硕大利什曼原虫表面金属蛋白酶（gp63）锌结合肽的免疫学分析。
Immunological analysis of the zinc-binding peptides of surface metalloproteinase (gp63) of Leishmania major.
作者信息
Yang D, Rogers M V, Brett S J, Liew F Y
机构信息
Department of Immunology, University of Glasgow, U.K.
出版信息
Immunology. 1993 Apr;78(4):582-5.
The surface metalloproteinase, gp63, is highly conserved and immunogenic. A peptide spanning the zinc-binding region of the molecule is immunogenic and can induce protective immunity in mice against Leishmania major infection. We report here that the minimum length of the immunogenic peptide in this region is a heptapeptide, VVTHEMA, corresponding to residues 161-167. Optimal immunogenicity is conferred by a decapeptide, LVTVVTHEMA, corresponding to residues 158 to 167, where H and E are consensus zinc-binding residues. These two residues determine the specificity of the peptide. The next two residues, M and A are necessary for the immunogenicity of the peptide. These results suggest that the zinc-binding residues are recognized by the T-cell receptor complex, while the two adjacent residues are involved in the peptide presentation by the major histocompatibility complex (MHC) molecule.
表面金属蛋白酶gp63高度保守且具有免疫原性。跨越该分子锌结合区域的一段肽具有免疫原性，可在小鼠中诱导针对硕大利什曼原虫感染的保护性免疫。我们在此报告，该区域免疫原性肽的最短长度为七肽VVTHEMA，对应于第161 - 167位氨基酸残基。由十肽LVTVVTHEMA（对应于第158至167位氨基酸残基）赋予最佳免疫原性，其中H和E是共有锌结合残基。这两个残基决定了肽的特异性。接下来的两个残基M和A对于肽的免疫原性是必需的。这些结果表明，锌结合残基被T细胞受体复合物识别，而两个相邻残基参与主要组织相容性复合体（MHC）分子的肽呈递。
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