Definition of a minimal optimal cytotoxic T-cell epitope within the hepatitis B virus nucleocapsid protein
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- A Bertoletti
- Cattedra Malattie Infettive, Università di Parma, Italy.
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- F V Chisari
- Cattedra Malattie Infettive, Università di Parma, Italy.
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- A Penna
- Cattedra Malattie Infettive, Università di Parma, Italy.
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- S Guilhot
- Cattedra Malattie Infettive, Università di Parma, Italy.
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- L Galati
- Cattedra Malattie Infettive, Università di Parma, Italy.
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- G Missale
- Cattedra Malattie Infettive, Università di Parma, Italy.
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- P Fowler
- Cattedra Malattie Infettive, Università di Parma, Italy.
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- H J Schlicht
- Cattedra Malattie Infettive, Università di Parma, Italy.
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- A Vitiello
- Cattedra Malattie Infettive, Università di Parma, Italy.
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- R C Chesnut
- Cattedra Malattie Infettive, Università di Parma, Italy.
書誌事項
- 公開日
- 1993-04
- 権利情報
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- https://journals.asm.org/non-commercial-tdm-license
- DOI
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- 10.1128/jvi.67.4.2376-2380.1993
- 公開者
- American Society for Microbiology
この論文をさがす
説明
<jats:p>Residues 11 to 27 of the hepatitis B virus nucleocapsid antigen contain a cytotoxic T-cell epitope that is recognized by cytotoxic T cells from virtually all HLA-A2-positive patients with acute hepatitis B virus infection. Using panels of truncated and overlapping peptides, we now show that the optimal amino acid sequence recognized by cytotoxic T cells is a 10-mer (residues 18 to 27) containing the predicted peptide-binding motif for HLA-A2 and that this peptide can stimulate cytotoxic T cells able to recognize endogenously synthesized hepatitis B core antigen. Since patients with chronic hepatitis B virus infection fail to mount an efficient cytotoxic T-cell response to it, this epitope might serve as the starting point for the design of synthetic peptide-based immunotherapeutic strategies to terminate persistent viral infection.</jats:p>
収録刊行物
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- Journal of Virology
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Journal of Virology 67 (4), 2376-2380, 1993-04
American Society for Microbiology