Sun D X, Seyer J M, Kovari I, Sumrada R A, Taylor R K
Department of Microbiology, University of Tennessee, Memphis 38163.
Infect Immun. 1991 Jan;59(1):114-8. doi: 10.1128/iai.59.1.114-118.1991.
From a collection of monoclonal antibodies (MAbs) that recognize the native structure of the toxin-coregulated pilus of Vibrio cholerae, two protective MAbs (16.1 and 169.1) were used to localize the corresponding epitopes on the pilus. These MAbs were shown to specifically recognize the carboxyl half of the TcpA pilin subunit, as determined by their recognition of proteolytic fragments and hybrid pilin proteins. The positions of the epitopes were precisely determined through the use of overlapping synthetic peptides corresponding to this region of the pilin. The MAbs were found to recognize adjacent peptides, delineating a region between residues 157 and 199. Since the protective nature is specific for these two antibodies, the findings suggest that this region defines a domain that participates in toxin-coregulated pilus-mediated colonization and therefore represents a target for studies of its potential as an immunogen for incorporation into a component cholera vaccine.
从一组识别霍乱弧菌毒素协同菌毛天然结构的单克隆抗体（MAb）中，选取了两种具有保护作用的单克隆抗体（16.1和169.1）来定位菌毛上相应的表位。通过它们对蛋白水解片段和杂交菌毛蛋白的识别确定，这些单克隆抗体可特异性识别TcpA菌毛蛋白亚基的羧基端一半。通过使用与该菌毛蛋白区域相对应的重叠合成肽，精确确定了表位的位置。发现这些单克隆抗体识别相邻的肽段，划定了157至199位氨基酸残基之间的区域。由于只有这两种抗体具有保护特性，这些发现表明该区域定义了一个参与毒素协同菌毛介导的定植的结构域，因此代表了一个研究其作为免疫原并入霍乱疫苗成分潜力的靶点。
