JP2006034296A - Wt1改変ペプチド - Google Patents
Wt1改変ペプチド Download PDFInfo
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Abstract
【解決手段】癌抑制遺伝子WT1産物に基づいて、Cys Tyr Thr Trp Asn Gln Met Asn Leu を含む、9〜30個のアミノ酸からなる、癌抗原ペプチドを作製した。これを、抗原提示細胞とインビトロで接触させ、細胞を体内に戻して細胞性免疫を活性化し、癌細胞を破壊する細胞療法に使用する。
【選択図】なし
Description
HLA−A*2402を有するヒトの末梢血単核球を分離し、これを24ウエルプレートに2×106細胞/ウエルの量で分配し、これにWT1ワイルドペプチド又はWT1改変ペプチドを20μMの濃度になるように添加し、1週間培養した。この際の培地として、45%RPMI、45%AIV、10%FCS、1×非必須アミノ酸、SM/PCGを用いた。上記の培養の後、細胞を2×106細胞/ウエルに調製し、レスポンダー(responder)細胞とした。
内因性(endogeneous)にWT1抗原を発現する白血病細胞(標的細胞)に対する、WT1ワイルドペプチド又はWT1改変ペプチドにより刺激したエフェクター細胞のcell killing活性を51Crリリース法により試験した。標的細胞としてWT1+/A*2402+細胞(#1AML患者の白血病細胞)、WT1−/A*2402+細胞(#2AML患者の白血病細胞)、WT1+/A*2402−細胞(#3AML患者の白血病細胞)、及びWT1−/A*2402−細胞(#4AML患者の白血病細胞)を用いた。
実施例1で調製したエフェクター細胞(E)と上記の標的細胞(T)とを、E/T比20:1で混合し、4時間培養し、細胞溶解の程度を測定した。結果を図2に示す。
この図から明らかな通り、WT1ワイルドペプチド又はWT1改変ペプチドにより刺激された細胞のいずれもWT1+/A*2402細胞に対して細胞毒性活性を示したが、その活性はWT1改変ペプチドの方が高かった。
実施例1と同様の実験を別のHLA−A*2402陽性の健常人の末梢血単核球から調製したエフェクター細胞を用いて試験した。結果を図3に示す。
この図から明らか通り、実施例1と同様にWT1ワイルドペプチドにより刺激した細胞に比べてWT1改変ペプチドにより刺激された細胞の方が強い細胞傷害活性を示した。
WT1ワイルドペプチド又はWT1改変ペプチドで刺激したエフェクター細胞の内因性(endogeneous)にWT1抗原を発現する肺癌由来の癌細胞株(標的細胞)に対する細胞傷害活性を51Crリリース法に従って試験した。標的細胞としてRERF-LCAI(WT1+/A*2402+)、LC1sq(WT1+/A*2402+)、11−18(WT1−/A*2402+)、LK87(WT1+/A*2402−)を用いた。
実施例1と同様な方法により調製したエフェクター細胞(E)と51Crで標識した上記の標的細胞(T)とを、実施例2と同様にE/T比20:1で混合して4時間培養し、細胞溶解の程度を測定した。結果を図4に示す。
この図から明らかな通り、WT1ワイルドペプチド又はWT1改変ペプチドにより刺激された細胞のいずれもWT1+/A*2402+の標的細胞に対してのみ細胞傷害活性を示したが、その活性はWT1改変ペプチドの方が高かった。
WT1ワイルドペプチド又はWT1改変ペプチドで刺激したエフェクター細胞がHLAクラスIに拘束性のCD8陽性キラー細胞であることを抗体を用いたブロッキングアッセイにより確かめた。抗体としては、抗HLAクラスI抗体、抗HLAクラスII抗体、抗CD8抗体を用いた。実施例1と同様な方法により調製したエフェクター細胞(E)、51Crで標識したC1R2402又はWT1ワイルドペプチドをパルスしたC1R2402細胞を標的細胞(T)とし、E/T比20:1で抗体とともに混合して4時間培養し、51Crリリース法に従って細胞溶解の程度を測定した。結果を図5に示す。
この図から明らかな通り、WT1ワイルドペプチド又はWT1改変ペプチドにより刺激された細胞のいずれも抗HLAクラスI抗体及び抗CD8抗体により細胞傷害活性が阻害されており、細胞傷害活性を示す細胞は、HLAクラスIに拘束性のCD8陽性キラー細胞であることが示された。
WT1改変ペプチドとWT1ワイルドペプチドのHLA−A*2402への結合親和性を調べた。C1RA2402細胞を酸緩衝液(131mM クエン酸、66mMリン酸ナトリウム、290m osmol、pH3.3)で1分間処理した後、0.5%のウシ血清アルブミンを含むDMEM培養液を加えて中和した。細胞は、培養液で洗浄した後、200nMのβ2−マイクログロブリン(シグマ社)と0.5%のウシ血清アルブミンを含むDMEM培養液で2×106細胞/mlの濃度に懸濁した。15μlの細胞懸濁液を各種濃度のWT1ペプチドを含む50μlの培養液と混合し、室温で4時間インキュベートした。細胞は洗浄後、FITCで標識したHLA−A24に対するモノクローナル抗体(クローン名7A12)で染色し、フローサイトメーターFACSでHLA−A24発現量を解析した。同様の操作をHLA-A*2402に結合することが報告されているメラノーマ抗原のpmel 15の抗原ペプチド(Ala Tyr Gly Leu Asp Phe Tyr Ile Leu)(配列番号:4)(J. Immunol., 154:5994,1995) についても行い、これをスタンダードとして、文献(Immunogenetics, 51:816,2000)に記載の方法によりWT1ペプチドの解離定数(Kd)を 算出した。結果を表2に示す。
Claims (3)
- Cys Tyr Thr Trp Asn Gln Met Asn Leu(配列番号:3)を含む9〜30個のアミノ酸から成る癌抗原ペプチドと、抗原提示能を有する細胞とをインビトロで接触させる工程を含むことを特徴とする、抗原提示細胞の製造方法。
- 癌抗原ペプチドが配列番号:3に示すアミノ酸配列を含む9〜12個のアミノ酸から成るペプチドである、請求項1に記載の製造方法。
- 癌抗原ペプチドが配列番号:3に示すアミノ酸配列から成るペプチドである、請求項1に記載の製造方法。
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ATE383375T1 (de) | 2008-01-15 |
EP1371664A4 (en) | 2006-03-22 |
JP3728439B2 (ja) | 2005-12-21 |
KR100863853B1 (ko) | 2008-10-15 |
TWI318630B (en) | 2009-12-21 |
ES2298353T3 (es) | 2008-05-16 |
EP1371664B1 (en) | 2008-01-09 |
KR20030084970A (ko) | 2003-11-01 |
DE60224508D1 (de) | 2008-02-21 |
BR0208183A (pt) | 2004-03-02 |
BRPI0208183B8 (pt) | 2021-05-25 |
JPWO2002079253A1 (ja) | 2004-07-22 |
CA2440303A1 (en) | 2002-10-10 |
CA2440303C (en) | 2013-03-19 |
WO2002079253A1 (fr) | 2002-10-10 |
EP1371664A1 (en) | 2003-12-17 |
US8105604B2 (en) | 2012-01-31 |
US20090325886A1 (en) | 2009-12-31 |
US20040097703A1 (en) | 2004-05-20 |
HK1070078A1 (en) | 2005-06-10 |
CN1281625C (zh) | 2006-10-25 |
BRPI0208183B1 (pt) | 2018-08-28 |
DE60224508T2 (de) | 2008-12-24 |
CN1531553A (zh) | 2004-09-22 |
JP3819930B2 (ja) | 2006-09-13 |
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