JP2018523710A - ナノ粒子の細胞表面共役 - Google Patents
ナノ粒子の細胞表面共役 Download PDFInfo
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Abstract
Description
本発明は、国立衛生研究所から与えられた助成金番号R01 CA172164の下での政府支援で行われた。政府は、本発明において、特定の権利を有する。
本願は、米国仮特許出願第62/204,337号(2015年8月12日に出願)の優先権および利益を主張し、その全体の内容は、参照によって本明細書に取り込まれる。
いくつかの実施態様において、リガンドは抗CD45抗体である。いくつかの実施態様において、抗CD45抗体は、ヒト抗CD45抗体またはヒト化抗CD45抗体である。いくつかの実施態様において、抗CD45抗体は、抗CD45モノクローナル抗体である。いくつかの実施態様において、抗CD45モノクローナル抗体は、BC8、4B2、9.4およびGAP8.3からなる群から選択される。
いくつかの実施態様において、リガンドは、細胞表面共役受容体と結合する。
いくつかの実施態様において、リガンドは、細胞表面共役受容体と結合し、少なくとも50%(例えば、少なくとも60%、少なくとも70%、少なくとも80%、少なくとも90%または少なくとも95%)のリガンド(例えば、抗CD45抗体)が、少なくとも24時間(例えば、少なくとも36時間、または少なくとも48時間)、細胞表面上に残存する。
いくつかの実施態様において、ナノ粒子は、タンパク質ナノゲル、核酸ナノゲルおよび凝固ポリマー(solidified polymer)からなる群から選択される。
いくつかの実施態様において、ナノ構造体はリポソームである。いくつかの実施態様において、リポソームは、膜間架橋多重層ベシクル(interbilayer-crosslinked multilamellar vesicle;ICMV)または、単層ベシクルである。
いくつかの実施態様において、ナノ粒子はタンパク質ナノゲルである。いくつかの実施態様において、タンパク質ナノゲルは、担体を含まない、タンパク質ナノゲルである。
ある態様において、リガンドは抗CD45モノクローナル抗体である。
ある態様において、担体細胞は負に帯電した細胞膜を有し、ナノ構造体は細胞膜と静電的に相互作用するポリカチオン性表面を有する。ある態様において、ポリカチオンはポリリジンである。ある態様において、ポリカチオンは、ポリエチレングリコール−b−ポリリジン(PEG−PLL)である。
様々な実施態様において、薬剤を、全身投与後に、インビボで同様の効果を達成するのに必要な投与量より低い投与量で、用いてもよい。いくつかの例において、投与量は、必要とされる全身投与量の、少なくとも2分の1、少なくとも5分の1、少なくとも10分の1、少なくとも20分の1、少なくとも50分の1、または少なくとも100分の1である。
本開示は、その適用において、以下で記述され、または図において説明される、構成の詳細および/または構成要素の配置に限定されない。
本開示のナノ構造体は、一般的に、1000nm未満(例えば、500nm未満、250nm未満、100nm未満)の、少なくとも1つの寸法を有する微細粒子である。用語「ナノ構造体」は、本明細書に記載されるリポソームおよびナノ粒子を包含する。いくつかの実施態様において、ナノ構造体は合成物質である。すなわち、ナノ構造体は天然に存在しない。
用語「ナノ粒子」は、ナノゲル(例えば、タンパク質ナノゲルおよび核酸ナノゲル)、固体コロイドナノ粒子、磁性ナノ粒子、新規(nobel)金属ナノ粒子、半導体ナノ粒子、多様式ナノ粒子、複合ナノ粒子および、生物医学的応用に典型的に用いられる他のナノ粒子(例えば、Blanco-Andujar et al. Annu. Rep. Prog. Chem., Sect. A, 2010, 106, 553-568参照、これは参照によって本明細書に組み込まれる)を含む。しかしながら、用語「ナノ粒子」は、ウイルスもしくはウイルス粒子またはリポソームを包含せず、いくつかの実施態様において、ウイルス遺伝物質を含まない非感染性ウイルス様粒子(VLP)が本明細書において想定されることが理解されるはずである。したがって、いくつかの実施態様において、組成物は、細胞表面と共役するVLPを含む。ナノ粒子は、フィルムまたは他の構造的に層状のポリマーマトリックスとは区別される。
いくつかの実施態様において、ナノ粒子はナノゲル(タンパク質ナノゲルまたは核酸ナノゲルなど)である。ナノゲルは、例えば、ナノスケールサイズの、化学的または物理的に架橋されたポリマーネットワークによって形成される粒子を含むハイドロゲルで構成され得る。いくつかの実施態様において、ナノゲルは、親水性または両親媒性のポリマー鎖で構成される膨張したナノサイズのネットワークで構成され得る。いくつかの実施態様において、ナノゲルは、カチオン性および中性ポリマー(例えば、分枝ポリエチレンイミン(PEI)およびポリエチレングリコール(PEG)(PEG−cl−PEI))の、膨張した化学的に架橋されたネットワークで構成され得る。いくつかの実施態様において、ナノゲルは、物理的に架橋された、コレステロール修飾された多糖類(例えば、プルラン、マンナン、アミロペクチンおよびデキストラン)で構成され得る。ナノゲルを、薬物輸送のための担体として用いてもよく、塩結合、水素結合または疎水性相互作用の形成を介して、生物活性分子を取り込むように設計してもよい。
いくつかの実施態様において、ナノ構造体はリポソームである。リポソームは、少なくとも1つの脂質二重層および内部の水性コンパートメントを含む、閉じたベシクルである。リポソームは、アニオン性、中性またはカチオン性であり得る。リポソームは単層または多重層であり得る。リポソームは、限定されないが、単層ベシクル脂質、多重層ベシクル脂質および押し出された脂質(単独または、DOTMAおよびコレステロール、DOTAPおよびコレステロール、DOTIMおよびコレステロール、ならびにDDABおよびコレステロールを生じるようにコレステロールを含む、DOTMA、DOTAP、DOTIM、DDABを含む)を含み得る。多重層ベシクルを調製する方法は、当分野で公知である(例えば、米国特許第6,693,086号参照、この多重層ベシクル脂質調製に関する教示は、参照によって本明細書に組み込まれる)。押し出された脂質は、類似の様式で調製されるが、次いで、Templeton et al., Nature Biotech, 15:647-652, 1997(押し出された脂質の調製に関する教示は、参照によって本明細書に組み込まれる)に記述されるように、サイズを減少させるフィルターを通して、押し出される。
本明細書は、ナノ構造体を作製する方法を提供する。ナノ構造体の例は、タンパク質ナノゲル(無傷の生物活性タンパク質を含み、担体(例えば、アルブミン、BSA)を含まない、タンパク質ナノゲルなど)である。いくつかの実施態様において、担体を含まない、生物活性タンパク質ナノゲルを作製する方法は、タンパク質を分解性リンカーと、分解性リンカーを介するタンパク質の相互の可逆的な共有結合の架橋を可能にする条件下において、接触させることを含み、これによって、担体を含まない、生物活性タンパク質ナノゲルを作製する。いくつかの実施態様において、本方法はさらに、タンパク質ナノゲルをポリマーと、ポリマーとタンパク質ナノゲルのタンパク質との架橋を可能にする条件下において、接触させることを含み、それによって、担体を含まない、生物活性タンパク質−ポリマーナノゲルを作製する。いくつかの実施態様において、複数のタンパク質ナノゲルまたは複数のタンパク質−ポリマーナノゲルを作製する。
細胞表面共役受容体を結合するリガンド
リガンドは、細胞表面受容体(例えば、CD45などの細胞表面共役受容体)などの別の分子と結合する、任意の分子である。リガンドの例は、抗体(免疫グロブリンとも呼ばれる)、可溶性タンパク質受容体(例えば、CD22;Sgroi et al. Proc. Natl. Acad. Sci. USA, 92:4026-30, 1995)、サイトカイン、ペプチド、小分子、補因子、ホルモンおよび神経伝達物質を含む。他のタンパク質結合パートナーが、本明細書で想定される。リガンドは、ナノ粒子またはリポソームと担体細胞との共役を促進するために、ナノ粒子またはリポソームに組み込まれ得る。
本開示のいくつかの態様は、その表面上にポリカチオンを有する、ナノ構造体(例えばナノゲル)を提供する。ポリカチオンは、いくつかの部位に正電荷を有する分子または化学複合体である。一般に、ポリカチオンは全体で正電荷を有する。本開示で用いるポリカチオンの例は、限定されないが、ポリリジン(ポリ−L−リジンおよび/またはポリ−D−リジン)、ポリ(アルギニングリセリルコハク酸)(poly(argininate glyceryl succinate);PAGS、アルギニンに基づくポリマー)、ポリエチレンイミン、ポリヒスチジン、ポリアルギニン、硫酸プロタミン、ポリエチレングリコール−b−ポリリジン(PEG−PLL)またはポリエチレングリコール−g−ポリリジンを含む。本明細書において、ポリカチオンを、ナノ粒子の担体細胞(例えばT細胞)への接着を改善し、共役反応の効率を向上するのに用いてもよい。具体的には、ポリカチオンを、ナノ構造体(例えばタンパク質ナノゲル)の担体細胞へのローディングを向上するのに用いてもよい。ポリカチオンをまた、ナノ構造体と担体細胞との共役または共役効率を向上するのに用いてもよい。ポリカチオンは、細胞膜の負に帯電したイオンとナノゲル表面の正に帯電したイオンとの間の静電相互作用を増強すると考えられる。
細胞表面受容体(例えば、膜貫通受容体)は、細胞とその細胞外環境との間の情報伝達を仲介するタンパク質である。細胞外リガンド(サイトカイン、増殖因子、ホルモン、神経伝達物質および細胞認識分子を含む)は同種の受容体と結合し、細胞外シグナルを伝達する立体構造変化をトリガーし、細胞内シグナル伝達経路を開始する。細胞表面受容体は、成長、分化、増殖および生存に関与する多数の生物学的経路を制御する。T細胞およびB細胞は共に、細胞の活性化に関与する細胞表面受容体を有する。
本開示の態様は、担体細胞(例えば、有核担体細胞)(またはより単純に「細胞」)に安定に結合するナノ構造体(例えば、タンパク質ナノゲルまたはリポソーム)を含む組成物を提供する。担体細胞は、ナノ粒子と共役する細胞であり、インビボにおいて投与された場合、典型的に標的部位に向かう細胞である。適切な標的細胞を、それらのホーミング能、(ナノ粒子との共役における)細胞表面の表現型に基づいて選択する。いくつかの実施態様において、細胞は、T細胞(Tリンパ球とも呼ばれる)、B細胞またはナチュラルキラー(NK)細胞および、限定されないが、マウス系列陰性細胞、Sca−1−陽性細胞およびc−kit−陽性細胞ならびにそれらのヒト対応物を含む、造血前駆細胞であり得る。相当なレベルの遊離チオール(−SH)基が、T細胞、B細胞および造血前駆細胞の表面上に存在し、これによって、ナノ構造体とこれらの細胞との共役が促進される。
いくつかの実施態様において、本開示の細胞はT細胞である。T細胞は、胸腺によって産生し、または処理される種類のリンパ球であり、免疫応答に能動的に関与する。T細胞は、細胞表面上のT細胞受容体(TCR)の存在によって、他のリンパ球(B細胞およびナチュラルキラー細胞(NK細胞)など)から区別され得る。本開示において使用されるT細胞の例は、Tヘルパー細胞(TH細胞、CD4+ T細胞)、細胞障害性T細胞(TC細胞、CTL、CD8+ T細胞)、メモリーT細胞、サプレッサーT細胞およびナチュラルキラーT細胞(NKT細胞)を含む。
いくつかの実施態様において、本開示の細胞はB細胞である。B細胞は、適応免疫系における液性免疫に関与する。B細胞は、その外側の表面上に存在するB細胞受容体(BCR)によって、区別できる。B細胞は、抗原に反応して抗体を作成し、抗原提示細胞として働き、抗原相互作用によって生じる活性化後に、メモリーB細胞に発達する。さらに、B細胞は、免疫制御機能において用いられるサイトカインを分泌する。B細胞は、血液およびリンパ系中を循環し、免疫監視を行う。B細胞は、完全に活性化するまで抗体を産生しない。B細胞受容体(BCR;B細胞表面上に存在する膜結合型免疫グロブリン)は、1つの特異的な抗原に結合する。B細胞は、T細胞依存的な様式またはT細胞非依存的な様式のいずれかで、活性化される。活性化に際して、B細胞は、血漿B細胞またはメモリーB細胞となる。B細胞はまた、中間の分化工程を経て、それによって、その免疫グロブリン遺伝子の可変領域を超変異させ、クラススイッチを起こし得る。制御性B細胞は、IL−10およびTGF−βを分泌し、様々な機構を介して免疫制御に関与する。
T細胞およびB細胞を、対象の末梢血から回収してもよい。
いくつかの実施態様において、本開示の細胞は、ナチュラルキラー(NK)細胞である。ナチュラルキラー細胞は、自然免疫応答の細胞傷害性リンパ球である。ナチュラルキラー細胞は大抵、抗原特異的な細胞表面受容体を持たず、事前の病原体への曝露なしに、即座に反応できる。これらは、ウイルス感染症を含むが、適応免疫応答は、抗原特異的な細胞傷害性T細胞を産生し、感染症を完全に除去する。ナチュラルキラー細胞の細胞質中の小顆粒は、パーフォリンおよびグランザイムを含み、これらはプロテアーゼである。これらの分子を、標的細胞の非常に近くで放出すると、パーフォリンは、標的細胞の細胞膜にポアを作り、これを介して、グランザイムおよび他の関連する分子が侵入でき、アポトーシスまたは浸透圧性細胞溶解をもたらす。ナチュラルキラー細胞はまたα−デフェンシンを分泌し、α−デフェンシンは、細胞壁を破壊することによって細菌を直接死滅させる抗菌分子であり、これは好中球の作用に類似している。サイトカイン(IL−12、IL−15、IL−18、IL−2およびCCL5を含む)は、細胞によってウイルス感染に反応して放出され、NK細胞に、その領域におけるウイルス病原体の存在を伝達する。ナチュラルキラー細胞は、ウイルス感染症に反応して、IFNγおよびTNFαを分泌する。INFγは、食作用および溶解について、マクロファージを活性化するが、TNFαは、直接的なNK腫瘍細胞死滅を促進する。ナチュラルキラー細胞はまた、免疫監視機能を有し、樹状細胞、マクロファージ、T細胞および内皮細胞との相互作用に関与する。
造血前駆細胞は、多数の供給源(限定されないが、臍帯血、骨髄、動員末梢血および、いくつかの場合において、分化胚性幹細胞を含む)から得られ得る。
T細胞を、キメラ抗原受容体(CAR)を発現するように設計してもよい。この最も単純な形態において、CARは、膜貫通ドメインと共役している抗原結合ドメインおよびCD3ζ鎖の細胞質側末端由来のシグナル伝達ドメインを有する。CD3ζ鎖が、形質導入したT細胞を完全に活性化するのに不十分であるという、いくつかの根拠がある。したがって、CARは、好ましくは、抗原結合ドメイン、同時刺激ドメインおよびCD3ζシグナル伝達ドメインを有する。CD3ζシグナル伝達ドメインを組み合わせた同時刺激ドメインの使用は、T細胞活性化の2つのシグナルモデルを模倣する。例えば、本開示のいくつかの実施態様は、抗原結合ドメイン、同時刺激ドメイン(4−1BB細胞内ドメインなど)およびCD3ζシグナル伝達ドメインを含む、キメラ抗原受容体に関する。いくつかの実施態様において、抗原結合ドメインを、リンカー(CD8aヒンジおよび膜貫通ドメインなど)を介して、同時刺激ドメインおよびCD3ζシグナル伝達ドメインと融合する。
トラスツズマブ(HERCEPTIN(商標) by Genentech, South San Francisco, Calif.)、これはHER−2/neu陽性乳がん、または転移性乳がんの処置に用いられる;
ベバシズマブ(AVASTIN(商標) by Genentech)、これは大腸がん、転移性大腸がん、乳がん、転移性乳がん、非小細胞肺がん、または腎細胞がんの処置に用いられる;
リツキシマブ(RITUXAN(商標) by Genentech)、これは非ホジキンリンパ腫または慢性リンパ性白血病の処置に用いられる;
ペルツズマブ(OMNITARG(商標) by Genentech)、これは乳がん、前立腺がん、非小細胞肺がん、または卵巣がんの処置に用いられる;
セツキシマブ(ERBITUX(商標) by ImClone Systems Incorporated, New York, N.Y.)、これは大腸がん、転移性大腸がん、肺がん、頭頸部がん、結腸がん、乳がん、前立腺がん、胃がん、卵巣がん、脳腫瘍、膵がん、食道がん、腎細胞がん、前立腺がん、子宮頸がん、または膀胱がんの処置に用いられる;
IMC−1C11(ImClone Systems Incorporated)、これは大腸がん、頭頸部がん、または他の潜在的ながん標的の処置に用いられる;
In111イブリツモマブチウキセタン(ibirtumomab tiuxetan);Y90イブリツモマブチウキセタン;In111イブリツモマブチウキセタンおよびY90イブリツモマブチウキセタン(ZEVALIN(商標) by Biogen Idec, Cambridge, Mass.)、これは、リンパ腫または非ホジキンリンパ腫の処置に用いられ、これらは再発した濾胞性リンパ腫;再発性もしくは抵抗性の、低悪性度もしくは濾胞性の非ホジキンリンパ腫;または形質転換したB細胞非ホジキンリンパ腫を含み得る;
EMD7200(EMD Pharmaceuticals, Durham, N.C.)、これは、非小細胞肺がんまたは子宮頸がんの処置に用いられる;
SGN−15(Seattle Geneticsによる、ドキソルビシンと共役するLewisγ関連抗原を標的とする、遺伝子操作されたモノクローナル抗体)、これは、非小細胞肺がんの処置に用いられる;
SGN−33(Seattle Geneticsによる、CD33抗原を標的とする、ヒト化抗体)、これは、急性骨髄性白血病(AML)および骨髄異形成症候群(MDS)の処置に用いられる;
SGN−40(Seattle Geneticsによる、CD40抗原を標的とする、ヒト化モノクローナル抗体)、これは、多発性骨髄腫または非ホジキンリンパ腫の処置に用いられる;
SGN−35(Seattle Geneticsによる、オーリスタチンE(auristatin E)と共役するCD30抗原を標的とする、遺伝子操作されたモノクローナル抗体)、これは、非ホジキンリンパ腫の処置に用いられる;
SGN−70(Seattle Geneticsによる、CD70抗原を標的とする、ヒト化抗体)、これは、腎がんおよび上咽頭がんの処置に用いられる;
SGN−75(Seattle Geneticsによる、SGN70抗体およびオーリスタチン誘導体で構成される複合体);および
SGN−17/19(Seattle Geneticsによる、メルファランプロドラッグと共役する、抗体および酵素を含む融合タンパク質)、これは、メラノーマまたは転移性メラノーマの処置に用いられる。
いくつかの実施態様において、本開示は、薬剤を送達する方法を提供し、これは、薬剤を含むナノ構造体と共有結合している担体細胞を、対象に投与することを含み、ここで細胞は、ナノ構造体を実質的にインターナライズせず、ナノ構造体を細胞表面上に維持し、薬剤はインビボにおいて、ナノ構造体から放出される。
さらに他のp38 MAPK阻害剤は、Tocriset、SB239063、SB203580、パマピモド(pamapimod)、ディルマピモド(dilmapimod)およびPH797804である。
リーシュマニア伸長因子(精製したリーシュマニアタンパク質;Corixa Corporation, Seattle, Wash.)、ISCOMS(混合したサポニン、脂質を含み、抗原を保持できるポアを有するウイルスサイズの粒子を形成する、免疫賦活性複合体;CSL, Melbourne, Australia)、Pam3Cys、SB−AS4(ミョウバンおよびMPLを含む、SmithKline Beecham adjuvant system #4;SBB, Belgium)、CRL1005などのミセルを形成する非イオン性ブロック共重合体(これらは、ポリオキシエチレン鎖に隣接する、疎水性ポリオキシプロピレン直鎖を含む;Vaxcel, Inc., Norcross, Ga.)およびモンタナイドIMS(例えば、IMS1312、可溶性免疫賦活剤を組み合わせた、水性ナノ粒子;Seppic)であり得る。
本明細書で与えられる組成物は、腫瘍に向かい、薬剤(例えば生物活性タンパク質)を含むナノ構造体(例えば、タンパク質ナノゲルまたはリポソーム)と共役している、有核担体細胞を含む、ここで担体細胞は、細胞表面共役受容体(例えばCD45)を有し、受容体と結合するリガンドを有するナノ構造体と共役している、または、担体細胞は負に帯電した細胞膜を有し、ナノ構造体は細胞膜と静電的に相互作用するポリカチオン性表面を有する。
本開示はまた、インビボにおいてナノ構造体と共役している担体細胞を含む組成物を、対象に投与する方法を提供する。本開示の方法を、本明細書で記述されるような薬剤(例えば、生物活性タンパク質)の送達によって恩恵を受ける可能性のある対象に、実行できる。いくつかの実施態様において、ヒト対象が好ましい対象である。対象はまた、家用のペット(例えば、イヌ、ネコ、ウサギ、フェレット)、家畜または農場の動物(例えば、ウシ、ウマ、ブタ、ヒツジ、ニワトリおよび他の家禽類)、実験動物(例えば、マウス、ラット、ウサギ)などの動物を含む。対象はまた、魚および他の水性種を含む。
がんの処置方法
本開示は、本明細書で記述される組成物の、がん(例えば固形腫瘍を含む)を患い、またはがんが発生するリスクのある対象への投与を提供する。がんは、がん腫、肉腫またはメラノーマであり得る。がん腫は、限定されないが、基底細胞がん、胆道がん、膀胱がん、乳がん、子宮頸がん、絨毛がん、CNSがん、大腸および直腸がん、腎がん又は腎細胞がん、喉頭がん、肝がん、小細胞肺がん、非小細胞肺がん(NSCLC;腺がん、巨(または燕麦)細胞がん、および扁平上皮がんを含む)、口腔がん、卵巣がん、膵がん、前立腺がん、皮膚がん(基底細胞がん及び扁平上皮がんを含む)、胃がん、精巣がん、甲状腺がん、子宮がん、直腸がん、呼吸器系のがん、および泌尿器系のがんを含む。
本開示は、本明細書で記述される組成物の、感染症(細菌感染症、ウイルス感染症、真菌感染症、寄生虫感染症またはマイコバクテリア感染症など)を患い、または感染症が発生するリスクのある対象への投与方法を提供する。
細菌感染症は、限定されないが、大腸菌感染症、ブドウ球菌感染症、連鎖球菌感染症、シュードモナス感染症、クロストリジウム・ディフィシル感染症、レジオネラ感染症、肺炎球菌感染症、ヘモフィルス感染症、クレブシエラ感染症、エンテロバクター感染症、シトロバクター感染症、ナイセリア感染症、赤痢菌感染症、サルモネラ菌感染症、リステリア感染症、パスツレラ感染症、ストレプトバチルス感染症、スピリルム感染症、トレポネーマ感染症、放線菌感染症、ボレリア感染症、コリネバクテリウム感染症、ノカルジア感染症、ガードネレラ感染症、カンピロバクター感染症、スピロヘータ感染症、プロテウス感染症、バクテロイデス(Bacteriodes)感染症、ピロリ菌感染症、または炭疽菌感染症であり得る。
本開示はさらに、本明細書で記述される組成物の、アレルギーまたは喘息を患い、またはアレルギーまたは喘息が発生するリスクのある対象への投与を提供する。アレルギーは、アレルゲンに対する獲得過敏性である。アレルギー疾患は、限定されないが、湿疹、アレルギー性鼻炎またはコリーザ、枯草熱、気管支喘息、じんましん(発疹)、および食物アレルギー、ならびに他のアトピー性疾患を含む。アレルギーは通常、無害なアレルゲンに対するIgE抗体の産生によって生じる。喘息は、炎症、気道狭窄、および吸入剤に対する気道の反応性の増加を特徴とする、呼吸器系の障害である。喘息は、必ずではないが、アトピーまたはアレルギー症状を伴うことが多い。本開示において、Th1サイトカイン(IL−12およびIFN−ガンマなど)の投与は、アレルギーまたは喘息の処置に使用され得る。
本開示は、本明細書で記述される組成物の、自己免疫疾患を患い、または自己免疫疾患が発生するリスクのある対象への投与を提供する。自己免疫疾患は、対象自身の抗体が宿主組織に反応する疾患の種類、または免疫エフェクターT細胞が、内在性の自己ペプチドに対して自己反応し、組織の破壊を生じる疾患の種類である。したがって、免疫応答は、対象自身の抗原(自己抗原と呼ばれる)に対して開始される。自己免疫疾患は一般に、Th1偏向性であると考えられている。結果として、Th2免疫応答またはTh2様サイトカインの誘導が有益となり得る。そのようなサイトカインは、IL−4、IL−5およびIL−10を含む。
本明細書で提供される方法はまた、移植治療後の免疫応答を調節するのに用いられ得る。移植の成功は、身体の免疫系による移植組織の拒絶によって制限されることが多い。結果として、移植レシピエントは通常、移植組織を生存させるために、長期間にわたって免疫反応を抑制する。本開示は、移植拒絶を最小化するため、免疫調節剤および、特に免疫抑制剤の、移植部位への局在化した送達を提供する。したがって、本開示は、移植を実行予定、実行中または実行後の対象への、組成物の投与を提供する。上記の記載は、包括的であることを意図せず、むしろ例示的である。当業者は、本開示の方法を用いた予防および処置に適した、各種類の疾患における他の例を同定する。
本明細書で記述される組成物は、有効量で投与される。有効量は、医学的に望ましい結果を提供するのに十分な、薬剤の投与量である。有効量は、処置される特定の疾患、処置される対象の年齢および体調、疾患の重症度、処置期間、(もしあれば)同時または併用療法の性質、特定の投与経路、ならびに医療関係者の知識および専門知識における類似の要素によって、様々である。最大投与量(すなわち、健全な医学的判断による最も高い安全投与量)を用いることが一般的に好ましい。
第1の態様において、本開示は、腫瘍に向かい、薬剤を含むナノ構造体と共役している、有核担体細胞を含む組成物を提供し、ここで担体細胞は細胞表面共役受容体を有し、ナノ構造体は、細胞表面共役受容体と結合するリガンドで、担体細胞と共役している。第1の態様のいくつかの実施態様において、リガンドは、抗体、抗体フラグメント、可溶性タンパク質受容体、サイトカイン、ペプチド、小分子、補因子、ホルモンおよび神経伝達物質からなる群から選択される。いくつかの実施態様において、細胞表面受容体はCD45(抗CD45モノクローナル抗体(例えば、ヒト抗CD45抗体またはヒト化抗CD45抗体)と結合する、または結合している受容体など)である。いくつかの実施態様において、抗CD45モノクローナル抗体は、BC8、4B2、9.4およびGAP8.3からなる群から選択される。第1の態様における上記の任意の実施態様において、担体細胞は、T細胞、B細胞またはナチュラルキラー(NK)細胞である。いくつかの実施態様において、担体細胞は、CD8+ T細胞またはCD4+ T細胞などの、T細胞である。いくつかの実施態様において、T細胞は養子導入T細胞である。いくつかの実施態様において、T細胞は、キメラ抗原受容体(CAR)T細胞である。
膜間架橋多重層ベシクル(ICMV)(Nature Mater. 2011, 10, 243-251)は、4日間を超えて、細胞表面(例えばT細胞表面)上に残存できる粒子の一種である。ゆっくりとインターナライズする受容体の候補プールを、ICMVに最も多く結合する、全ての表面タンパク質の質量分析によって、得た。ICMVの長期の表面保持における主要な原因物質についてのスクリーニングを、最大の候補である表面受容体(CD2、CD11およびCD45など)に対する抗体で表面共役したリポソームを用いて、行った。抗体と共役したリポソームは、担体細胞と共役した。
抗体と共役するリポソームを、2.5%PEG−マレイミドおよび1%ビオチン頭部を含む、乾燥した、高いTMのリン脂質フィルムを水和させることによって、作製した。具体的には、2.5/27/68/1.5のモル比における、1,2−ジステアロイル−sn−グリセロ−3−ホスホエタノールアミン−N−[マレイミド(ポリエチレングリコール)−2000](マレイミド−PEG2000−DSPE)/コレステロール/水素化ダイズL−α−ホスファチジルコリン(HSPC)/1,2−ジステアロイル−sn−グリセロ−3−ホスホエタノールアミン−N−[ビオチニル(ポリエチレングリコール)−2000](ビオチン−PEG2000−DSPE)(Avanti Polar Lipids, Alabaster, AL, USA)から構成され、1%の蛍光親油性トレーサー色素DiDを含む、真空乾燥させた脂質フィルムを、250μLの50mM 4−(2−ヒドロキシエチル)−1−ピペラジンエタンスルホン酸(HEPES)/150mM NaCl緩衝液(pH=6.5)で再水和した。脂質を、62℃で1時間、10分ごとにボルテックスしてベシクルを形成し、ポリカーボネート膜(0.2μm)に通して、サイズ排除した。過剰のPBSで洗浄し、110,000xg、4時間での超遠心で沈降させた後、リポソームを、1.4mgの脂質当たり100μLのPBSで再懸濁した。リポソームのマレイミド基との共役において、抗体、サイトカインおよび、異なるモル比(2−5mg/mL)での抗体/サイトカイン混合物を、10mM EDTA存在下において、1.8mMジチオスレイトール(DTT)で、20分間、25℃で処理し、ヒンジ部位のフリーのチオールを露出させた。次に、マレイミドを有するリポソームとPBS中で混合する(タンパク質/脂質における、1/1の重量/重量)前に、DTTを、Zeba脱塩カラムを用いて除去した。回転子上での25℃、18時間のインキュベーション後、余剰タンパク質を、過剰PBS中における超遠心で除去した。T細胞を、ロズウェルパーク記念研究所(RPMI)培地中で37℃でインキュベートする前に、非結合のリポソームを洗い流した。
100μL PBS中における、抗体と共役したリポソーム(0.7mg脂質)を、10%ウシ胎仔血清(FCS)を添加した0.5mlの完全RPMI中における20×106個の抗原刺激したpmel−1 Thy1.1+ CD8+ T細胞と共に、30分間、37℃で、15分ごとに穏やかに撹拌しながら、インキュベートした。共役したT細胞を、PBS(20mLx2)で洗浄し、非結合のリポソームを除去し、組換えIL−7(1.5ng/mL)および10%FCSと共に、RPMI中において、37℃、0.5x106細胞/mLで、インキュベートした。
非結合のリポソームを洗い流し、細胞を、完全RPMI中、37℃でインキュベートした。細胞を、ストレプトアビジンフルオロフォアで染色し、共役前0時間、6時間、24時間および48時間、または共役後0時間、19時間、45時間および69時間において、フローサイトメトリーで分析した(図1Bおよび1C)。蛍光標識された細胞の割合を、時間に対してプロットした。インターナライズしたリポソームは、ストレプトアビジン色素にアクセスできないため、表面リポソームを有するT細胞のみが蛍光標識される。48時間後、ほぼ100%の細胞が未だ、表面上に係留した、抗CD45(α−CD45)抗体で装飾されたリポソームを有していたが、表面が抗CD11(α−CD11)抗体および抗CD2(α−CD2)抗体で装飾されたリポソームは、それぞれわずか30%および70%の細胞において、見出された(図1A)。意外にもCD45は、より速いインターナリゼーションの受容体CD11およびCD2に対して、長期間の細胞表面における滞留時間を示した。α−CD45を、α−CD2またはα−CD11と組み合わせて、リポソームの表面装飾に用いると、CD45およびCD2(またはCD45およびCD11)の両方に係留したリポソームが、より速いインターナリゼーションの受容体CD2およびCD11との結合に関係なく、2日後に未だ100%の細胞上に残存していた(図1A)。抗CD45リポソームは、CD2およびCD11だけでなく、CD8およびThy1.1と比較しても、長期間の細胞表面の保持を示した(図1B)。
サイトカインナノゲル(NG)を、国際公開番号WO 2015/048498 A2(2015年4月2日に出願、これは参照によって本明細書に取り込まれる)において記述されるように、調製した。さらなる修飾を、上述のように、サイトカインナノゲルに行った。一般に、サイトカインを、可逆性リンカー(NHS−SS−NHS)と化学的に架橋し、タンパク質の架橋したナノ構造体(タンパク質ナノゲル(NG)と呼ぶ、図2)を形成した。サイトカインの架橋反応完了後、抗CD45抗体および/またはポリカチオンを、インサイチュ(in situ)で添加し、NG表面を修飾した(図2)。合成後、ナノゲルを特徴付けし、さらに後述するように、担体細胞と共役した。
NHS−SS−NHS架橋剤の合成:125mLの丸底フラスコにおいて、2−ヒドロキシエチルジスルフィド(1.54g、10mmol)を、テトラヒドロフラン(THF、30mL、無水物)中に溶解し、ホスゲンの溶液(15mL、トルエン中における15重量%、22mmol)に滴下した。混合物を、25℃で10時間撹拌し、その後、真空下で溶媒を除去した。N−ヒドロキシスクシンイミド(NHS)(2.3g、22mmol)をTHF(30mL、無水物)中に溶解し、一部として添加し、次いで乾燥したトリエチルアミン(1.57mL、11mmol)を注入した。反応物を、40℃で16時間保持した。溶媒を真空下で除去し、混合物を濾過し、沈殿を除去した。粗生成物を、シリカゲルカラムクロマトグラフィー(ジクロロメタン/メタノール=10/1)で精製し、氷冷ヘキサン(80mL)で再結晶させた。得られた白色固体を、真空下で乾燥させた(3.1g、収率71%)。1H−NMR(CDCl3、500MHz);δ4.58(t、4H)、3.05(t、4H)、2.84(s、8H)。13C−NMR(CDCl3、500MHz):δ168.77、151.66、68.84、36.68、25.69。ESI(m/z):C14H16N2O10S2における計算値、436.4[M];実測値、459.0[M+Na]+。
ヒトIL−15Saナノゲル:NHS−SS−NHS(93.5μg、0.214μmol)を、9.35μL DMSO中に溶解し、132μLリン酸緩衝生理食塩水(PBS)pH7.4のIL−15Sa(ALT−803(1320μg、0.0143μmol)、Altor BioScience Corporation (Miramar, FL, USA.)、US2014/0134128およびCytokine 2011, 56, 804-810も参照)溶液に添加した。混合物を25℃で30分間回転させ、次いで、1188μL PBS緩衝液を添加した。CD45を標的とする抗体を組み込むナノゲル(NG)において、次に、31.7μl PBS緩衝液中の抗CD45(215μg、0.0014μmol)を希釈溶液に添加した。抗マウスCD45RB(クローン:MB23G2:BioXCell (West Lebanon, NH, USA)から購入)または抗ヒトCD45(クローン:MEM−28:Abcam (Cambridge, United Kingdom)から購入)のいずれかを用いた。反応混合物を、25℃で、さらに30分間回転させた。抗CD45を含まないIL−15Sa−NGの調製は、抗CD45を、35.8μL PBS緩衝液中の永久的なリンカーであるNH2−PEG10k−NH2(715μg、0.0715μmol)(Laysan Bio: Arab, AL, USA)に置換したことを除き、同様であった。非分解性NG(例えば、aCD45/IL−15Sa−NG(非分解性))を、NHS−SS−NHSの代わりに、永久的なリンカーであるビス(スルホスクシンイミジル)基質(Thermo Fisher Scientific,Waltham, MA, USA)を用いて調製した。
T細胞表面上により多くのNGを濃縮するため、担体細胞との共役の前に、ポリカチオン(例えば、ポリエチレングリコール−b−ポリリジン(PEG−PLL))を、インサイチュにおいて、いくつかの試料に添加した。例えば、新たに調製した抗CD45/IL−15Sa−NG溶液を1μg/μlに希釈し、その後、後述のT細胞共役の前に、43.6μL PBS中のポリエチレングリコール−b−ポリリジン(PEG5K−PLKC200、19μg、0.0005μmolまたは43.6μg、0.0011μmol)(Alamanda Polymers, Huntsville, AL, USA)を添加した。次いで、混合物を25℃で30分間回転させ、さらなる精製をせずに用いた。
蛍光標識したNGを調製するため、サイトカインカーゴを、Alexa Fluor 647 NHSエステル(Thermo Fisher Scientific)で蛍光標識し、アミコン超遠心式フィルター(カットオフ分子量50kDa)で精製した。上述と同じ操作後、蛍光NGを調製するため、蛍光サイトカインを非標識サイトカインと混合した(10mol%の標識化サイトカイン)。ビオチン化NGを調製するため、9.35μL DMSO中に溶解したNHS−SS−NHS(93.5μg、0.214μmol)を、132μL PBS緩衝液のIL−15Sa(1320μg、0.0143μmol)溶液に添加した。混合物を25℃で20分間回転させ、次いで、7.5μL DMSO中のEZ−Link NHS−LC−LC−ビオチン(40.6μg、0.072μmol、Thermo Fisher Scientific)を添加した。混合物を、25℃で、さら20分間回転させ、1188μL PBS緩衝液で希釈し、その後、31.7μL PBS緩衝液中の抗CD45(215μg、0.0014μmol)を添加した。残りの操作は、上述と同じであった。
典型的な実験において、950μL PBS中の、Alexa Fluor 647で標識されたaCD45/IL−15Sa−NG(950μg、0.010μmol)を、475μL HBSS中のマウスCD8+ T細胞(95x106)に添加し、次いで、37℃で1時間インキュベートした。表面に共役したNGを有するT細胞を、800xg、5分間の遠心で回収し、PBSで洗浄し(1.0mLx2)、インビトロまたはインビボでの研究における所望の濃度で、緩衝液または培地に再懸濁した。全NG共役の測定において、蛍光標識したNGをT細胞と共役させ、上清を回収し、プレートリーダー(Tecan Infinite(登録商標) M1000 PRO)を用いて、640/680nmの励起波長/蛍光波長で、蛍光強度を測定した。蛍光の読み取りを、NG原液の段階希釈から作成した検量線を用いて、NG濃度に変換した。共役したNGの量を、全添加量から非結合のNGを引くことで、計算した。細胞当たりのNGローディングを、共役において細胞に添加するNGの質量を変えることによって、制御した。抗CD45を持たないNGとT細胞との共役において、PBS(950μL)中のIL−15Sa−NG(950μg、0.010μmol)をまず、スルホスクシンイミジル4−(N−マレイミドメチル)シクロヘキサン−1−カルボン酸(218μg、0.50μmol)またはビス(スルホスクシンイミジル)基質(286μg、0.50μmol)で活性化し、アミコン超遠心式フィルター(カットオフ分子量50kDa)で回収し、PBSで洗浄し(1.5mLx3)、次いで、475μL HBSS中のCD8+ T細胞(95x106)に添加し、その後、37℃で1時間インキュベートした。細胞を、同様に洗浄し、回収した。共役したNGの量を、上述と同様に決定した。抗ヒトCD45を含む、または含まないNGと、ヒトCD8+ T細胞との共役は、上述と同様の操作に従った。同様のアッセイを、末梢血単核球から単離した、抗CD3/CD28が活性化したヒトCD8+ T細胞において、行った。
インビトロでのT細胞増殖アッセイを行い、T細胞増殖における抗CD45の効果を決定した。ナイーブpmel−1 CD8+ T細胞を、カルボキシフルオレセインスクシンイミジルエステル(CFSE)で標識し、次いで上述のように、それぞれaCD45/IL−15Sa−NG、IL−15Sa−NGまたはaCD45/IL−15Sa−NG(非分解性)と共役した。非結合NGの除去後、T細胞を、10%FCS(5.0x105/mL)を含むRPMI中に再懸濁し、抗CD3/CD28で被覆したビーズに、ビーズ:T細胞比を1:2として、添加した。遊離IL−15Saを、対照群における細胞に、(瞬間的または継続的に)当量添加した。細胞培地を3日毎に交換し、遊離IL−15Saを継続的な処置の群に補充した。選択した時点において、T細胞の複製物を、カウントビーズを用いて追加し、フローサイトメトリー緩衝液(2%FCSを含むPBS)で洗浄し、次いでaqua live/dead染色を行った。細胞を、抗体を含む表面マーカー(CD8、CD122)で染色し、その後、細胞内固定化&透過処理緩衝液セット(Intracellular Fixation & Permeabilization Buffer Set, eBioscience)で固定化および透過処理した。次いで、細胞内をpSTAT5およびKi67で染色し、フローサイトメトリー(BD Canto, BD Biosciences)で分析した。
上述の同種のB16F10メラノーママウスモデルを用いたが、処置群は以下であった。動物は、PBSのシャム注射、T細胞のみ、T細胞後における、単回投与(養子移植直後)もしくは複数回投与(7、10、13および16日目)に分けた、種々の用量の遊離IL−15Saのi.v.注射、または種々の用量で抗CD45/IL−15Sa NGと共役したT細胞を受けた。体重ならびに全身性サイトカイン、ケモカインおよび肝臓酵素のレベルを、経時的に分析した。相対的な体重を、7日目の体重で正規化した。血中のサイトカイン+内在性CD8+ T細胞およびACT CD8+ T細胞の細胞数を、14日目において、細胞内サイトカイン染色およびフローサイトメトリーで分析した。血清サイトカインレベルおよび肝臓酵素を、17日目、または動物を毒性のために安楽死させた場合に、回収した試料から測定した。サイトカインレベルを、Cytometric Bead Array(CBA)マウス炎症キット(BD Biosciences)を用いて、測定した。血清試料をまた、アラニントランスアミナーゼ(ALT)およびアスパラギン酸トランスアミナーゼ(AST)の分析のために、IDEXX Reference Laboratoriesに送った。データは、平均値±s.e.m(n=5/群)を示し、統計解析において対照群(T細胞のみ)と比較した。一元配置分散分析およびテューキーの検定による*、p<0.05;**、p<0.01;***、p<0.001;n.s.、有意でない;n.d.、不検出。
NGで送達したサイトカインが、臨床におけるT細胞療法の重要な様式としての、CAR T細胞の機能に正の影響を与えるか否かを評価した。この目的において、免疫不全NSGマウスのルシフェラーゼ発現ヒト神経膠芽腫モデルにおける、EGFRを標的とするヒトCAR T細胞を用いた。CAR T細胞を、ヒトCD8αの細胞外ドメインおよび膜貫通ドメインの一部、それに続く4−1BBおよびCD3ζの細胞内ドメインと融合した、単鎖可変フラグメントを形成するように、セツキシマブの重鎖および軽鎖に基づいて設計した、huEGFRscFv−BBzキメラ抗原受容体(Johnson et. Al., 2015, Sci Transl Med., 7(275); US2014/0271635A1)を用いて、調製した。2シストロン性ベクターはまた、選択可能マーカーとしてヒトCD19切断型をコードし、T2Aリボソームスキップ配列後に位置していた。huEGFRscFv−BBz−CARをコードするプラスミドを合成し、レンチウイルスパッケージングを、VectorBuilderによって、作成した。単離したT細胞は、IRB承認プロトコル下において、匿名化された健常ドナーから得た、購入した白血球除去生成物(leukapheresis product)由来であった。T細胞を、DynabeadsヒトT活性化因子CD3/CD28(Life Technologies)で、ビーズと細胞の比を3:1として、刺激した。T細胞を、10%ウシ胎仔血清、Hepes緩衝液(20mM)、ペニシリンおよびストレプトマイシン(1%)ならびにIL−2(20IU/mL)を添加した、RPMI1640培地中で培養した。ビーズ刺激の1日後に、T細胞にCARレンチウイルスを導入し(TDN)、かつ/または、導入しないままであり(UTD)、次いで、T細胞を10日間増殖し、使用するまで凍結保存した。CARの表面発現を、ビオチン化ヒトEGFRタンパク質(ACRO Biosystems)で、確認および定量化した。
Claims (26)
- 腫瘍に向かい、生物活性タンパク質を含むナノ構造体と共役している、有核担体細胞を含む組成物、ここで担体細胞はCD45受容体を有し、CD45受容体に結合するリガンドを有するナノ構造体と共役している、または担体細胞は負に帯電した細胞膜を有し、ナノ構造体が細胞膜と静電的に相互作用するポリカチオン性表面を有する、ここでナノ構造体はタンパク質ナノゲルまたはリポソームである。
- 担体細胞が、CD45受容体を有し、CD45受容体に結合するリガンドを含むナノ構造体と共役している、請求項1に記載の組成物。
- リガンドが抗CD45モノクローナル抗体である、請求項2に記載の組成物。
- 担体細胞が負に帯電した細胞膜を有し、ナノ構造体が細胞膜と静電的に相互作用するポリカチオン性表面を有する、請求項1〜3のいずれかに記載の組成物。
- ポリカチオンがポリリジンである、請求項4に記載の組成物
- ポリカチオンが、ポリエチレングリコール−b−ポリリジン(PEG−PLL)である、請求項4に記載の組成物。
- ナノ構造体がタンパク質ナノゲルであり、タンパク質ナノゲルが、分解性リンカーを介して互いに可逆的かつ共有結合的に架橋する、複数の生物活性タンパク質を含む、請求項1〜6のいずれかに記載の組成物。
- 分解性リンカーが、ジスルフィド結合を含む酸化還元応答性リンカーである、請求項7に記載の組成物。
- ナノ構造体がリポソームであり、リポソームが複数の生物活性タンパク質を含む、請求項1〜6のいずれかに記載の組成物。
- リポソームが、膜間架橋多重層ベシクル(ICMV)または単層ベシクルである、請求項9に記載の組成物。
- 担体細胞が、T細胞、B細胞、ナチュラルキラー(NK)細胞または造血前駆細胞である、請求項1〜10のいずれかに記載の組成物。
- 担体細胞がT細胞である、請求項11に記載の組成物。
- T細胞が、CD8+ T細胞またはCD4+ T細胞である、請求項12に記載の組成物。
- T細胞が養子導入T細胞である、請求項12に記載の組成物。
- T細胞がキメラ抗原受容体(CAR)T細胞である、請求項12に記載の組成物。
- 生物活性タンパク質が抗体またはサイトカインである、請求項1〜15のいずれかに記載の組成物。
- 生物活性タンパク質が抗体である、請求項16に記載の組成物。
- 生物活性タンパク質がサイトカインである、請求項16に記載の組成物。
- サイトカインが、IL−2、IL−15またはIL−15−Saである、請求項18に記載の組成物。
- サイトカインがIL−15−Saである、請求項18に記載の組成物。
- IL−15−Saが、二量体IL−15RαSu/Fcおよび2分子のIL−15N72Dを含む複合体を含む、請求項20に記載の組成物。
- 二量体IL−15RαSu/Fcが、配列番号2に記載のアミノ酸配列を含み、IL−15N72D分子が、配列番号1に記載のアミノ酸配列を含む、請求項21に記載の組成物。
- 薬学的に許容し得る担体をさらに含む、請求項1〜22のいずれかに記載の組成物。
- 生物活性タンパク質を、腫瘍を有する対象に送達する薬物としての使用のための、請求項1〜23のいずれかに記載の組成物。
- 腫瘍が固形腫瘍である、請求項24に記載の組成物。
- 請求項1〜25のいずれかに記載の組成物を、それを必要とする対象に投与することを含む、対象のがんを処置する方法。
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