JP2019533989A - 抗pd−1(cd279)抗体 - Google Patents
抗pd−1(cd279)抗体 Download PDFInfo
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- JP2019533989A JP2019533989A JP2019512990A JP2019512990A JP2019533989A JP 2019533989 A JP2019533989 A JP 2019533989A JP 2019512990 A JP2019512990 A JP 2019512990A JP 2019512990 A JP2019512990 A JP 2019512990A JP 2019533989 A JP2019533989 A JP 2019533989A
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Abstract
Description
本出願は、2016年9月14日に出願された米国仮出願第62/394,314号の、35U.S.C.119(e)下の利益を主張し、その内容は、参照によりその全体が本明細書に組み込まれる。
本出願は、ASCII形式で電子的に提出された配列表を含み、参照によりその全体が本明細書に組み込まれる。2017年8月10日に作成されたこのASCIIコピーは、381493−327WO_SL.txtという名称であり、サイズは33,195バイトである。
本出願は、とりわけ、新規抗PD−1抗体、新たな抗体を含む組成物、該抗体をコードする核酸並びにそれらを作製及び使用する方法に関する。
がん療法は、手術、放射線、及び化学療法を含む広範な治療アプローチを含む。様々なアプローチが、がんを治療するために医師に利用可能である治療の幅広い選択を可能にするが、既存の治療剤は、正常な健康細胞よりもがん細胞を標的とする選択性の欠如、治療に対してがんにより耐性が生じることなどの、多数の不利益を与える。
5.要旨
本開示は、PD−1に特異的に結合する抗PD−1抗体及びその結合断片を提供する。例示的なCDRのアミノ酸配列並びに例示的な抗PD−1抗体の重鎖及び軽鎖のVH及びVL領域のアミノ酸配列は、下記の詳細な説明において提供されている。本明細書で提供される、PD−1受容体とそのリガンドのいずれか(PD−L1、配列番号3;PD−L2、配列番号4)との相互作用を妨げる抗体は、負のシグナル伝達の阻害及び適応免疫応答の上方制御をもたらす。
本開示は、PD−1に特異的に結合する抗体及び断片、該抗体を含む組成物、抗PD−1抗体をコードするポリヌクレオチド、該抗体を産生することができる宿主細胞、該抗体及び結合断片を作製するために有用な方法及び組成物並びにそれらを使用する様々な方法に関する。
本明細書に記載されている抗体、結合断片及びポリヌクレオチドは、多数の実施形態において、それぞれのポリペプチド配列又はポリヌクレオチド配列によって記載されている。別段に示されない限り、ポリペプチド配列はN→C配向で提供されている;ポリヌクレオチド配列は5’→3’配向で提供されている。ポリペプチド配列について、以下の表1に示すように、遺伝的にコードされたアミノ酸の通常の3文字略語又は1文字略語を使用することができる。
本明細書において別段に定義されない限り、本開示に関連して使用される科学用語及び技術用語は、当業者によって一般的に理解される意味を有するものとする。
一態様において、本開示は、プログラム細胞死タンパク質1(PD−1)受容体(PDCD1、CD279、PD1、SLEB2又はSLE1としても知られる)に特異的に結合する抗体及び/又はその結合断片に関する。
Ki=IC50/(1+[参照Ab濃度]/Kd)
に従って計算され、IC50は、参照抗体の結合の50%減少をもたらす試験抗体の濃度であり、Kdは、ヒトPD−1に対する参照抗体の親和性の尺度である、参照抗体の解離定数である。本明細書に開示される抗PD−1抗体と競合する抗体は、本明細書に記載されるアッセイ条件下で10pM〜10nMのKiを有することができる。
本開示は、抗PD−1抗体の免疫グロブリン軽鎖及び重鎖遺伝子をコードする核酸分子、そのような核酸を含むベクター並びに本開示の抗PD−1抗体を生成することができる宿主細胞を包含する。
本明細書に記載されている抗PD−1抗体は、抗体、並びに1つ以上の担体、賦形剤及び/又は希釈剤を含む組成物の形態であってもよい。組成物は、獣医学的使用又はヒトにおける薬学的使用のような、特定の使用のために製剤化され得る。組成物の形態(例えば、乾燥粉末、液体製剤など)、並びに使用される賦形剤、希釈剤及び/又は担体は、抗体の意図された使用、及び治療的使用については、投与様式に依存する。
7.6.1. 治療上の利益
本明細書において提供されるデータは、本開示の抗PD−1抗体が、がん細胞の存在下でPD−1に拮抗し、インビボで固形腫瘍又は血液悪性腫瘍などのがんに対して強力な抗腫瘍活性を発揮することを実証する。したがって、抗PD−1抗体、結合断片及び/又は抗PD−1抗体を含む医薬組成物は、固形腫瘍又は血液悪性腫瘍を処置するために治療的に使用することができる。
抗PD−1抗体は、抗がん特性を有する他の薬剤若しくは治療に対して補助的に又はそれとともに使用することができる。補助的に使用される場合、抗PD−1及び他の薬剤(単数又は複数)は、単一の組合せ医薬製剤に一緒に製剤化されてもよく、又は単一の協調された投与レジメン若しくは異なる投薬レジメンのいずれかで個別に製剤化及び投与されてもよい。抗PD−1抗体に補助的に又は抗PD−1抗体とともに投与される薬剤は、典型的には、抗PD−1抗体に対して相補的な活性を有し、そのため、抗体及び他の薬剤が互いに悪影響を及ぼさない。
投与される抗PD−1抗体の量は、様々な因子に依存し、例えば、限定されないが、治療される固形腫瘍の特定のタイプ、治療される固形腫瘍のステージ、投与様式、投与頻度、所望の治療上の利益、並びに患者の年齢、体重及び他の特徴など他のパラメータなどが挙げられる。特定の投与様式及び投与頻度について治療上の利益を与えるのに有効な投薬量の決定は、当業者の能力の範囲内である。
以下は、本開示の例示的な列挙される実施形態である。
本明細書に記載される抗PD−1抗体の実施形態の特定の特徴及び特性を強調する以下の実施例は、限定ではなく説明の目的で与えられる。
8.1.1.ELISAによるヒトPD−1結合プレートへの抗体結合
Immunolon 4xHB 96ウエルプレートを、1ug/mlのヒトPD−1 Fc融合体と4℃で一晩コーティングした。プレートを、1%BSAを含有するPBSで室温において30分間ブロッキングし、次いでプレートウォッシャーを使用して0.1%Tween20を含有するPBS(PBST)で3回洗浄した。PD−1でコーティングされたプレートを、次いで、指示された濃度の抗体と室温(RT)で1時間インキュベートした。プレートをPBSTで4回洗浄し、次いで、1%BSAを含有するPBS中1:5000の希釈液に調製した100μLのヤギ抗ヒトFab断片特異的ビオチンと室温で1時間インキュベートした。プレートをPBSTで5回洗浄し、100μLのストレプトアビジン−HRPの1:1000希釈液をそれぞれのウエルに加え、室温において30分間インキュベートした。プレートをPBSTで5回洗浄し、100μLのTMB One Componentをそれぞれのウエルに加え、発色するまで室温においてインキュベートした(約5〜10分)。光学濃度(OD)を、Spectromax190(Molecular Devices)を使用して650nmで読み取った。
PD−1発現Jurkat細胞をフラスコから採取し、1%BSAを含有するPBS中2×106細胞/mLに再懸濁した。100μLの細胞を、100μLの滴定試験抗体又はアイソタイプ対照を含有する丸底96ウエルプレートに加えた。細胞を、抗体と室温で25分間インキュベートし、次いで1%BSAを含有するPBSで2回洗浄した。細胞ペレットを、100μLの1:250希釈二次抗体ヤギ抗ヒトFab PEに再懸濁した。室温で25分間インキュベーションした後、1%BSAを含有するPBSで細胞を2回洗浄し、200μLの1%BSAで再懸濁した。細胞を、Becton Dickinson FACSCantoフローサイトメーターを使用して分析した。データを、BD FACSDivaソフトウェア(バージョン8.0.1)を使用して分析した。
Immunolon 4xHB 96ウエルプレートを、DPBS中1μg/mLのカニクイザルPD−1 Fc融合体を用いて4℃で一晩コーティングした。プレートを、1%BSAを含有するPBSを用いて室温で30分間ブロッキングし、次いでプレートウォッシャーを使用してPBST(PBS Tween20 0.1%)で3回洗浄した。PD−1でコーティングされたプレートを、次いで、指示された濃度の抗体と室温で1時間インキュベートした。プレートをPBSTで4回洗浄し、次いで、1%BSAを含有するPBS中1:5000の希釈液に調製した100μLのヤギ抗ヒトFab断片特異的ビオチンと室温で1時間インキュベートした。プレートをPBSTで5回洗浄し、100μLのストレプトアビジン−HRPの1:1000希釈液をそれぞれのウエルに加え、室温で30分間インキュベートした。その後、プレートをPBST及び100μLのTMBで5回洗浄した。一成分をそれぞれのウエルに加え、発色するまで室温においてインキュベートした(約5〜10分)。光学濃度(OD)を、Spectromax190(Molecular Devices)を使用して650nmで読み取った。
ヒト末梢血単核細胞(PBMC)は、Stanford Blood Center(Palo Alto、CA)から購入したバフィーコートから単離した。簡単に述べると、バフィーコートを、マグネシウム及びカルシウム無しのPBSと1:1の比で希釈した。希釈した血液(30mL)を、SepMateチューブに含まれたマグネシウム及びカルシウム無しのPBSで調製した15mLの90%Ficoll−Paque Plus上で層状にした。チューブを1200gで10分間、遠心分離した。中間相を回収し、1×PBSで2回洗浄した。PBMCを、1μg/mLのPHA及び50U/mLの組換えヒトIL−2を有する10%HI FCSを含有するRPMI培地中で48時間2×106細胞/mLで培養した。細胞を回収し、洗浄し、抗体と室温で25分間インキュベートした。標識された細胞を、1%BSAを含有するPBSで2回洗浄した。細胞を100μLのPBS+1%BSAに再懸濁し、PEコンジュゲートヤギ抗ヒトFab断片の1:250希釈液及び抗CD4−FITCを加えた。30分後、1%BSAを含有するPBSで細胞を2回洗浄し、200μLの1%BSAで再懸濁した。細胞を、Becton Dickinson FACSCantoフローサイトメーターを使用して分析した。データを、BD FACSDivaソフトウェア(バージョン8.0.1)を使用して分析した。
組換え可溶性PD−1 ECD(細胞外ドメイン)に対する抗PD−1抗体の結合動態を、抗Fc捕捉アッセイアプローチを使用して25℃でBiacore T200機器でなされた表面プラズモン共鳴に基づく測定によって決定した。ヒトPD−1(残基1〜167)及びカニクイザルPD−1(残基21〜167)の組換え細胞外ドメインは、商業的供給源から購入し、10mMのHEPES、pH7.4、150mMのNaCl、3mMのEDTA中でのゲル濾過によってさらに精製した。チップの調製及び結合動態の測定は、アッセイバッファーHBS−EP+(10mMのHEPES、pH7.4、150mMのNaCl、3mMのEDTA、0.05%のTween20)中で行った。抗Fc捕捉チップ調製のために、10mMの酢酸ナトリウム(pH4.5)中25μg/mLに希釈した約2000RUのヤギ抗ヒトIgG Fcポリクローナル抗体を、標準的なアミンカップリングキットを使用して、製造業者の教示及び手順に従ってCM5バイオセンサーチップの全面に直接固定した。バイオセンサー表面の未反応部分を、エタノールアミンでブロッキングした。結合動力学的測定のために、各アッセイサイクルは、(1)試験表面のみで試験抗体を捕捉するステップ;(2)参照及び試験表面の両方に80μL/分で240μLの検体注入(PD−1 ECD又はバッファーのみ)を行い、その後、解離を80μL/分で900秒間モニタリングするステップ;及び(3)参照及び試験表面の両方に10mMのグリシン塩酸塩、pH1.5を注入することにより捕捉表面を再生するステップを含む。アッセイ中、全ての測定を、捕捉表面のみ(つまり、捕捉試験抗体無し)及びバッファーのみの注射に対して参照させ、二重参照のために使用した。PD−1注射は、無作為化3倍希釈系列で900nM〜11.1nMの濃度範囲であった。データを処理し、Biacore T200 Evaluationソフトウェアを使用して1:1結合モデルに全体的に適合させ、結合動力学的速度定数ka(M−1・秒−1)及びkd(秒−1)及び平衡解離定数KD(M)を決定した。
ヒトPD−1発現HEK293G細胞を、コンフルエントなフラスコから採取した。細胞を、2×106細胞/mLの濃度でPBS中に再懸濁した。細胞(1×105)を96ウエルV底プレートの各ウエルに加え、ヒトFcRブロックを使用して4℃で15分間、細胞をブロッキングした。別のプレートでは、試験抗体及びアイソタイプ対照溶液を20μg/mLの出発濃度の3倍連続希釈を使用して調製した。細胞を1×PBSで洗浄し、50μLの調製された抗体希釈液並びに50μLのPD−L1 Hisタグ化又はPD−L2 Hisタグ化リガンド(10μg/ml)を、細胞を含有するプレートに加えた。細胞を4℃で30分間インキュベートし、1×PBSで2回洗浄した。PBS中1:50希釈で調製した抗His APC抗体(50μL)を各ウエルに加え、4℃で30分間インキュベートした。細胞を2回洗浄し、PBS中に再懸濁し、LSR II Fortessa(BD Biosciences、San Jose、CA)上で取得した。
ヒトPBMCを、Stanford Blood Center(Palo Alto、CA)から購入したバフィーコートから単離した。簡単に述べると、バフィーコートを、マグネシウム及びカルシウム無しのPBSと1:1の比で希釈した。希釈した血液(30mL)を、SepMateチューブに含まれたマグネシウム及びカルシウム無しのPBSで調製した15mLの90%Ficoll−Paque Plus上で層状にした。チューブを1200gで10分間、遠心分離した。中間相を回収し、1×PBSで2回洗浄した。細胞を、ベータメルカプトエタノールを含有するAIM−V培地中1mLあたり1×108個で再懸濁した。樹状細胞(DC)を、T75フラスコ中で80ng/mLのGM−CSF及び50ng/mLのIL−4の存在下、プラスチック接着性のPBMCを7日間培養することによって誘導した。5日目に、50pg/mLのIL−1α及び200pg/mLのTNF−αをDC培養物に加えた。7日目に、DCをフラスコから採取し、414R/分で7.3分間照射し、完全培地(L グルタミン含有10%FBS、1×非必須ビタミン、1%Pen/Strep溶液、1%ピルビン酸ナトリウム、1%HEPESを有するRPMI)中1×105細胞/mLの最終濃度に再懸濁した。同種異系ヒトCD4 T細胞を、CD4 T細胞単離キットを使用して単離した。DC(1×104/ウエル)及び精製されたCD4 T細胞(1×105/ウエル)を、U底プレートに加えた。試験抗体又はアイソタイプ対照(10μg/mL)を、DC及びT細胞を含有するプレートに加えた。インキュベーションの5日後、上清を回収し、Milliplexサイトメトリービーズアレイキットを使用してIL−2及びIFN−γについて分析した。IFN−γを、BioRad Bioplex System(Bioplexマネージャー6.0)を使用して測定した。
ヒトPBMCを、先に記載されているようにStanford Blood Centerから購入したバフィーコートから単離した。細胞を、ベータメルカプトエタノールを含有するAIM−V培地中2×106細胞/mLの最終濃度に再懸濁した。PBMC(2×105)を、1ウエル当たり0.2μg/mLの破傷風トキソイドとともに使用した。抗体を滴定し、プレートを5日間インキュベートした。上清を5日目に収集し、Milliplex サイトメトリービーズアレイキットを使用してIFN−γについて評価した。IFN−γを、BioRad Bioplex System(Bioplexマネージャー6.0)を使用して測定した。
マウスを、当該技術分野で既知の方法により免疫化した(E.Harlow、D.Lane.Antibody: A Laboratory Manual、(Cold Spring Harbor Laboratory Press、Cold Spring Harbor、NY、1998))。各モノクローナル抗体のアイソタイプを、Mouse Isotypingキット(Roche)を使用して決定した。目的の抗体を産生するハイブリドーマクローンを精製し、さらに表面プラズモン共鳴及びリガンド競合(ELISA)によって親和性について特性決定した。
例示的な抗体の安定性を、酸化又は可変温度条件下で処置した後に抗体のPD−1の結合を測定することによって決定した。
下記の表4−1は、米国特許第9,073,994号で見出された手法に従って調製された文献記載の抗PD−1抗体ニボルマブと比較した例示的な抗体Hu12A11.2b4のインビトロ結合親和性データを示す。Hu12A11.2b4は、表面プラズモン共鳴、ヒト(Hu)若しくはカニクイザル(Cyno)PD−1を用いたELISAアッセイ又は実施例1のアッセイで測定されるようなヒトJurkat細胞において、ニボルマブと比較して、PD−1に対して同様の結合特性を示した。
Hu12A11.2b4を、実施例1に記載のいくつかのインビトロのヒト細胞アッセイで生物学的活性について評価した。表5−1に示されるように、Hu12A11.2b4は、CD4+ T細胞においてPD−1に対して180pMの結合を実証した。さらにHu12A11.2b4の抗PD−1活性は、フローサイトメトリーによって評価されるように、PD−1とのPD−L1又はPD−L2の相互作用をブロッキングするその能力によって少なくとも部分的に媒介されることが示された。この生物学的活性は、ヒトPD−1の構成的発現を有するNFAT応答エレメントの制御下にホタルルシフェラーゼ遺伝子を発現する組換えJurkat T細胞におけるHu12A11.2b4の活性と一致していた(Jurkat NFATアッセイ)。
Claims (25)
- (i)3つのCDRを含むVH鎖;及び(ii)3つのCDRを含むVL鎖を含む抗PD−1結合タンパク質であって、
VHCDR#1は、GYTFTHYGMN(配列番号11)であり、
VHCDR#2は、WVNTYTGEPTYADDFKG(配列番号12)であり、
VHCDR#3は、EGEGLGFGD(配列番号13)であり、
VLCDR#1は、RSSQSIVHSHGDTYLE(配列番号14)であり、
VLCDR#2は、KVSNRFS(配列番号15)であり、
VLCDR#3は、FQGSHIPVT(配列番号16)である、抗PD−1結合タンパク質。 - ヒト化されている、請求項1に記載の抗PD−1結合タンパク質。
- 配列番号36の配列に対応するVH鎖;及び配列番号42の配列に対応するVL鎖を含む、請求項2に記載の抗PD−1結合タンパク質。
- IgGである、請求項3に記載の抗PD−1結合タンパク質。
- IgG1である、請求項4に記載の抗PD−1結合タンパク質。
- アミノ酸置換L234A及びL235Aを有する変異体CH2ドメインを含む、請求項5に記載の抗PD−1結合タンパク質。
- IgG4である、請求項4に記載の抗PD−1結合タンパク質。
- アミノ酸置換S228Pを有する変異体Fc領域を含む、請求項7に記載の抗PD−1結合タンパク質。
- カッパ軽定常領域を含む、請求項3に記載の抗PD−1結合タンパク質。
- 配列番号51又は配列番号52の配列に対応する重鎖、及び配列番号61の配列に対応する軽鎖を含む、請求項3に記載の抗PD−1結合タンパク質。
- 約100nM未満のKDを有する、請求項1に記載の抗PD−1結合タンパク質。
- 約10nM未満のKDを有する、請求項11に記載の抗PD−1結合タンパク質。
- 請求項1に記載の抗PD−1結合タンパク質及び薬学的に許容される担体を含む医薬組成物。
- 抗PD−1結合タンパク質をコードするヌクレオチド配列を含む核酸であって、結合タンパク質は、(i)3つのCDRを含むVH鎖;及び(ii)3つのCDRを含むVL鎖を含み、ここで
VHCDR#1は、GYTFTHYGMN(配列番号11)であり、
VHCDR#2は、WVNTYTGEPTYADDFKG(配列番号12)であり、
VHCDR#3は、EGEGLGFGD(配列番号13)であり、
VLCDR#1は、RSSQSIVHSHGDTYLE(配列番号14)であり、
VLCDR#2は、KVSNRFS(配列番号15)であり、
VLCDR#3は、FQGSHIPVT(配列番号16)である、核酸。 - 請求項14に記載の核酸を含むベクター。
- 請求項15に記載のベクターで形質転換された原核宿主細胞。
- 請求項15に記載のベクターで形質転換された真核宿主細胞。
- 請求項14に記載の核酸を発現するように遺伝子操作された真核宿主細胞。
- 哺乳動物宿主細胞である、請求項18に記載の真核宿主細胞。
- 抗PD−1結合タンパク質を生成する方法であって、(a)請求項19に記載の宿主細胞を培養すること及び(b)抗PD−1結合タンパク質を回収することを含む、方法。
- 免疫系を活性化する方法であって、それを必要とする患者に、請求項18に記載の宿主細胞によって発現される抗PD−1結合タンパク質の有効量を投与することを含む、方法。
- がんを治療する方法であって、それを必要とする患者に、抗PD−1結合タンパク質の治療有効量を投与することを含み、結合タンパク質は、(i)3つのCDRを含むVH鎖;及び(ii)3つのCDRを含むVL鎖を含み、ここで
VHCDR#1は、GYTFTHYGMN(配列番号11)であり、
VHCDR#2は、WVNTYTGEPTYADDFKG(配列番号12)であり、
VHCDR#3は、EGEGLGFGD(配列番号13)であり、
VLCDR#1は、RSSQSIVHSHGDTYLE(配列番号14)であり、
VLCDR#2は、KVSNRFS(配列番号15)であり、及び
VLCDR#3は、FQGSHIPVT(配列番号16)である、方法。 - がんが、膀胱がん、乳がん、頭頸部がん、腎臓がん、肺がん、リンパ腫、黒色腫及び胃がんから選択される、請求項22に記載の方法。
- 肺がんが、非小細胞肺がんである、請求項23に記載の方法。
- 抗PD−1結合タンパク質が、静脈内投与される、請求項21に記載の方法。
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