JP7333360B2 - 結合エピトープを含有する融合タンパク質を封入する粒子 - Google Patents
結合エピトープを含有する融合タンパク質を封入する粒子 Download PDFInfo
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Description
本出願は、参照によりその内容全体が本明細書中に組み込まれる、2016年1月4日に出願された米国仮特許出願第62/274,711号の優先権を主張する。
本明細書とともに電子的に提出されるテキストファイルの内容は、参照によりその全体が本明細書に組み込まれる:配列表のコンピュータ可読形式のコピー(ファイル名:COUR-013_01WO_Seqlist.txt、記録日:2016年1月4日、ファイルサイズ:1.17メガバイト)。
本発明の特定の実施形態は、複数の抗原またはエピトープを封入する粒子が、切断可能なリンカーによって融合タンパク質中で抗原が一緒に結合される場合、これらの抗原の各々に対して寛容を誘導することができるという新規発見に少なくとも一部基づいている。いくつかの実施形態において、リンカーは、特異的プロテアーゼ部位を含有するアミノ酸配列であり、クラスI経路またはクラスII経路によるプロセシングを可能にするように設計することができる。そのような実施形態において、同じ融合タンパク質上で結合した粒子に封入されたエピトープは、クラスI経路及びクラスII経路の両方によってプロセシングされ得る。したがって、クラスI経路によってプロセシングされるエピトープは、封入された融合タンパク質中でクラスII経路によってプロセシングされるエピトープと結合され得る。
ある特定の実施形態は、特異的プロテアーゼ部位を含むアミノ酸リンカー配列によって接続された2つ以上のペプチド、抗原、またはエピトープを含む融合タンパク質を封入する生分解性粒子を対象とする。特定の実施形態は、これらの粒子が、融合タンパク質の結合したペプチド、抗原、またはエピトープのうちのいくつかまたは全てに対する寛容を誘導するのに驚くほど効果的であることを企図する。ある特定の実施形態は、これらの生分解性粒子の製造が、融合タンパク質中の結合していない1つより多くのペプチド、抗原、及び/またはエピトープを封入する生分解性粒子と比較して改善されることを企図する。
いくつかの実施形態において、本明細書に記載の融合タンパク質を封入する生分解性粒子は、組成物に配合され得る。本明細書で使用される場合、「組成物」という用語は、対象及び/または細胞に投与することができる1つ以上の融合タンパク質を封入する1つ以上の粒子の配合物を指す。いくつかの実施形態において、組成物は複数の粒子からなってもよく、それらの各々が同じ融合タンパク質を封入する。いくつかの実施形態において、組成物は複数の粒子からなってもよく、それらの各々が2つ以上の異なる融合タンパク質を封入する。例えば、組成物は、各々が、2、3、4、5、6、7、8、9、10個、またはそれ以上の異なる融合タンパク質のうちの1つを封入する複数の粒子からなってもよい。いくつかの実施形態において、組成物は、任意選択的に、1つ以上の追加の治療剤をさらに含む。代替として、本発明の粒子は、それを必要とする患者に、1つ以上の他の治療剤の投与と組み合わせて投与されてもよい。例えば、本発明の化合物との共同投与のため、または本発明の化合物を含む薬学的組成物中に包含するための追加の治療剤は、承認された抗炎症剤であり得るか、あるいは制御されない炎症性免疫応答または細菌もしくはウイルス感染によって特徴付けられる任意の障害の治療のために最終的に承認を得る、Food and Drug Administrationで承認段階にある多くの薬剤のうちのいずれか1つであり得る。また、本発明の粒子は、治療のために遊離形態で存在し得るか、または必要に応じて、その薬学的に許容される誘導体として存在し得ることも理解されたい。
いくつかの実施形態において、本発明は、対象に本明細書に記載の粒子または組成物を投与することを含む、対象、好ましくは哺乳動物、より好ましくはヒトにおいて、既存の免疫応答を誘導するかまたは別様に制御するための方法を提供する。本明細書で使用される場合、「免疫応答」という用語は、自然免疫応答及び獲得免疫応答の両方(例えば、T細胞媒介性及び/またはB細胞媒介性免疫応答)を含む。一般的に、自然及び獲得免疫応答は、抗原特異性のレベルによって区別される。例えば、獲得免疫応答に直接関与する細胞(例えば、T細胞及びB細胞)は、特定の抗原に特異的なT細胞受容体(TCR)及びB細胞受容体を発現する。したがって、獲得免疫受容体は、活性化され、特異的抗原(例えば、より大きな抗原の特異的エピトープまたは成分)に応答する。対照的に、自然免疫の細胞は、TLR、CLR、NLR、RLR、及び他の自然免疫受容体(例えば、パターン認識受容体(PRR))を発現する。PRRは、幅広い種類の抗原を認識する生殖系列にコードされる、再編成しない受容体である(例えば、CLRは一般的に炭水化物部分を認識し、RLRはウイルス核酸を認識する)。したがって、自然免疫系の受容体は、活性化され、広い範囲の抗原に応答し、抗原特異的であるとは見なされない。
異なるペプチドエピトープを封入するPLG粒子の物理的特性及び機能的特性を決定するために実験を行った。寛容原性及び対照エピトープの一覧を図2に示す。一例として、PLP139-151を封入するPLG粒子を生成し、光散乱によってサイズ分布及びゼータ電位を決定した。PLP139-151を封入するPLG粒子のサイズ分布のピークは748.9nm、Z平均サイズは882.6nmであり、より大きな種の存在も示唆された(図3A)。さらに、恐らく乳化剤としてポリ(エチレン-コ-マレイン酸)(PEMA)を使用したために、PLP139-151を封入するPLG粒子は非常に高い負電荷を有していた(Z電位=-97.5mV、図3B)。
ペプチドエピトープを封入するナノ粒子が異なる細胞集団に与える影響を評価するために、ex vivoアッセイを使用して実験を行った。端的に述べると、-2日目に、PLP139-151TCRトランスジェニックマウス(5B6マウス、ドナー、Thy1.1+)からの3.5x106 CD4+細胞を、ナイーブな6~8週齢の雌SJLレシピエントマウスの静脈内に移入した。0日目に、SJLレシピエントマウスに、PLP139-151-SEを封入するPLGナノ粒子またはOVA323-339-SE(対照粒子)を封入するPLGナノ粒子のいずれかを注入した。注入後3日目及び5日目に、レシピエントマウスから脾臓を採取し、フローサイトメトリーにより制御性T細胞集団を分析した(図8)。全ての集団のCD90.1/Thy1.1+細胞にゲートをかけてPLP139-151-TCR+集団を選別した。
OVA323-339TCRドナー(DO11マウス)からの2.5x106 CD4+細胞を、6~8週齢のナイーブなメスBalb/c RAG KOレシピエントマウスの静脈内に移入して、相補的実験を行った。移入の2週間後、レシピエントマウスにOVA323-339-SE PLGまたはPLP139-151-SE PLG(対照)のいずれかを注入した。注入後にマウスから脾臓を採取し、フローサイトメトリーにより制御性T細胞集団を分析した(図12)。細胞集団はDO11-TCR+集団にゲートをかけた。図示されるように、PLP139-151-SE PLGを注入した対照と比較して、OVA323-339-PLGを注入した動物からのCD25+FoxP3+CD4+ T細胞の割合(図12A)及び合計数(図12B)の両方に著しい増加が見られた。同様の実験において、IFNγを産生する抗原特異的制御性T細胞の割合(図13A)及び数(図13B)も、PLP139-151-SE PLGを注入した対照と比較して、OVA323-339-PLGを注入した動物において著しく増加した。IFNγ+非制御性T細胞の数には、実験群と対照群との間に著しい差は見られなかった(図13)。さらに、DO11ドナーからのTR1集団の割合(図14A)及び数(図14B)の増加には、SJLマウスから単離した5B6 CD90.1+TR1細胞に見られた傾向と同様の傾向が見られた。
カテプシン特異的切断部位を含むペプチドリンカーによって結合されたPLP139-151及びOVA323-339エピトープの融合ペプチドを生成した(図16、PLP139-Ova323融合ペプチド)。DO11.10(図17A)または5B6(図17B)トランスジェニックマウスからの2x105脾細胞を様々な量のOVA323-339、PLP139-151、OVA323-339+PLP139-151、またはPLP139-Ova323融合ペプチド(リンカー)とともに播種し、細胞増殖を評価した。PLP139-Ova323融合ペプチドは、DO11細胞でOVA323-339及び5B6細胞でPLP139-151によって誘導された応答に匹敵する細胞増殖を誘導した。これらの結果は、エピトープ単独または組み合わせのいずれかと同様に、融合タンパク質が細胞応答を調節することが可能であることを示唆するものである。
EAEのモデルにおいてPLP139-OVA323融合タンパク質を封入するナノ粒子のin vivoでの影響を決定するために実験を行った。アジュバントに乳化したPLP139-151ペプチドエピトープまたはPLP139-OVA323融合タンパク質を用いた免疫化によりSLJマウスにおいてEAEを誘導した(群当たりN=5)。図22Aに示すように、PLP139-OVA323融合タンパク質を用いた免疫化は、EAEを誘導するのに十分であった。結果として得られた疾患スコアの大きさは、PLP139-151ペプチドによる免疫化によって誘導されたものに匹敵するものであった(図22A)。図22→PLP-OVA結合EAEスコア。PLP-OVA結合ペプチドは、疾患を誘導し、PLGAナノ粒子に封入されると寛容を誘導する。重要なのは、封入されたPLP-OVA融合タンパク質(PLP-OVA)の投与がEAE疾患スコアの抑止をもたらしたということである(図22A)。さらに、封入されたPLP-OVA融合タンパク質が、PLPで免疫化したSLJマウスの免疫応答のみを低減させ、MOGペプチドによる免疫化によって誘導された免疫応答には影響を与えなかったことから、この免疫調節は抗原特異的であった(図22B)。これらの結果は、結合エピトープ融合ペプチドを封入するナノ粒子が抗原特異的な様式で寛容原性免疫応答を誘導することを示唆するものである。
カテプシン特異的切断部位を含むペプチドリンカーによって結合されたPLP PLP139-151、PLP178-191、MOG92-106、及びMBP84-104エピトープの融合ペプチドを生成した(図23A、寛容原性EAE-1融合ペプチド)。さらに、カテプシン特異的切断部位を含むペプチドリンカーによって結合されたOVA323-339、PLP56-70、VP1233-250、及びVP270-86エピトープを含む対照融合ペプチドも生成した(図23B、EAE-1対照融合ペプチド)。寛容原性融合ペプチドを封入するナノ粒子の物理的特性(Z平均直径、PDI、ピーク直径、及びゼータ電位)をDLSにより決定した。粒子の画像は、カーボンでコーティングした銅メッシュ網上で粒子を乾燥させ、透過型電子顕微鏡法(TEM)を使用して得た。DLS及びEMの両方のデータが、通常よりもサイズ分布が大きいことを示唆している(図24)。
EAEモデルにおいて、結合したEAE-1融合ペプチド(PLP139:PLP178:MOG92:MBP)を封入するPLGAナノ粒子の影響を決定するために実験を行ったところ、無関係な対照ペプチド(OVA)または対照結合エピトープ(OVA323:PLP56:VP1:VP2)と比較して、EAE疾患において著しい低減をもたらした。封入された結合EAE-1融合ペプチドを用いたマウスの処理は、対照融合ペプチドまたは無関係な対照ペプチド(OVA)を用いた処理と比較してEAE疾患スコアを著しく減少させた(図28)。これらのデータは、複数の結合した疾患エピトープを含む融合ペプチドが自己免疫モデルにおいて寛容を誘導することができることを実証するものであり、それらの治療的可能性を示唆している。図29は、FALKペプチドもまたEAEを誘導することができることを示しており、このタンパク質中に見られるエピトープも寛容原性EAE融合タンパク質に組み込まれ得ることが示唆される。
ネオ抗原または腫瘍抗原の結合エピトープを含む融合ペプチドも癌の治療に使用される。そのようなエピトープは、治療効果を増大するためにPD1等の免疫調節因子またはToll様受容体アゴニストと組み合わされる(図29を参照のこと)。データは、抗PD1等の免疫調節因子とともに送達されるNy-Eso1等の封入された癌抗原が、T細胞増殖(図31Aの例示的な結果を参照のこと)、IFNγ産生(図31Bの例示的な結果を参照のこと)、及びIFNα産生(図31Cの例示的な結果を参照のこと)をもたらすことを示している。これらの結果は、封入された癌抗原が免疫原性応答を媒介し、炎症促進性サイトカインの産生をもたらすことを示している。
結合エピトープを含むさらなる融合タンパク質が生成されてもよい。例えば、複数の疾患の種類に由来するエピトープを含む融合タンパク質を生成して1つより多くの疾患の治療に使用することができる。代替として、TLRアゴニストをさらに含む疾患関連エピトープを含む融合タンパク質が生成されてもよい。そのようなアゴニストの包含は、タンパク質の免疫原性を増加させ、治療効果を増大させる。感染性ウイルス、細菌、または真菌に由来するエピトープを用いてさらなる融合タンパク質が生成されてもよい。そのような構築物に対するTLRアゴニストの添加もまた、治療効果を増大させることができる。
Claims (16)
- 封入された1つ以上の融合タンパク質を含む生分解性粒子であって、
前記1つ以上の融合タンパク質の各々は、重症筋無力症に関連する2つ以上の抗原エピトープを含み、前記2つ以上の抗原エピトープの各々は、アセチルコリン受容体(AChR)タンパク質の少なくとも一部を含み、
前記2つ以上の抗原エピトープは、細胞内プロテアーゼによって切断可能なリンカーによって分離され、
前記生分解性粒子は、負のゼータ電位を有する、生分解性粒子。 - 前記生分解性粒子はポリ(ラクチド-コ-グリコリド)(PLG)を含む、請求項1に記載の生分解性粒子。
- 前記生分解性粒子は、50:50のポリ乳酸:ポリグリコール酸のコポリマー比でPLGを含む、請求項1または2のいずれか一項に記載の生分解性粒子。
- 前記生分解性粒子は、-100mV~0mVのゼータ電位を有する、請求項1~3のいずれか一項に記載の生分解性粒子。
- 前記生分解性粒子は、0.1μm~10μmの直径を有する、請求項1~4のいずれか一項に記載の生分解性粒子。
- 前記リンカーは、細胞のファゴリソソームに位置するプロテアーゼによる特異的切断に感受性のアミノ酸配列、または細胞のサイトゾルに位置するプロテアーゼによる特異的切断に感受性の部位を含む、請求項1~5のいずれか一項に記載の生分解性粒子。
- 前記リンカーは、細胞のファゴリソソームに位置するプロテアーゼによる特異的切断に感受性のアミノ酸配列、及び細胞のサイトゾルに位置するプロテアーゼによる特異的切断に感受性の部位を含む、請求項1~5のいずれか一項に記載の生分解性粒子。
- 前記ファゴリソソームに位置するプロテアーゼによる特異的切断に感受性の前記部位は、フューリンまたはカテプシンプロテアーゼによる切断に感受性である、請求項6または7に記載の生分解性粒子。
- 前記ファゴリソソームに位置するプロテアーゼによる特異的切断に感受性の前記部位は、カテプシンA、カテプシンB、カテプシンC、カテプシンD、カテプシンE、カテプシンF、カテプシンG、カテプシンH、カテプシンK、カテプシンL、カテプシンO、カテプシンW、またはカテプシンZのうちの1つ以上である、請求項6~8のいずれか一項に記載の生分解性粒子。
- 前記リンカーの前記アミノ酸配列は、Gly-Ala-Val-Val-Arg-Gly-Ala(配列番号5141)である、請求項1~9のいずれか一項に記載の生分解性粒子。
- 請求項1~10のいずれか一項に記載の生分解性粒子を含む、薬学的組成物。
- 薬学的に許容される担体または賦形剤をさらに含む、請求項11に記載の薬学的組成物。
- 有効量の請求項1~10のいずれか一項に記載の生分解性粒子を含む、重症筋無力症を有する対象において抗原特異的寛容を誘導するための薬学的組成物。
- 前記有効量の前記生分解性粒子は、対象に、経口、静脈内、舌下、頬側、腸内、局所、直腸、皮下、経鼻、骨内(すなわち、骨内注入)、腹腔内、くも膜下腔内、経皮、または経粘膜投与される、請求項13に記載の薬学的組成物。
- 対象に有効量の請求項1~10のいずれか一項に記載の生分解性粒子を含む、対象において組織再生を増加させるための薬学的組成物。
- 有効量の請求項1~10のいずれか一項に記載の生分解性粒子を含む、対象において防御免疫応答を増大または誘導させるための薬学的組成物。
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US10363288B2 (en) * | 2015-01-14 | 2019-07-30 | National Jewish Health | Insulin mimotopes and methods of using the same |
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KR20190019068A (ko) | 2016-05-18 | 2019-02-26 | 큐 바이오파마, 인크. | T-세포 조절 다량체 폴리펩타이드 및 이의 사용 방법 |
EP3558339B1 (en) | 2016-12-22 | 2024-01-24 | Cue Biopharma, Inc. | T-cell modulatory multimeric polypeptides and methods of use thereof |
EP3565829A4 (en) | 2017-01-09 | 2021-01-27 | Cue Biopharma, Inc. | MULTIMER POLYPEPTIDES T-LYMPHOCYTE MODULATORS AND THEIR METHODS OF USE |
IL269000B2 (en) | 2017-03-15 | 2024-06-01 | Cue Biopharma Inc | Methods for modulating an immune response |
KR102661060B1 (ko) * | 2017-07-06 | 2024-04-25 | 니토 보세키 가부시기가이샤 | 항인간 IgG4 모노클로날 항체, 및 그 항체를 이용한 인간 IgG4 측정 시약 |
EP3678677A4 (en) * | 2017-09-07 | 2021-06-16 | Cue Biopharma, Inc. | ANTIGEN PRESENTATION POLYPEPTIDES AND THEIR METHODS OF USE |
WO2019131769A1 (ja) * | 2017-12-26 | 2019-07-04 | 公立大学法人名古屋市立大学 | 新規抗pad4抗体 |
WO2019139896A1 (en) | 2018-01-09 | 2019-07-18 | Cue Biopharma, Inc. | Multimeric t-cell modulatory polypeptides and methods of use thereof |
CN110041408B (zh) * | 2018-01-16 | 2021-05-18 | 华中科技大学 | 一种小分子多肽及其在制备防治帕金森综合症药物中的应用 |
MX2020013155A (es) | 2018-06-05 | 2021-04-29 | Anji Pharma Us Llc | Composiciones y metodos para tratar la pancreatitis. |
WO2019238686A1 (en) * | 2018-06-13 | 2019-12-19 | Aziende Chimiche Riunite Angelini Francesco - A.C.R.A.F. S.P.A. | Peptides having inhibitory activity on muscarinic receptor m3 |
MX2022000752A (es) * | 2019-07-19 | 2022-03-25 | Univ Michigan Regents | Composiciones y metodos para tratar trastornos autoinmunes. |
US20230302083A1 (en) * | 2020-04-20 | 2023-09-28 | The General Hospital Corporation | Highly-networked coronavirus immunogen composition |
KR20230009872A (ko) | 2020-05-12 | 2023-01-17 | 큐 바이오파마, 인크. | 다량체 t-세포 조절 폴리펩타이드 및 이의 사용 방법 |
IT202000010888A1 (it) * | 2020-05-13 | 2021-11-13 | Consiglio Nazionale Ricerche | Nanovescicole di mielina e loro impieghi |
GB202017119D0 (en) * | 2020-10-28 | 2020-12-09 | Oxford Vacmedix Uk Ltd | Polypeptides for cancer treatment |
CA3215545A1 (en) | 2021-04-16 | 2022-10-20 | John PUISIS | Method of tracking maintenance of immunological tolerance |
WO2022238689A1 (en) * | 2021-05-11 | 2022-11-17 | Oxford Vacmedix UK Limited | Vaccine formulation comprising recombinant overlapping peptides and native prtoeins |
EP4368629A1 (en) * | 2021-07-07 | 2024-05-15 | Osaka University | Peptide and composition |
WO2023070104A1 (en) | 2021-10-21 | 2023-04-27 | Cour Pharmaceuticals Development Company Inc. | Treatment of primary biliary cholangitis (pbc) with tolerizing nanoparticles |
WO2023097260A1 (en) * | 2021-11-24 | 2023-06-01 | Cour Pharmaceuticals Development Company Inc. | Preparation of tolerizing nanoparticles for the treatment of peanut allergy |
WO2023180547A1 (en) * | 2022-03-24 | 2023-09-28 | Julius-Maximilians-Universität Würzburg | Mhc ib-mediated islet-antigen-specific immunosuppression as a novel treatment for type 1 diabetes |
WO2023212341A1 (en) | 2022-04-29 | 2023-11-02 | Cour Pharmaceuticals Development Company Inc. | Tolerizing immune modifying nanoparticles for overcoming the immunogenicity of therapeutic vectors and proteins |
CN115541872A (zh) * | 2022-09-22 | 2022-12-30 | 中山大学肿瘤防治中心(中山大学附属肿瘤医院、中山大学肿瘤研究所) | 一种pd-l1检测试剂盒及其检测方法 |
WO2024086706A1 (en) | 2022-10-19 | 2024-04-25 | Cour Pharmaceuticals Development Company Inc. | Treatment of peanut allergy with tolerizing nanoparticles |
CN115771883B (zh) * | 2022-11-28 | 2024-02-23 | 淮阴工学院 | 从酿酒酵母发酵液中提取的蛋白酶a在化学法合成纳米硒形貌控制和稳定性影响中的用途 |
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WO2015023796A2 (en) | 2013-08-13 | 2015-02-19 | Shea Lonnie D | Peptide conjugated particles |
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US20190365656A1 (en) | 2019-12-05 |
EP3400069A1 (en) | 2018-11-14 |
IL260296B1 (en) | 2023-09-01 |
IL304580A (en) | 2023-09-01 |
IL260296B2 (en) | 2024-01-01 |
JP2021143206A (ja) | 2021-09-24 |
IL260296A (en) | 2018-08-30 |
JP2019507113A (ja) | 2019-03-14 |
JP2023160828A (ja) | 2023-11-02 |
EP3400069A4 (en) | 2019-09-25 |
US20240122864A1 (en) | 2024-04-18 |
WO2017120222A1 (en) | 2017-07-13 |
CA3009799A1 (en) | 2017-07-13 |
JP6904959B2 (ja) | 2021-07-21 |
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