JP5191537B2 - ヒトのプログラムされたデスレセプターpd−1に対する抗体 - Google Patents
ヒトのプログラムされたデスレセプターpd−1に対する抗体 Download PDFInfo
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Description
プログラムされたデスレセプター1(PD−1)は、活性化されたT細胞およびB細胞において主に発現される免疫抑制受容体である。そのリガンドとの相互作用はin vitroおよびin vivoの両方でT細胞応答を減弱させることが示されている。PD−1とそのリガンドの1つPD−L1との相互作用の遮断は、腫瘍特異的CD8+T細胞免疫を増強することが示されており、したがって免疫系による腫瘍細胞の排除において有益でありうる。
本発明は、ヒトおよびカニクイザルのPD−1に結合する単離された抗体および抗体断片を提供する。いくつかの実施形態において抗体または抗体断片は、ヒトPD−L1およびヒトPD−L2のヒトPD−1への結合を遮断する。いくつかの実施形態において本発明のPD−1抗体または抗体断片は、配列番号9、10、11、12、13、14、15、16、17、18、19および20から選択される1つまたは複数のCDR(抗体相補性決定領域)を含み、さらなる実施形態においては、配列番号12、13、14、18、19および20の1つまたは複数の重鎖CDRならびに/または配列番号9、10、11、15、16および17の軽鎖CDRを含む。いくつかの実施形態において抗体または抗体断片は、キメラ抗体、ヒト抗体、ヒト化抗体またはその断片である。
本発明は、例えば以下の項目を提供する。
(項目1)
a.配列番号9、10、11、15、16および17からなる群から選択される少なくとも1つのCDR、もしくは任意の該配列の変異体、ならびに/または
b.配列番号12、13、14、18、19および20からなる群から選択される少なくとも1つのCDR、もしくは任意の該配列の変異体
を含む、ヒトPD−1に結合する単離された抗体または抗体断片。
(項目2)
a.配列番号9、10および11の軽鎖CDR、もしくは任意の該配列の変異体、ならびに配列番号12、13および14の重鎖CDR、もしくは任意の該配列の変異体、または
b.配列番号15、16および17の軽鎖CDR、もしくは任意の該配列の変異体、ならびに配列番号18、19および20の重鎖CDR、もしくは任意の該配列の変異体
を含む、項目1に記載の抗体または抗体断片。
(項目3)
a.i.配列番号5もしくはその変異体、
ii.配列番号7もしくはその変異体、
iii.配列番号30のアミノ酸残基20から139もしくはその変異体、および
iv.配列番号30のアミノ酸残基20から139に少なくとも90%の相同性を有するアミノ酸配列
からなる群から選択されるアミノ酸配列を含む重鎖可変領域
を含み、
b.i.配列番号6もしくはその変異体、
ii.配列番号8もしくはその変異体、
iii.配列番号32のアミノ酸残基20から130もしくはその変異体、
iv.配列番号33のアミノ酸残基20から130もしくはその変異体、
v.配列番号34のアミノ酸残基20から130もしくはその変異体、および
vi.配列番号32、33もしくは34のアミノ酸残基20から130に少なくとも90%の相同性を有するアミノ酸配列
からなる群から選択されるアミノ酸配列を含む軽鎖可変領域
をさらに含む、項目2に記載の抗体または抗体断片。
(項目4)
a.i.配列番号31のアミノ酸残基20から466もしくはその変異体、および
ii.配列番号35のアミノ酸残基20から469もしくはその変異体
からなる群から選択されるアミノ酸配列を含む重鎖、
ならびに
b.i.配列番号36のアミノ酸残基20から237もしくはその変異体、
ii.配列番号37のアミノ酸残基20から237もしくはその変異体、および
iii.配列番号38のアミノ酸残基20から237もしくはその変異体
からなる群から選択されるアミノ酸配列を含む軽鎖
を含む、項目1に記載の抗体。
(項目5)
(1つまたは複数の)任意の前記変異体が3個までの保存的に改変されたアミノ酸置換を含みうる、項目1から4のいずれかに記載の抗体または抗体断片。
(項目6)
a.ヒト重鎖定常領域、もしくは20個までの保存的に改変されたアミノ酸置換を含むその変異体、および/または
b.ヒト軽鎖定常領域、もしくは20個までの保存的に改変されたアミノ酸置換を含むその変異体
をさらに含む、項目1から3のいずれかに記載の抗体。
(項目7)
前記ヒト重鎖定常領域がγ4もしくはγ1ヒト重鎖定常領域、または20個までの保存的に改変されたアミノ酸置換を含むその変異体を含む、項目6に記載の抗体。
(項目8)
a.約100pMのK D またはそれより低いK D でヒトPD−1に結合する、
b.約30pMのK D またはそれより低いK D でヒトPD−1に結合する、
c.配列番号31のアミノ酸配列を含む重鎖および配列番号32のアミノ酸配列を含む軽鎖を有する抗体と同程度のK D でヒトPD−1に結合する、
d.配列番号31のアミノ酸配列を含む重鎖および配列番号33のアミノ酸配列を含む軽鎖を有する抗体と同程度のK D でヒトPD−1に結合する、
e.約7.5×10 5 1/M・sまたはそれより速いk assoc でヒトPD−1に結合する、
f.約1×10 6 1/M・sまたはそれより速いk assoc でヒトPD−1に結合する、
g.約2×10 −5 1/sまたはそれより遅いk dissoc でヒトPD−1に結合する、
h.約2.7×10 −5 1/sまたはそれより遅いk dissoc でヒトPD−1に結合する、
i.約3×10 −5 1/sまたはそれより遅いk dissoc でヒトPD−1に結合する、
j.約1nMのIC 50 またはそれより低いIC 50 でヒトPD−L1またはヒトPD−L2のヒトPD−1への結合を遮断する、
項目1から7のいずれかに記載の抗体または抗体断片。
(項目9)
項目1から4に記載のいずれかの抗体とPD−1上の結合エピトープについて競合し、以下の特徴:
a.約100pMのK D またはそれより低いK D でヒトPD−1に結合する、
b.約30pMのK D またはそれより低いK D でヒトPD−1に結合する、
c.配列番号31のアミノ酸配列を含む重鎖および配列番号32のアミノ酸配列を含む軽鎖を有する抗体と同程度のK D でヒトPD−1に結合する、
d.配列番号31のアミノ酸配列を含む重鎖および配列番号33のアミノ酸配列を含む軽鎖を有する抗体と同程度のK D でヒトPD−1に結合する、
e.約7.5×10 5 1/M・sまたはそれより速いk assoc でヒトPD−1に結合する、
f.約1×10 6 1/M・sまたはそれより速いk assoc でヒトPD−1に結合する、
g.約2×10 −5 1/sまたはそれより遅いk dissoc でヒトPD−1に結合する、
h.約2.7×10 −5 1/sまたはそれより遅いk dissoc でヒトPD−1に結合する、
i.約3×10 −5 1/sまたはそれより遅いk dissoc でヒトPD−1に結合する、または
j.約1nMのIC 50 またはそれより低いIC 50 でヒトPD−L1またはヒトPD−L2のヒトPD−1への結合を遮断する、
のうち1つを有する
単離された抗体または抗体断片。
(項目10)
a.キメラ抗体もしくはその断片、
b.ヒト抗体もしくはその断片、
c.ヒト化抗体もしくはその断片、または
d.Fab、Fab’、Fab’−SH、Fv、scFv、F(ab’) 2 およびダイアボディーからなる群から選択される抗体断片
である、項目1から9のいずれかに記載の抗体または抗体断片。
(項目11)
T細胞の活性化を増大させる、項目1から10のいずれかに記載の抗体または抗体断片。
(項目12)
項目1から7のいずれか一項に記載の抗体または抗体断片をコードする単離されたポリヌクレオチド。
(項目13)
項目12に記載の単離されたポリヌクレオチドを含む発現ベクター。
(項目14)
項目13に記載の発現ベクターを含む宿主細胞。
(項目15)
a.前記核酸配列が発現される条件下で、培地中で項目14に記載の宿主細胞を培養し、それにより前記軽鎖および前記重鎖可変領域を含むポリペプチドを産生するステップと、
b.該宿主細胞または該培地から該ポリペプチドを回収するステップと
を含む、項目1から11のいずれか一項に記載の抗体または抗体断片を産生する方法。
(項目16)
薬学的に許容される担体または希釈剤と組み合わせて、項目1から11のいずれか一項に記載の抗体または抗体断片を含む組成物。
(項目17)
免疫細胞を項目1から11に記載の抗体のいずれか1つと接触させるステップを含む、該免疫細胞の活性を増大させる方法。
(項目18)
治療有効量の項目1から11のいずれか一項に記載の抗体または抗体断片を、それを必要とする対象に投与するステップを含む、免疫細胞の活性を増大させる方法。
(項目19)
a.癌の治療のため、
b.感染症もしくは感染性疾患の治療のため、または
c.ワクチンアジュバントとして
使用される、項目18に記載の方法。
(項目20)
前記対象由来の試料においてex vivoでT細胞活性化を測定するステップをさらに含み、T細胞活性における増大が前記治療を継続すべきであることを示すか、または前記治療が成功する可能性を予測する、項目18に記載の方法。
(項目21)
T細胞活性における前記増大が
a.IL−2、TNFα、IL−17、IFNγ、GM−CSF、RANTES、IL−6、IL−8、IL−5およびIL−13からなる群から選択される1つまたは複数のサイトカインのSEB誘発産生を測定するステップ、または
b.IL−2、TNFα、IL−17、IFNγ、GM−CSF、RANTES、IL−6、IL−8、IL−5およびIL−13からなる群から選択されるサイトカインのTT誘発産生を測定するステップ
によって決定される、項目20に記載の方法。
(項目22)
a.免疫細胞活性化を増大させるための、
b.癌を治療するための、または
c.感染症もしくは感染性疾患を治療するための
薬剤の調製のための、項目1から11のいずれか一項に記載の抗体または抗体断片の使用。
(項目23)
診断的使用のための、項目1から11のいずれか一項に記載の抗体または抗体断片の使用。
略語および定義
本発明の詳細な記載および実施例を通じて以下の略語が使用される。
hPD−1.09A マウスモノクローナル抗hPD−1抗体
08A−VH hPD−1.08Aハイブリドーマから単離されたVH
08A−VK hPD−1.08Aハイブリドーマから単離されたVK
09A−VH hPD−1.09Aハイブリドーマから単離されたVH
09A−VK hPD−1.09Aハイブリドーマから単離されたVK
c109A hPD−1.09A抗体のキメラIgG1バージョン
c109A−VH hIgG1定常領域に融合しているマウス09A−VHからなるキメラ重鎖
c109A−VK ヒトκ定常領域に融合しているマウス09A−VKからなるキメラ軽鎖
109A−H 復帰突然変異を含まないヒト化IgG1 09A重鎖配列
409A−H FWR復帰突然変異を含まないヒト化IgG4−09A重鎖配列
K09A−L−11 長さ11AAのCDR1を独自に有するフレームワークを含むヒト化09A−κ配列
K09A−L−16 長さ16AAのCDR1を独自に有するフレームワークを含むヒト化09A−κ配列
K09A−L−17 長さ17AAのCDR1を独自に有するフレームワークを含むヒト化09A−κ配列
h409A11 409A−Hの配列を含む重鎖およびK09A−L−11の配列を含む軽鎖を含む09A抗体のヒト化IgG4バージョン
h409A16 409A−Hの配列を含む重鎖およびK09A−L−16の配列を含む軽鎖を含む09A抗体のヒト化IgG4バージョン
h409A17 409A−Hの配列を含む重鎖およびK09A−L−17の配列を含む軽鎖を含む09A抗体のヒト化IgG4バージョン
hPD−1 ヒトPD−1タンパク質
CDR 免疫グロブリン可変領域中の相補性決定領域、Kabat番号付け方式を使用して定義される
EC50 50%有効性または結合を生じる濃度
ELISA 酵素結合免疫吸着検定法
FW 抗体フレームワーク領域、CDR領域を除く免疫グロブリン可変領域
HRP 西洋わさびペルオキシダーゼ
IL−2 インターロイキン2
IFN インターフェロン
IC50 50%抑制を生じる濃度
IgG 免疫グロブリンG
Kabat Elvin A Kabatによって開発された免疫グロブリン配列比較(alignment)および番号付け方式
mAb モノクローナル抗体
MES 2−(N−モルホリノ)エタンスルホン酸
NHS 正常ヒト血清
PCR ポリメラーゼ連鎖反応
SAM ヒツジ抗マウス(IgG)ポリクローナル抗体
V領域 異なる抗体間の配列において可変であるIgG鎖のセグメント。軽鎖におけるKabat残基109および重鎖における113に及ぶ。
VK 免疫グロブリンκ軽鎖可変領域。
PD−1に対するモノクローナル抗体は、被験体にPD−1抗原を注射し、次いで所望の配列または機能特性を有する抗体を発現しているハイブリドーマを単離する当技術分野における知識および技術によって作製できる。
抗体DNAは、例えばヒト重鎖および軽鎖の定常ドメインのコード配列を相同なマウス配列の代わりに置換することによって(米国特許第4,816,567号;Morrisonら、1984年、Proc. Natl Acad. Sci. USA、81巻:6851頁)、または免疫グロブリンではない物質(例えばタンパク質ドメイン)のコード配列の全てまたは一部を免疫グロブリンコード配列に共有結合させることによっても改変されうる。典型的には、そのような免疫グロブリンではない物質は、抗体の定常ドメインの代わりをするか、または、抗原に対する特異性を有する1つの抗原結合部位および異なる抗原に対する特異性を有する他の抗原結合部位とを含むキメラ二価抗体を作るために抗体の1つの抗原結合部位の可変ドメインの代わりをする。
ヒト化抗体は、ヒトではない供給源由来の1つまたは複数のアミノ酸残基を有する。非ヒトアミノ酸残基は、しばしば「移入」残基と称され、典型的には「移入」可変ドメインから取り込まれる。ヒト化は、一般にWinterおよび協力者らの方法(Jonesら、1986年、Nature321巻:522〜525頁;Riechmannら、1988年、Nature、332巻:323〜327頁;Verhoeyenら、1988年、Science 239巻:1534〜1536頁)に従って、げっ歯類CDRまたはCDR配列をヒト抗体の対応する配列の代わりに置換することによって実施されうる。したがってそのような「ヒト化」抗体は、無傷のより実質的に少ないヒト可変ドメインがヒトではない種由来の対応する配列によって置換されているキメラ抗体(米国特許第4,816,567号)である。実際にヒト化抗体は、典型的には、いくつかのCDR残基および場合によりいくつかのFR残基がヒトではない、例えばげっ歯類の抗体中の類似部位由来の残基によって置換されているヒト抗体である。
組換え技術を使用する場合、抗体は細胞内、周辺質間隙に産生されるか、または培地に直接分泌されうる。抗体が細胞内に産生される場合、最初の段階として宿主細胞または溶解断片のいずれかの粒子細片は、例えば遠心分離または限外濾過によって除去される。Carterら、1992年、Bio/Technology 10巻:163〜167頁は、E.coliの周辺質間隙に分泌される抗体の単離のための手順を記載している。簡潔には、細胞ペーストを酢酸ナトリウム(pH3.5)、EDTAおよびフッ化フェニルメチルスルホニル(PMSF)の存在下で約30分間かけて融解する。細胞細片は、遠心分離によって除去されうる。抗体が培地に分泌される場合は、そのような発現系由来の上清を一般的には最初に、市販で入手可能なタンパク質濃縮用フィルター、例えばAmiconまたはMillipore,Pellicon限外ろ過ユニットを使用して濃縮する。PMSFなどのプロテアーゼ阻害剤は、任意の前述のステップにタンパク質分解を阻害するために含まれてよく、抗生物質は外来性の混入物の増殖を防ぐために含まれてよい。
本発明は、本発明のPD−1抗体または抗体断片の医薬製剤を含む。医薬組成物または滅菌組成物を調製するために、抗体およびその断片は、薬学的に許容される担体または賦形剤と混合される、例えばRemington’s Pharmaceutical Sciences and U.S. Pharmacopeia: National Formulary、Mack Publishing Company、Easton、PA(1984年)を参照されたい。治療剤および診断剤の製剤は、生理学的に許容される単体、賦形剤または安定化剤と、例えば凍結乾燥粉末、スラリー、水性溶液または懸濁液の形態で混合することによって調製されうる(例えばHardmanら、(2001年)Goodman and Gilman’s The Pharmacological Basis of Therapeutics、McGraw−Hill、New York、NY;Gennaro(2000年)Remington:The Science and Practice of Pharmacy、Lippincott、Williams、and Wilkins、New York、NY;Avisら(eds.)(1993年)Pharmaceutical Dosage Forms: Parenteral Medications、Marcel Dekker、NY;Liebermanら(eds.)(1990年))Pharmaceutical Dosage Forms:Tablets、Marcel Dekker、NY;Liebermanら(eds.)(1990年)Pharmaceutical Dosage Forms:Disperse Systems、Marcel Dekker、NY;Weiner and Kotkoskie (2000年)Excipient Toxicity and Safety、Marcel Dekker、Inc.、New York、NYを参照されたい)。
ヒトPD−1に特異的に結合する本発明の抗体または抗原結合断片は、免疫応答を増大、増強、刺激または上方制御するために使用されうる。本発明の抗体および抗体断片は、T細胞媒介の免疫応答の増大によって治療されうる障害を有する対象を治療するために特に適切である。好ましい対象は、免疫応答を増強する必要のあるヒト患者を含む。
本発明の抗体または抗原結合断片は、癌を治療する(すなわち腫瘍細胞の増殖または生存を抑制する)ために使用されうる。本発明の抗体を使用して増殖が抑制されうる好ましい癌は、典型的には免疫療法に応答する癌を含むが、免疫療法にこれまで関連がなかった癌も含む。治療について好ましい癌の非限定的例として、黒色腫(例えば転移性悪性黒色腫)、腎臓癌(例えば明細胞癌)、前立腺癌(例えばホルモン難治性前立腺腺癌)、膵臓腺癌、乳癌、結腸癌、肺癌(例えば非小細胞肺癌)、食道癌、頭頸部の扁平上皮癌、肝臓癌、卵巣癌、子宮頸癌、甲状腺癌、神経膠芽腫、神経膠腫、白血病、リンパ腫および他の腫瘍性悪性疾患が挙げられる。追加的に、本発明は、本発明の抗体を使用して増殖が抑制されうる難治性または再発性悪性疾患を含む。
本発明の抗体または抗体断片は、感染症および感染性疾患を予防または治療するためにも使用されうる。抗体または抗体断片は、病原体、毒素および自己抗原への免疫応答を刺激するために、単独でまたはワクチンとの組合せで使用されうる。抗体またはその抗原結合断片は、非限定的にヒト免疫不全ウイルス、肝炎ウイルスクラスA、BおよびC、エプスタインバーウイルス(Eppstein Barr virus)、ヒト(hyman)サイトメガロウイルス、ヒトパピローマウイルス、ヘルペスウイルスなどの、ヒトに感染性のウイルスへの免疫応答を刺激するために使用されうる。抗体またはその抗原結合断片は、細菌性または真菌性寄生生物および他の病原体での感染への免疫応答を刺激するために使用されうる。
本発明の抗体または抗体断片は、他の組換えタンパク質および/またはペプチド(腫瘍抗原または癌細胞など)と結合してこれらのタンパク質への免疫応答を増大させるために(すなわちワクチン接種手順において)使用されうる。
本発明の抗PD−1抗体および抗体断片は、喘息およびアレルギーなどのTh2介在性疾患を治療するためにも使用されうる。これは、本発明の抗体がTh1応答の誘発を支援できるという発見に基づく。したがって本発明の抗体は、より(mofre)バランスのとれた免疫応答を作り出すためにTh2介在性疾患において使用されうる。
本発明の抗体および抗原断片は、抗原特異的T細胞のex vivo活性化および増殖、ならびに腫瘍に対する抗原特異的T細胞を増加させるためのこれらの細胞のレシピエントへの養子移入のためにも使用されうる。これらの方法は、CMVなどの感染性物質へのT細胞応答を活性化させるためにも使用されうる。抗PD−1抗体の存在下でのex vivo活性化は、養子移入されたT細胞の頻度および活性を増大させることが期待されうる。
既に記載されたとおり本発明の抗PD−1抗体は、1つまたは複数の他の治療剤、例えば細胞傷害性剤、放射毒性剤または免疫抑制剤と同時投与されうる。抗体は、該薬剤(免疫複合体として)と結合されうるか、または該薬剤とは別に投与されうる。後者の場合(別々の投与)、抗体は該薬剤の前、後もしくは同時に投与されることができ、または他の既知の療法と同時投与されうる。
非治療用使用についての抗PD−1抗体の市場は、San Diego、Clifornia、USAのeBioscienceによって販売されている、フローサイトメトリー分析、免疫組織化学およびin vitro機能アッセイにおける使用のためのJ116およびJ105モノクローナル抗hPD−1抗体、ならびにMinneapolis、MN、USAのR&D Systemsによって販売されている、フローサイトメトリー、ウェスタンブロットおよびELISAにおける使用のためのmab1086、モノクローナル抗hPD−1抗体、の商業的販売によって示されるとおり既に存在する。本発明の抗体は、J116、J105および/またはMab1086によって現在果たされている任意の非治療用目的のために使用されうる。
抗体は、in vivo診断アッセイのためにも使用されうる。一般に抗体は、放射性核種(111In、99Tc、4C、3H、125I、3H、32P35Sまたは18Fなど)で標識して、免疫シンチグラフィー(immunoscintiography)、または陽電子放出断層撮影を使用して、抗原またはそれを発現する細胞を限局化し得る。
ヒト化抗体h409A11、h409A16およびh409A17の重鎖および軽鎖の可変領域をコードするDNA構築物は、American Type Culture Collection Patent Depository(10801 University Blvd.、Manassas、VA)に寄託されている。h409A−11、h409A−16およびh409A−17の重鎖をコードするDNAを含有するプラスミドは、2008年6月9日に寄託され、081469_SPD−Hと認定された。h409A11の軽鎖をコードするDNAを含有するプラスミドは、2008年6月9日に寄託され、0801470_SPD−L−11と認定された。h409A16の軽鎖をコードするDNAを含有するプラスミドは、2008年6月9日に寄託され、0801471_SPD−L−16と認定された。h409A17の軽鎖をコードするDNAを含有するプラスミドは、2008年6月9日に寄託され、0801472_SPD−L−17と指定された。寄託は、特許手続きのための微生物寄託の国際認識に関するブダペスト条約の規定およびその規則(ブダペスト条約)に基づいて行われた。
抗PD−1抗体の免疫化および選択
hPD−1cDNAでのマウスの免疫化
ヒトPD−1(「hPD−1」)受容体に対する抗体を生成するために、hPD−1受容体のオープンリーディングフレームをコードするcDNAをPCRによって得て、ベクターpcDNA3.1(Invitrogen、Carlsbad、CA)にサブクローン化した。次にCHO−K1細胞をhPD−1で安定に形質移入し、発現をフローサイトメトリーを使用してモニターした。ヒトPD−1を膜上に発現するCHO−K1クローンを単離し、CHO−hPD1と名付けた。
抗ヒトPD−1抗体産生B細胞クローンを選択するために、hPD−1 DNA免疫化マウス、すなわちマウス730、731および738(表1を参照されたい)由来の赤血球除去脾臓細胞2×107個をB細胞培養のためにプールした。脾臓細胞をDMEM/HAM’s F12/10%子ウシ血清(Hyclone、Logan、UT、USA)で37℃、1時間、プラスチック培養フラスコ中で単球を除くためにインキュベートした。非接着細胞を1回のCHO−K1細胞でのネガティブパニング、続いてCHO−hPD1細胞でのポジティブパニングにかけた。両方の選択手順は、21cm2ペトリ皿またはT25培養フラスコでコンフルエントに増殖した培養物において37℃、1時間実施した(細胞培養物は使用前に合計線量2000RADまで照射した)。ポジティブパニング後、未結合細胞を、0.132%CaCl2.2H2Oおよび0.1%MgCl2.6H2Oを補充したPBSでの10回洗浄によって除去した。最後に結合性B細胞をトリプシン処理によって回収した。
マウス抗PD−1抗体の精製および特徴付け
抗PD−1産生ハイブリドーマの安定化および抗PD−1抗体の精製
クローン細胞集団を各ハイブリドーマから、それらを複数回(>4)の限界希釈にさらすことによって得た。次いで安定なハイブリドーマを無血清条件でCELLineバイオリアクター(Integra−biosciences)を使用して6から8日間培養した。細胞を内側の容器の無血清培地中に1mLあたり細胞3×106個の密度で15mLに蒔き、およそ1mLあたり細胞4×107個に8日間かけて増殖させた。外側の容器を10%までのBCS(仔ウシ血清)で補充した培地で満たした。6日目から8日目に、内側の容器の培養物を回収し、15mL SF培地で洗浄し、ハイブリドーマと再播種した。バイオリアクター上清および洗浄液を合わせ、遠心分離で澄ませた。得られた上清を0.22μM濾過膜で濾過した。抗体精製のために、上清を1:1で高塩濃度の結合緩衝液(1M グリシン/2M NaCl、pH9.0)に希釈し、mAbをプロテインG HiTrap 5mLカラム(GEhealthcare)を使用して精製した。PBSで洗浄後、結合抗体を0.1Mグリシン pH=2.7を使用して溶出し、3M Trisを使用するpH中和が続いた。最後に緩衝液をPD−10ゲル濾過カラム(GEhealthcare)を使用してPBSに交換し、抗体をUltra−15遠心濃縮器(Amicon)を使用して濃縮し、分光光度法を使用して定量した。
以下の市販の抗体を本明細書に記載の種々の研究において使用した:抗PD−1抗体クローンJ116(#14−9989)はeBioscienceから購入した。抗CTLA−4クローン14D3(mAb 16−1529)はeBioscienceから購入した。抗PD−1クローン192106(mAb1086)はR&D systemsから購入した(#mAb1086)。アイソタイプ対照抗体mIgG1、κ、クローンMOPC21はSigmaから購入した(#M9269)。アイソタイプ対照mIgG1κ(mAb 16−4714)およびIgG2aκ(mAb 16−4724)はeBioscienceから購入した。
タンパク質に基づく、および細胞に基づくELISA(「CELISA」)実験を見かけの結合親和性(EC50値として報告される)を決定するために使用した。場合により、抗PD−1抗体の結合を市販の抗PD−1抗体J116(eBioscience)およびMab1086(R&D systems)のそれと比較した。
抗体の結合特性をさらに特徴付けるために、それぞれをOctet system(ForteBio、Menlo Park、CA)での生物光学干渉法を使用して概要を示し、結合動態を明らかにし、および平衡結合定数を算出した。このアッセイは、PD−1Fc融合タンパク質(R&D systems)の、標準的アミン化学を使用するアミン反応性バイオセンサー(Fortebio)へのカップリングによって実施された。次いで抗PD−1mAbのバイオセンサーへの結合およびバイオセンサーからの解離を種々の抗体濃度で観察した。具体的には、アミン反応性バイオセンサーを、0.1M MES pH=5.5を含むウェルに5分間浸漬することによって予め湿らせた。次いでバイオセンサーを0.1M NHS/0.4M EDC混合物を5分間使用して活性化した。PD−1/Fc融合タンパク質(R&D systems)を、バイオセンサーを0.1M MES中の12μg/mL PD−1/Fcの溶液に7.5分間浸漬することによってカップリングさせた。バイオセンサーの表面を1Mエタノールアミン溶液を5分間使用してクエンチさせた。バイオセンサーをPBS中に5分間、平衡化させた。抗PD−1mAbの会合を、種々の抗体濃度(PBS中、10〜80nM精製抗体>99% SDS−PAGEによる)を含むウェル中にバイオセンサーを置き、干渉(interferometry)を30分間モニターすることによって観察した。解離は、バイオセンサーをPBS中に移し、干渉シグナルを60分間モニターした後に測定した。観察された会合速度および解離速度(kobsおよびkd)を、検査した全ての濃度を含む1:1結合の包括的フィットモデルを使用して適合させ、平衡結合定数KDを算出した。動態研究からの結果を表IIおよび下の図6に示す。
フローサイトメトリーを使用して研究したリガンド結合の遮断。ヒトPD−1を発現するCHO細胞を接着培養フラスコから解離させ、種々の濃度の抗PD−1抗体、および一定濃度(600ng/mL)の未標識hPD−L1/Fcまたは組換えヒトPD−L2/Fc融合タンパク質(どちらもR&D Systemsから)と96ウェルプレートで混合した。混合物を30分間氷上で平衡化させ、FACS緩衝液(1%BCSおよび0.1%アジ化ナトリウムを含有するPBS)で3回洗浄し、FITC標識ヤギ抗ヒトFcとさらに15分間、氷上でインキュベートした。細胞を再びFACS緩衝液で洗浄し、フローサイトメトリーによって分析した。データを非線形回帰を使用するPrism(GraphPad Software、San Diego、CA)で分析し、IC50値を算出した。
リガンド遮断は、蛍光比色微量容積アッセイ(fluorometric microvolume assay)技術(FMAT)を使用する同質的競合アッセイおよび検出を使用して確認された。簡潔には、CHO.hPD−1を接着培養フラスコから解離させ、種々の濃度の抗PD−1抗体および一定濃度(600ng/mL)のhPD−L1/FcまたはhPD−L2/Fc融合タンパク質(どちらもR&D Systemsから)と混合し、96ウェルプレート中で蛍光色素(AlexaFluor647、Invitrogen)で標識した。混合物を90分間、37℃で平衡化させ、AB8200Cellular Detection Analyzer(Applied Biosystems、Foster City、CA)を使用して読み取った。データは非線形回帰を使用するPrism(GraphPad Software、San Diego、CA)で分析し、IC50値を算出した。図3は、リガンド遮断の程度は抗体濃度によって決定されることを示す用量応答実験の結果を示す。hPD−L1/FcおよびhPD−L2/Fcの両方のCHO−hPD−1細胞への結合は、hPD−1.08A、hPD−1.09Aおよび(より少ない程度で)J116によって用量依存的な様式で完全に抑制されうる。算出されたIC50データを表IIにまとめる。フローサイトメトリーを使用して得られた結果を確認して、高親和性抗体hPD−1.08AおよびhPD−1.09Aは、PD−L1結合を1nMより低いIC50値で抑制した。
抗体の種の交差反応性を評価するために、マウスおよびcynomolgus macaque PD−1受容体をPCRによってクローン化し、安定に形質移入したCHO−K1細胞を作製した。抗体をカニクイザル受容体への結合についてCELISAを使用して検査した。市販の抗体J116、hPD−1.08AおよびhPD−1.09Aは、ヒトおよびカニクイザルPD−1に同等な親和性で結合し、hPD−L1/FcおよびhPD−L2/FcのカニクイザルPD−1への結合をヒトPD−1と比較して同様の有効性で遮断することが見いだされた。カニクイザルPD−1の細胞外部分のアミノ酸配列がヒトPF−1のそれと97%同一であることが見いだされたことから、これは驚くべきことではない。cynomolgous macaque由来のPD−1に加えて、hPD−1.08AおよびhPD−1.09Aは、rhesus macaques由来のPD−1も実施例3に記載のSEM刺激血液細胞培養物中で機能的に遮断した。検査した抗体で、使用したいずれのアッセイにおいても検出可能な親和性でマウスPD−1に結合したものはなかった。
抗PD−1抗体の機能的プロファイリング
SEBへのヒトT細胞応答は、hPD−1.08AおよびhPD−1.09Aによって増強される。
SEB刺激血液細胞がPD−1の増強された発現をフローサイトメトリーで示したことから、これらの細胞を、hPD−1.09Aが組織学的使用のためのホルマリン固定パラフィン包埋組織においてPD−1を検出できるかどうかを決定するために使用した。ヒトドナー末梢血単核球を、0.1μg/mL SEBで3日間刺激し、その後非接着細胞(主にリンパ球)を回収し、PBSで2回洗浄し、遠心分離(1100rpm、5分間)した。細胞を10分間、4%ホルムアルデヒドで固定し、細胞沈渣をアガロースに包埋し、エタノール(70%、80%、96%および100%と続いて)およびキシレン中で脱水し、その後パラフィンに包埋した。切片(4μm)をガラススライドにマウントし、水和させ(キシレン、エタノール100%、96%、80%、70%、PBS緩衝液)、その後加熱したクエン酸緩衝液への抗原回収を標準的方法を使用して実施した。ペルオキシダーゼ活性を0.3%H2O2を含む100%メタノールを使用して遮断し、スライドを水およびPBS、0.1%Tweenでリンスした。切片をhPD−1.09Aと1.5時間、室温でインキュベートし、PBS−Tweenでリンスし、標準的検出法が続いた。スライドをヘマトキシリンで30秒間、室温で対比染色し、キシレンで脱水し、マウントして顕微鏡検査した。これらの実験は、SEB刺激PBCM培養物由来のリンパ球は、未刺激のPBMC培養物とは対照的に、hPD−1.09Aで(アイソタイプ対照と比較した場合)強く染まり、hPD−1.09Aが診断試薬として有用であることを示した。
抗PD−1抗体配列および続くヒト化
免疫グロブリンcDNAのクローニング
縮重プライマーPCRに基づく方法を使用して、ハイブリドーマhPD−1.08AおよびhPD−1.09Aによって発現されるマウス抗体の可変領域をコードするDNA配列を決定した。簡潔には、重鎖および軽鎖についての遺伝子特異的cDNAをiScript Select cDNA合成キット(Biorad #1708896)を製造者の説明書に従って使用して生成した。使用したPCRプライマーは、Ig−プライマーセット(Novagen #69831−3)に基づいた。縮重PCR反応は、TaqポリメラーゼをNovagenプライマーセット手順書に従って使用して実施した。PCR産物をアガロースゲル電気泳動によって分析した。重鎖および軽鎖の可変領域の両方について予測される増幅産物サイズは、約500塩基対である。適切なバンドをもたらした反応からのTaq−増幅PCR産物2μlをpCR4 TOPOベクター(Invitrogen #K4595−40)にクローン化し、DH5−αE.coliに製造者による指示のとおり形質転換した。クローンをユニバーサルM13順方向および逆方向プライマーを使用してコロニーPCRによって選別し、各反応から2から3クローンをDNA配列分析用に選択した。
キメラ軽鎖および重鎖を、マウスhPD−1.09A VLおよびVH領域のPCRでクローン化したcDNAをヒトκおよびIgG1定常領域にそれぞれ連結することによって構築した。マウスcDNA配列の5’および3’末端を、各鎖に適切なリーダー配列および既存の組換え抗体発現ベクターへのクローニングを可能にする制限部位を付加するために設計したPCRプライマーを使用して改変した。
hPD−1.09A抗体をMRCT(Cambridge UK)によりCDR移植技術を使用してヒト化した(例えば、米国特許第5,225,539号を参照されたい)。簡潔には、マウス抗体hPD−1.09Aの可変鎖配列をResearch Collaboratory for Structural Bioinformatics(RCSB)タンパク質データバンクにおいて入手可能な配列と比較した。hPD−1.09Aの相同性モデルを最も近いVHおよびVK構造に基づいて生成した。hPD−1.09Aに最も高い同一性を有するヒト配列を同定し、分析した(Foote and Winter、J. Mol. Biol. 224巻:487〜499頁(1992年);Morea V.ら、Methods 20巻:267〜270頁(2000年);Chothia C.ら、J. Mol. Biol. 186巻:651〜663頁(1985年))。CDR移植重鎖および軽鎖を構築するために最も適切なヒトフレームワークを同定した。
ヒト化抗PD−1抗体の結合特性および機能特性
産生および精製
ヒト化抗体h409A11、h409A16およびh409A17をCHO−S細胞の一過的形質移入によって産生させた。細胞をCD−CHO(Gibco)およびC5467培地(Sigma)で8日間、振盪フラスコ中で増殖させた。抗体をプロテインAクロマトグラフィーによって細胞上清から精製し、洗浄し、1M酢酸を使用して溶出し、3M Trisを使用して中和した。最後に緩衝液を、1M Tris塩基でpH5.5に調整した100mM酢酸に交換した。
見かけの結合親和性を決定するために(EC50値として報告される)タンパク質に基づく、および細胞に基づくELISAを実施例2に記載のとおり実施した。ヒト化抗PD−1抗体は、PD−1/Fcおよび細胞で発現されるPD−1にマウス親抗体に匹敵するEC50値でそれぞれ結合した(表V)。
PD−L1およびPD−L2のPD−1への結合を遮断するヒト化抗体の能力を、実施例2に記載のとおりFMAT競合アッセイを使用する同質的競合アッセイおよび検出を使用して測定した。
Claims (16)
- 配列番号15、16および17の軽鎖CDR、ならびに
配列番号18、19および20の重鎖CDR
を含む、ヒトPD−1に結合する単離された抗体または抗体断片。 - a.i.配列番号7、および
ii.配列番号30のアミノ酸残基20から139
からなる群から選択されるアミノ酸配列を含む重鎖可変領域
を含み、
b.i.配列番号8、
ii.配列番号32のアミノ酸残基20から130、
iii.配列番号33のアミノ酸残基20から130、および
iv.配列番号34のアミノ酸残基20から130
からなる群から選択されるアミノ酸配列を含む軽鎖可変領域
をさらに含む、請求項1に記載の抗体または抗体断片。 - a.i.配列番号31のアミノ酸残基20から466、および
ii.配列番号35のアミノ酸残基20から469
からなる群から選択されるアミノ酸配列を含む重鎖、
ならびに
b.i.配列番号36のアミノ酸残基20から237、
ii.配列番号37のアミノ酸残基20から237、および
iii.配列番号38のアミノ酸残基20から237
からなる群から選択されるアミノ酸配列を含む軽鎖
を含む、請求項1に記載の抗体。 - (i)γ4もしくはγ1ヒト重鎖定常領域、および
(ii)ヒトκ軽鎖定常領域
をさらに含む、請求項1から3のいずれか一項に記載の抗体または抗体断片。 - a.キメラ抗体もしくはその断片、
b.ヒト化抗体もしくはその断片、または
c.Fab、Fab’、Fab’−SH、Fv、scFv、F(ab’)2およびダイアボディーからなる群から選択される抗体断片
である、請求項1から4のいずれか一項に記載の抗体または抗体断片。 - T細胞の活性化を増大させる、請求項1から5のいずれか一項に記載の抗体または抗体断片。
- 配列番号31のアミノ酸残基20から466を含む重鎖および配列番号36のアミノ酸残基20から237を含む軽鎖を含む抗体。
- 請求項1から7のいずれか一項に記載の抗体または抗体断片をコードする単離されたポリヌクレオチド。
- 配列番号23および配列番号27を含む、請求項8に記載の単離されたポリヌクレオチド。
- 請求項8または9に記載の単離されたポリヌクレオチドを含む発現ベクター。
- 請求項10に記載の発現ベクターを含む単離された宿主細胞。
- a.前記核酸配列が発現される条件下で、培地中で請求項11に記載の宿主細胞を培養し、それにより前記軽鎖および前記重鎖可変領域を含むポリペプチドを産生するステップと、
b.該宿主細胞または該培地から該ポリペプチドを回収するステップと
を含む、請求項1から7のいずれか一項に記載の抗体または抗体断片を産生する方法。 - 薬学的に許容される担体または希釈剤と組み合わせて、請求項1から7のいずれか一項に記載の抗体または抗体断片を含む組成物。
- 癌の治療のため、または感染症もしくは感染性疾患の治療のための、請求項13に記載の組成物。
- 請求項14に記載の組成物であって、前記抗体が、配列番号31のアミノ酸残基20から466を含む重鎖および配列番号36のアミノ酸残基20から327を含む軽鎖を含み、該組成物が癌の治療のためのものである、組成物。
- 癌を治療するための、または感染症もしくは感染性疾患を治療するための薬剤の調製のための、請求項1から7のいずれか一項に記載の抗体または抗体断片の使用。
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