(リン酸緩衝食塩水(PBS)および1%(w/v)ウシ血清アルブミン(BSA)および0.05%(v/v)tween-20)を用いてブロックした。抗体ファージライブラリーVH(例、Lee et al., J. Immunol. Meth. 284: 119-132, 2004を参照のこと)およびVH/VL(Liang et al., J. Mol. Biol .366: 815-829, 2007を参照のこと)を別々に抗原プレートに加え、室温で一晩インキュベートした。次の日、抗原コートされたプレートをPBT(0.05% Tween-20を伴うPBS)を用いて10回洗浄し、結合したファージを50mM HClおよび500mM NaClを用いて30分間にわたり溶出し、等容積の1M Trisベース(pH7.5)を用いて中和した。回収したファージをE.coli XL−1 Blue細胞において増幅させた。続く選択ラウンドの間、抗原コートプレートを用いた抗体ファージのインキュベーションを2〜3時間に低下させ、プレート洗浄のストリンジェンシーを徐々に増加させた。
ファージミドpW0703(ファージミドpV0350−2b(Lee et al., J. Mol.Biol 340: 1073-1093 (2004))に由来し、全てのCDR−L3位置に終始コドン(TAA)を含み、M13バクテリオファージの表面上に一価Fabを提示する)は、親和性成熟のためにVHライブラリーからの目的のクローンの重鎖可変ドメイン(VH)を移植するためのライブラリーテンプレートとしての役割を果たした。ハードおよびソフトの両方のランダム化戦略を親和性成熟のために使用した。ハードなランダム化のために、3つの軽鎖CDRの選択された位置を伴う1つの軽鎖ライブラリーを、天然ヒト抗体を模倣するように設計されたアミノ酸を使用してランダム化し、設計されたDNA縮重はLee et al.(J. Mol. Biol 340, 1073-1093 (2004)に記載された。ソフトなランダム化のために、CDR−L3の位置91〜94、および96、CDR−H1の28〜31および34〜35、CDR−H2の50、52、および53〜58、CDR−H3の95〜99および100Aを標的化した;ならびに、CDRループ(L3/H1/H2およびL3/H3)の2つの異なる組み合わせをランダム化のために選択した。ソフトなランダム化条件(それにより選択された位置での約50%の突然変異率が産生された)を達成するために、突然変異DNAを、野生型ヌクレオチドを支持する塩基の70−10−10−10混合物を用いて合成した(Gallop et al., Journal of Medicinal Chemistry 37:1233-1251 (1994))。
以前に同定されたファージクローンを、第1ラウンドのためのプレート選別に供し、5または6ラウンドの溶液選別が続いた。ライブラリーを、ヒトおよびマウスPD−L1−Fcに対してそれぞれ選別した(R&D Systems、それぞれcat.#156−B7、cat #1019−B7)。ヒトPD−L1−Fcのために、第1ラウンドのプレート選別で、3つのライブラリーを、標的コートプレート(NUNC Maxisorp(登録商標)プレート)に対して、1% BSAおよび0.05% Tween-20中のファージインプット(約3 O.D./ml)を別々に用いて、2時間にわたり室温で選別した。第1ラウンドのプレート選別後、溶液選別を実施し、選択のストリンジェンシーを増加した。溶液選別のために、第1ラウンドのプレート選別から増殖させた1 O.D./mlファージを、1% Superblock(Pierce Biotechnology)および0.05% Tween-20を含む100μL緩衝液中で20nmビオチン化標的タンパク質(濃度は、親クローンファージのIC50値に基づく)を用いて、30分間にわたり室温でインキュベートした。混合物を、さらに、1% Superblockを用いて10×希釈し、100μL/ウェルをニュートラアビジンコートされたウェル(5μg/ml)に、15分間にわたり室温で、穏やかに撹拌しながら(ビオチン化標的がファージに結合するように)適用した。ウェルをPBS−0.05% Tween-20を用いて10×洗浄した。バックグラウンド結合を決定するために、ビオチン化されなかった標的を伴うファージを含むコントロールウェルを、ニュートラアビジンコートされたプレート上で捕捉した。結合したファージを0.1N HClを用いて20分間にわたり溶出させ、1/10容積の1M Tris pH−11により中和し、滴定し、次のラウンドために増殖させた。次に、5を上回るラウンドの溶液選別を、増加する選択ストリンジェンシーの2つの方法を一緒に用いて行った。その第1は、ビオチン化標的タンパク質濃度を減少させる(4nMから0.5nMまで)ことによるオンレート選択のためであり、その第2は、過剰量の非ビオチン化標的タンパク質(100〜2000倍以上)を加え、弱い結合剤を室温または37℃のいずれかで競合除去することによるオフレート選択のためである。また、ファージインプットをより低いバックグラウンドファージ結合まで減少させた(0.1〜0.5O.D/ml)。マウスPD−L1−Fc標的について、ファージ選別方法は、ヒトPD−L1 Fc抗原について上で記載されるものと類似であり、少数の改変を伴う。具体的には、100nmビオチン化マウスPD−L1−Fcを、第1ラウンドのプレートパニングの直後に溶液パニングのために使用した。4回の続くラウンドの溶液パニングにおいて、ビオチン化標的を10nMから1nMまで低下させ、200〜500倍過剰の非ビオチン化標的を室温で加えた。
コロニーを、それぞれヒトおよびマウスのPD−L1標的についての7回目および6回目のラウンドのスクリーニングから選んだ。コロニーを、一晩37℃で、96ウェルプレート(Falcon)において150μL/ウェルの2YT培地(50μg/mlカルベニシリンおよび1E10/ml KO7)中で増殖させた。同じプレートから、親ファージの感染したXL−1コロニーをコントロールとして選んだ。96-well Nunc Maxisorp(登録商標)プレートを、PBS中の100μL/ウェルのヒトおよびマウスPD−L1−Fcタンパク質(2μg/ml)を別々に用いて、4℃で一晩または室温で2時間にわたりコートした。プレートを、65μLの1% BSAを用いて30分間にわたり、そして40μLの1% Tween-20を用いて別の30分間にわたりブロックした。
OD450nm低下(%)=[(競争相手を伴うウェルのOD450nm)/(競争相手を伴わないウェルのOD450nm)]×100
hPD−1−Fc、hPD−L1−Fc、hB7.1−Fc、mPD−1−Fc、mPD−L1−Fc、およびmB7.1をR & D Systemsから購入した。hPD−L1発現293細胞を、Genentechで、従来の技術を使用して生成した。F(ab’)2ヤギ抗ヒトIgG FcをJackson ImmunoResearch Laboratoriesから購入した。
PD−1−FcおよびB7.1−Fcタンパク質を、 EZ−Link sulfo−NHS−LC−LC−ビオチン(Pierce)を用いて30分間にわたり室温で、製造業者により記載される通りにビオチン化した。過剰の未反応ビオチンを、Quick Spin High Capacity Columns, G50-Sephadex(Roche)を用いて、製造業者により記載される通りに除去した。
hPD−L1発現293細胞へのhPD−1−Fcの結合の50%阻害(IC50)をもたらす抗体濃度を、電気化学発光(ECL)細胞結合アッセイにより測定した。hPD−L1発現293細胞を、リン酸緩衝食塩水(PBS)を用いて洗浄し、96ウェルHigh Bindプレート(Meso Scale Discovery)で25μLのPBS中に1ウェル当たり25,000個の細胞を播種した。プレートを室温でインキュベートし、細胞が、プレートのカーボン表面に付着することを可能にする。25μLの30% FBSを各ウェルに加え、プレートを30分間にわたり軽く撹拌しながらインキュベートし、非特異的結合部位をブロックする。プレートを3回、PBSを用いて、ELISAマイクロプレートウォッシャー(ELx405 Select, Bio-Tek Instruments)で、穏やかな分注および吸引条件下で洗浄する。ウェル中の過剰なPBSを、プレートをペーパータオル上で吸い取ることにより除去する。12.5μLの2×濃度の抗体を、PBS中の3%FBS(アッセイ緩衝液)中の各ウェルに、続いてアッセイ緩衝液中の12.5μLの4μg/ml(2×濃度)のhPD−1ビオチンを加え、プレートを1時間にわたり軽く撹拌しながらインキュベートする。プレートを、PBSを用いてマイクロプレートウォッシャーで3回洗浄し、プレートをペーパータオル上で吸い取る。25μLの2μg/mlのストレプトアビジン−ルテニウム(Meso Scale Discovery)を加え、アッセイ緩衝液中で、室温で30分間にわたり穏やかに撹拌しながらインキュベートする。PBSを用いてマイクロプレートウォッシャーで3回洗浄し、プレートをペーパータオル上で吸い取る。サーファクタントを伴わない150μLの1×MSD Read Buffer(Meso Scale Discovery)を加える。放出されたルミネセンス光をSector Imager 6000リーダー(Meso Scale Discovery)で、620nmで読み取る。ECL値を、アッセイにおいて使用されるテスト抗体の濃度を用いて、4パラメーターの非線形最小二乗法を使用して分析し、アッセイにおける各競合相手のIC50値を得た。
ヒトおよびマウスの両方のPD−L1に結合した、YW243.55に由来する15の固有ファージ抗体を選び、さらなる評価のために全長IgG1抗体に再フォーマットした。これらの抗体の軽鎖および重鎖可変領域配列を、図11AおよびBに報告する。
抗PD−L1抗体の特徴付け(BIAcore)
組換えヒトおよびマウスPD−L1に対する抗PD−L1ファージ抗体YW243.55およびYW243.55S70の結合親和性を、表面プラズモン共鳴(SRP)によりBIAcore(商標)−3000機器を使用して測定した。組換えヒトPD−L1−Fc(R&D Systems、cat#156−B7)および組換えマウスPD−L1−Fc(R&D Systems、cat#1019−B7)を、CM5バイオセンサーチップ上に直接コートし、約500応答単位(RU)を達成した。動態測定のために、2倍連続希釈物(3.9nm〜500nm)を、PBT緩衝液(0.05% Tween-20を伴うPBS)中で、25℃で、流速30μL/分で注射した。会合速度(kon)および解離速度(koff)を、簡単な1対1のLangmuir結合モデル(BIAcore Evaluation Softwareバージョン3.2)を使用して算出する。平衡解離定数(kD)を比率koff/konとして算出する。
ヒト、アカゲザル、およびマウスのPD−L1についての抗PD−L1 Abの特異性−FACSおよび放射性リガンド細胞結合アッセイ
この実施例は、ヒト、アカゲザル、およびマウスのPD−L1についての本発明の抗PD−L1抗体についての特異性を示す。また、それは、トランスフェクションされた293細胞上の細胞膜で発現されたマウスおよびヒトのPD−L1についてのAbの親和性を示す。
ヒトおよびマウスのPD−L1に対する抗PD−L1 Abの親和性測定−平衡結合放射性リガンド細胞結合アッセイ
ヒトまたはマウスのPD−L1を用いてトランスフェクションされた293細胞を増殖培地(10%ウシ胎仔血清(FBS)、2mM L−グルタミン、1×ペニシリン−ストレプトマイシンを添加したRPMI 1640培地からなる)中で、37℃で5% CO2において培養した。細胞を結合緩衝液(2% FBSおよび50mM Hepes,pH7.2を伴う50:50 DMEM/F12)を用いて洗浄し、96ウェルプレート中に、0.2mLの結合緩衝液中に約230,000個の細胞でプレーティングした。抗PD−L1抗体YW243.55.S70.hIgGを、Iodogen方法を使用してヨード化した。放射標識された抗PD−L1抗体を、遊離125I−NAから、ゲルろ過により、NAP−5カラムを使用して精製した;精製されたAbは17.41μCi/μgの比放射能を有した。一定濃度のヨード化抗体および減少濃度の連続希釈された非標識抗体を含む50μL容積の競合反応混合物を、96ウェルプレート中に置いた。ヒトPD−L1およびマウスPD−L1を発現する293安定的トランスフェクタント細胞株を、増殖培地(10%ウシ胎仔血清(FBS)、2mM L−グルタミン、1×ペニシリン−ストレプトマイシンを添加した50:50 DMEM/F12培地からなる)中で、37℃で5% CO2において培養した。細胞を結合緩衝液(2% FBS、50mM Hepes,pH7.2、および2mMアジ化ナトリウムを伴う50:50 DMEM/F12)を用いて洗浄し、50μLの競合反応混合物に、0.2mLの結合緩衝液中の約200,000個の細胞密度で加えた。細胞を伴う各競合反応におけるヨード化抗体の最終濃度は〜150pM(〜120,000cpm/0.25mL)であり、細胞を伴う競合反応における非標識抗体の最終濃度は変動し、500nMで開始し、次に10濃度について2倍ずつ減少した。細胞を伴う競合反応物を2時間にわたり室温でインキュベートした。非標識抗体の各濃度についての細胞を伴う競合反応物を3通りにアッセイした。2時間のインキュベーション後、競合反応物をMillipore Multiscreenフィルタープレートに移し、結合緩衝液を用いて4回洗浄し、結合ヨード化抗体から遊離物を分離した。フィルターをWallac Wizard 1470ガンマカウンター(PerkinElmer Life and Analytical Sciences Inc.Wellesley, MA)でカウントした。結合データを、NewLigandソフトウェア(Genentech)を使用して評価し、それはMunsonおよびRobardの適合アルゴリズムを使用し、抗体の結合親和性を決定する。Musson et al., Anal. Biochem. 107: 220-39 (1980)。
抗PD−L1 Abの選択性および親和性(IC 50 )
この実施例は、PD−1およびB7.1の両方に対するPD−L1の結合を遮断するためのその能力について本発明の全長抗PD−L1抗体を評価するために使用される結合選択性および親和性(IC50として)を示す。
hPD−L1−Fc ELISAに対するhB7.1−Fc−ビオチンおよびhPD−1−Fc−ビオチン結合(フォーマット4):
Nunc Maxisorp 384ウェルプレートを、PBS中の25μLの250ng/ml hPD−L1−Fcを用いてコートした。ウェルをPBS中の0.05% Tween(洗浄緩衝液)を用いてマイクロプレートウォッシャーで3回洗浄し、ウェルをPBS中の0.5% BSAを用いてブロックする。12.5μLの2×濃度の抗体を、各ウェルへ、PBS中の0.05% Tween、0.5% BSA(アッセイ希釈剤)中に、続いてアッセイ希釈剤中の12.5μLの250ng/ml(2×濃度)のhB7.1−Fc−ビオチンを加え、プレートを1時間半にわたり撹拌しながらインキュベートする。ウェルを、洗浄緩衝液を用いて6回洗浄し、25μLのストレプトアビジン−HRP(アッセイ希釈剤中の1:40,000、GE Healthcare)を加える。プレートを30分間にわたり撹拌しながらインキュベートし、洗浄緩衝液を用いて6回洗浄する。25μLのTMB基質(Kirkegaard and Perry Laboratories)を1時間にわたり加え、反応を25μLの1Mリン酸を用いて停止する。吸光度を450nmで読み、IC50値を、実施例1におけるECL細胞結合アッセイの下に記載される通りに分析する。
hPD−L1−FcへのhPD−1−Fc−ビオチン結合(フォーマット5)のために、フォーマットは、hPD−1−Fc−ビオチンがhB7.1−Fc−ビオチンの代わりに結合のために使用されたことを除き、上のアッセイと類似している。TMB基質の反応時間は17分であった。
指定された結合対の間での相互作用を遮断するための親和性成熟ファージ抗PD−L1抗体YW243.55.S70のIC50の評価を、表4に報告する。YW243.55S70は、hB7.1 FcへのヒトPD−L1の結合を遮断することができた(半最高阻害濃度は38pMであり、PD−L1/PD−1相互作用を遮断するためのそのIC50値(42pM)と比較的同程度の濃度である)。PD−L1とPD−1およびB7.1の両方との相互作用を遮断するためのYW243.55S70の能力を測定するBiacore試験は、これらのELISAでの結果と一致した(データ示さず)。
抗PD−L1抗体YW243.55.S70 PMEL/B16in vitroアッセイによるin vitroでのCD4+およびCD8+T細胞活性の増強
この実施例は、PMEL T細胞受容体トランスジェニックCD8+T細胞の活性化時での本発明の抗PD−L1抗体の効果を示す(メラノサイトペプチドgp100に応答したγ−IFN産生の増強により測定)。この手順において、CD8+T細胞が、CD8+T細胞がgp100ペプチドに特異的なTCRを発現するPMEL TCRトランスジェニックマウスから得られる。CD8+T細胞の精製に続き、複数回ラウンドの刺激を実施し、活性化CD8+T細胞を生成および増殖し、それは次にPD−1発現をアップレギュレーションする。並行して、B16メラノーマ細胞をIFN−γを用いて処置し、それらのPD−L1発現をアップレギュレーションする。次に、細胞を、抗PD−L1抗体の存在において同時培養し、IFN−γ産生に対する効果を評価する。B16細胞を三次刺激のために選んだ。なぜなら、それらは、低レベルのgp100ペプチドを内因性に発現するからである(ペプチドの外因性適用と反対)。さらに、これらの細胞が、また、PD−L2、B7.1、またはB7.2を発現しないため、PD−L1と無関係である追加シグナル伝達(例、PD−1を通じたCD28またはCTLA−4またはPD−L2誘導性シグナル伝達を通じたシグナル伝達)の効果が最小限になる。
図3に示す通り、抗PD−L1抗体は、IFN−γ産生PMEL CD8+T細胞のパーセンテージおよび指定量のgp100ペプチドに応答して産生されるIFN−γの平均レベルの両方を増強する。
Ova特異的TCR Tg CD4+T細胞を利用した同様のアッセイでは、PD−1の発現を誘導するためのOvaペプチドを用いた事前の刺激に続き、抗PD−L1 Abの存在における増強されたT細胞増殖が示される(図4)。最終刺激において、PD−L1を発現する照射A20 B細胞を使用し、DO.11.10 T細胞に対して指定濃度のOvaペプチドを提示した。とりわけ、PD−1/PD−L1軸の寄与が、より低い程度(生理学的に関連する大きさの刺激をより厳密に反映するレベル)の抗原受容体刺激でより顕著である。
PMELアッセイ
一次刺激(0〜4日目)
脾臓および腸間膜リンパ節をPMELトランスジェニックT細胞受容体マウスから収集した。臓器を単一の細胞懸濁液中に粉砕し、赤血球を溶解させた。CD8+T細胞を、CD8+T細胞単離キットおよびAutoMACSセルセパレーター(Miltenyi Biotec)を使用して、製造業者の指示の通りに単離した。
PMEL培養物をスピンダウンし、培地を、マルチチャネルピペットを使用して吸引した。新鮮培地を加え、混合して細胞を洗浄し、別のスピンが続いた。大部分の培地を除去し、抗体(Herceptin(登録商標)、YW243.55.S70、またはなし)を、最終濃度10μg/mlで加えた。条件を2通りのウェルにおいて設定し、平均IFN−γ産生をエンドポイントで評価できるようにした。
6日目の三次刺激の1日前に、B16メラノーマ細胞を、20ng/mlのマウスIFN−γ(R&D Systems)を用いて一晩インキュベートし、それらのPD−L1発現をアップレギュレーションした。
Golgi-Plug(BD Biosciences)を、培養の最後の5時間にわたり、製造業者の指示の通りに加えた。IFN−γ細胞内染色を、BD Biosciences Cytofix/Cytoperm Fixation/Permeabilization Solutionキットを使用して、製造業者の指示の通りに行い、全ての染色抗体もBD Biosciencesからであった。細胞を、CD8a PEおよびThy1.1 FITCを用いて表面染色し、飽和濃度のIFN−γ APCを用いて細胞内染色した。
DO11.10トランスジェニックマウスからの脾臓および腸間膜リンパ節を収集し、単一の細胞懸濁液中に粉砕し、赤血球を溶解させた。細胞を、72時間にわたり、6ウェルプレートにおいて密度1×106個細胞/mlで、Ovaペプチド(0.3μM)を用いて培養した。培養液は、RPMI 1640+10%ウシ胎仔血清+20μM HEPES、およびGibcoからの以下の添加剤の1:100希釈物:Gluta-MAX、ピルビン酸ナトリウム、ペニシリン/ストレプトマイシン、および非必須アミノ酸であった。
抗PD−L1による混合リンパ球反応におけるヒトCD8+T細胞の増強された増殖
図5は、MHC不適合ドナーからの細胞に応答した、ヒトCD8 T細胞の増殖を増強する抗PD−L1(例、YW243.55.S1)の能力を実証する。応答性CD8+T細胞を、ドナーAの全血から、最初にCD8+T細胞RosetteSep(登録商標)(StemCell Technologies)を製造業者の指示の通りに使用して濃縮した。細胞を次に等容積のリン酸緩衝食塩水(PBS)により希釈し、Ficoll-Paque Plus(GE Healthcare)に重層することにより勾配遠心分離により分離した。分離後、細胞を、CD8 APC(BD Biosciences)を用いて染色し、78%のCD8+T細胞であることが見出された。細胞を、2.5μMのCFSEトレーサー染料(Molecular Probes)を用いて蛍光標識した。
LCMVin vivoモデルに対するPD−L1遮断の効果
慢性刺激の条件下のT細胞は、阻害的受容体PD−1の発現をアップレギュレーションし、維持することが示されている。その2つのリガンドPD−L1およびPD−L2のいずれかによるPD−1の連結は、慢性的に活性化されたT細胞の抵抗状態に寄与し、その同種抗原に対するその応答を減弱する。リンパ球性脈絡髄膜炎ウイルス(LCMV)に持続感染したマウスにおいて、PD−1またはそのリガンドPD−L1の遮断は、慢性的に抵抗性であるT細胞を再活性化するために十分であり、抗ウイルスT細胞応答の大きさおよび機能的な質を増強する。同様に、HIVまたはHCVに慢性的に感染されたヒトは、その活性がPD−1またはPD−L1の遮断によりin vitroで増強されうる刺激に対して抵抗性であるT細胞を示す。従って、LCMVモデルにおけるPD−L1遮断の活性は、抗ウイルスおよび抗腫瘍免疫を増強するための治療的な潜在能力を示唆する。
LCMV gp33ペプチドに応答したCD8 T細胞による%IFNガンマ産生の決定
脾臓を感染マウスから単離し、単一の細胞懸濁液を、完全培地:IMDM(Invitrogen Inc., Carlsbad, CA)(10%熱不活化ウシ胎児血清、2mM L−グルタミン、100U/mlペニシリン/ストレプトマイシン、および10mM 2−メルカプトエタノールを含む)中で臓器を破砕することにより生成した。赤血球を、ACK溶解緩衝液(0.15M NH4Cl、10mM KHCO3、0.1mM EDTA)を使用して溶解した。抗原特異的CD8 T細胞応答を測定するために、脾細胞を完全培地中で洗浄し、LCMVペプチドGP33(KAVYNFATC, ProImmune Inc., Bradenton, FL)を用いて4時間にわたりin vitroで再刺激した。1×106個の脾細胞を96ウェル平底プレート中で100ng/mlのGP33ペプチドを用いて100単位/mlのヒトインターロイキン2(Sigma-Aldrich, St. Louis, MO)、1μL/mlのブレフェルジンA、および1μL/ml(1:1000希釈)のモネンシン(BD pharmingen)および抗CD107a FITC(クローンID4B, BD Biosciences, San Jose, CA)の存在において培養した。インキュベーション後、細胞を、2%ウシ胎児血清を含むPBS中で1回洗浄し、細胞表面マーカーを、蛍光色素抱合抗体を使用して染色した:抗CD8 APC(クローン53.67、BD Biosciences, San Jose, CA)、抗CD4 PerCp−Cy5.5(クローンRM4−5,BD Biosciences, San Jose, CA)、および抗PD−1 PE(クローンJ43、BD Biosciences, San Jose, CA)。細胞内IFN−γについての染色を、Cytofix Cytoperm Plusキット(BD Biosciences, San Jose, CA)を使用し、製造業者の指示に従い、抗IFN−γ PE−Cy7(クローンXMG1.2,eBioscience Inc. San Diego, CA)を使用して行った。GP33特異的CD8 T細胞の数を検出し、新鮮脾細胞をGP33五量体(APCに連結されたH2−Db,ProImmune Inc., Bradenton, FL)を用いて、製造業者の指示に従って染色した。データを、BD FACSAria(BD Biosciences, San Jose, CA)を使用して収集し、FlowJo Software(Tree Star Inc. Ashland OR)を用いて分析した。
MC57線維肉腫細胞を、完全IMDM中のLCMV含有血液または組織ホモジネートの10倍連続希釈物を用いて感染させる。反応物を、次に、組織培養インキュベーターにおいて37℃で2〜6時間にわたりインキュベートし、次に1%メチルセルロースを含むDMEMを用いて重層する。これには3〜5日間にわたるインキュベーションが続き、次に、メチルセルロース層を吸引により除去する。細胞をPBS/4%パラホルムアルデヒドを用いて固定し、次に0.5% Triton-xを用いて20分間にわたり透過性化し、PBS中で洗浄し、次に10% FCS中で1時間にわたり軽く揺らしながらブロックする。LCMVについての染色を、VL4抗体を用いて行い(1時間)、2回洗浄し、次にブロッキング緩衝液中の抗ラットHRP(1:400)を用いて現像する。これには3回の洗浄が続き、次にo−フェニレンジアミン基質(SIGMA P8806-50TAB 3mg/錠)をウェルに加えて現像する。
癌におけるPD−L1遮断
現在、多くの腫瘍が、PD−1リガンドの発現を、抗腫瘍T細胞応答を減弱させるための手段として利用することが明らかである。いくつかのヒトの癌が、腫瘍および腫瘍浸潤白血球の両方で上昇レベルのPD−L1を発現すると特徴付けられており、この上昇したPD−L1発現は、しばしば、より悪い予後と関連する。マウス腫瘍モデルでは、腫瘍内のPD−L1発現における類似の増加が実証され、腫瘍免疫を阻害する際でのPD−1/PD−L1経路についての役割が実証される。
グループ2:抗PD−L1抗体、10mg/kg IP、100μL、1日目、3×/週
グループ3:抗gp120抗体、10mg/kg IP、100μL、14日目、3×/週
グループ4:抗PD−L1抗体、10mg/kg IP、100μL、14日目、3×/週
グループ5:抗CTLA−4抗体、10mg/kg IP、100μL、14日目、3×/週
***グループ1および2は1日目に;グループ3、4、および5は14日目に投与を開始した。
抗腫瘍効果を提供するための他の薬剤との抗PD−L1の組み合わせまたは免疫増強治療−MC38.Ovaモデル
0日目に、150匹の動物に、100マイクロリットルのHBSS+matrigel中の0.5百万個のMC38.Ova細胞を用いて皮下接種した。マウスで腫瘍を増殖させる。マウスを体重測定し、11日目まで2×/週で測定した(腫瘍容積が100〜200mm3である場合)。11日目に、腫瘍測定に続き、マウスを以下の12処置群の1つに補充する。異なる腫瘍容積のために以下の処置群に補充されなかったマウスは、安楽死させる。ゲムシタビン(グループ4)処置は12日目に開始され、残りの抗体群のための処置は14日目に開始される。全容積は不活性賦形剤中で100μLであり、追加の詳細が以下に報告される:
グループ2:抗PD−L1抗体、10mg/kg IP、100μL、3×/週×5、n=10
グループ3:抗VEGF抗体、5mg/kg IP、100μL、2×/週×5、n=10
グループ4:ゲムシタビン、40mg/kg IP、100μL、12、16、20日目、n=10
グループ5:抗PD−L1抗体 + 抗gp120抗体、n=10
グループ6:抗PD−L1抗体 + 抗VEGF抗体、n=10
グループ7:抗PD−L1抗体 + ゲムシタビン、n=10
グループ8:抗gp120抗体 + ゲムシタビン、n=10
グループ9:抗gp120抗体 + 抗VEGF、n=10
14日目および22日目:グループ4からのマウスを、CBC分析のために、麻酔下で眼窩後から出血させた(100マイクロリットル)。
19日目:全てのマウス(グループ4を除く)を、CBC分析のために、麻酔下で眼窩後から出血させた(100マイクロリットル)。
26日目:全てのマウス(グループ4を除く)を、PK分析のために、麻酔下で眼窩後から出血させた(100マイクロリットル)。
哺乳動物細胞における抗PD−L1抗体の発現
この実施例は、哺乳動物細胞における組換え発現による、潜在的なグリコシル化形態の抗PD−L1抗体の調製を例示する。
E.coliにおける抗PD−L1抗体の発現
この実施例は、E.coliにおける組換え発現による非グリコシル化形態の抗PD−L1抗体の調製を例示する。
Claims (18)
- 抗PD−L1抗体またはその抗原結合性フラグメントの軽鎖および重鎖可変領域をコードする単離された核酸であって、それにおいて:
(a)重鎖可変領域が、配列GFTFSDSWIH(配列番号15)、AWISPYGGSTYYADSVKG(配列番号16)、およびRHWPGGFDY(配列番号3)をそれぞれ有するHVR−H1、HVR−H2、およびHVR−H3配列を含み、かつ
(b)軽鎖可変領域が、配列RASQDVSTAVA(配列番号17)、SASFLYS(配列番号18)、およびQQYLYHPAT(配列番号19)をそれぞれ有するHVR−L1、HVR−L2、およびHVR−L3配列を含み、
重鎖可変領域アミノ酸配列が、配列番号20の重鎖可変領域アミノ酸配列と少なくとも95%の配列同一性を有し、軽鎖可変領域アミノ酸配列が、配列番号21の軽鎖可変領域アミノ酸配列と少なくとも95%の配列同一性を有する、単離された核酸。 - 軽鎖可変領域アミノ酸配列が、配列番号21の軽鎖可変領域アミノ酸配列と少なくとも99%の配列同一性を有する、請求項1記載の核酸。
- 重鎖可変領域アミノ酸配列が、配列番号20の重鎖可変領域アミノ酸配列と少なくとも99%の配列同一性を有する、請求項1記載の核酸。
- 軽鎖可変領域アミノ酸配列が、配列番号21の軽鎖可変領域アミノ酸配列と少なくとも99%の配列同一性を有し、重鎖可変領域アミノ酸配列が、配列番号20の重鎖可変領域アミノ酸配列と少なくとも99%の配列同一性を有する、請求項1記載の核酸。
- 抗PD−L1抗体が、マウス抗体に由来する定常領域を含む、請求項1記載の核酸。
- 抗PD−L1抗体がヒト抗体に由来する定常領域を含む、請求項1記載の核酸。
- 定常領域が、IgG1である、請求項6記載の核酸。
- 抗PD−L1抗体が、低下したまたは最小のエフェクター機能を有する、請求項7記載の核酸。
- 最小のエフェクター機能が、エフェクターなしFc突然変異に起因する、請求項8記載の核酸。
- エフェクターなしFc突然変異が、N297Aである、請求項9記載の核酸。
- 請求項1〜10のいずれか1項記載の核酸を含むベクター。
- 請求項11記載のベクターを含む宿主細胞。
- 真核生物である請求項12記載の宿主細胞。
- 哺乳動物である請求項13記載の宿主細胞。
- チャイニーズハムスター卵巣(CHO)細胞である請求項14記載の宿主細胞。
- 原核生物である請求項12記載の宿主細胞。
- E.coliである請求項16記載の宿主細胞。
- 請求項12〜17のいずれか1項記載の宿主細胞を、抗PD−L1抗体またはその抗原結合性フラグメントをコードするベクターの発現のために適した条件下で培養すること、およびその抗体または抗原結合性フラグメントを回収することを含む、抗PD−L1抗体、又はその抗原結合性フラグメントを作製するためのプロセス。
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