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- W2128097988 abstract "Abstract The 16‐kDa protein of Mycobacterium tuberculosis provokes specific immune responses; it is thus a target for the development of peptide‐based diagnostic reagents and subunit vaccines. Previous studies have demonstrated the presence of several regions containing murine and human T‐cell epitopes. Within the 91–110 immunodominant domain, we found that peptides comprising the sequence of 91 SEFAYGSFVRTVSL 104 elicit specific T‐cell responses in both human T‐cell clones and human peripheral blood mononuclear cells (PBMC) from PPD + (purified protein derivative) individuals. Elongation of this peptide towards the C‐terminal end did not provide more effective peptides, but the removal of residue 91 Ser resulted in an almost complete loss of functionality. However, the introduction of an acetyl group at the N‐terminal of residue 92 Glu produced a shorter peptide (Ac‐ 92 EFAYGSFVRTVSL 104 ) exhibiting properties required for efficient T‐cell responses. CD measurements indicated that peptide 91 SEFAYGSFVRTVSLPVGADE 110 adopts a helical conformation in triflouroethanol. We found that the N‐terminal part of this sequence plays a major role in the induction of proliferative T‐cell responses and is responsible for the highly ordered, helical secondary structure. The “lead” structure described here could also be considered in the development of synthetic peptides or multicomponent peptide mixtures for the early detection, monitoring, or preventing Mycobacterium tuberculosis infection with optimized T‐cell response‐provoking capacity. © 2004 Wiley Periodicals, Inc. Biopolymers (Pept Sci), 2004" @default.
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- W2128097988 date "2004-01-01" @default.
- W2128097988 modified "2023-10-18" @default.
- W2128097988 title "In vitro T-cell immunogenicity of oligopeptides derived from the region 92-110 of the 16-kDa protein ofMycobacterium tuberculosis" @default.
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- W2128097988 doi "https://doi.org/10.1002/bip.20153" @default.
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