Bakker D, Willemsen P T, Simons L H, van Zijderveld F G, de Graaf F K
Department of Molecular Microbiology, Faculty of Biology, Vrije Universiteit, de Boelelaan Amsterdam, The Netherlands.
Mol Microbiol. 1992 Jan;6(2):247-55. doi: 10.1111/j.1365-2958.1992.tb02006.x.
The two K88 serotypes, K88ab and K88ac, differ in terms of antigenic and adhesive properties. The structural determinants of the serotype-specific epitopes and the identify of the amino acid residues involved in fimbriae-receptor interaction were studied by the construction and analysis of K88 hybrid proteins in which various parts of the K88ab and K88ac fimbrial subunit FaeG were exchanged, and by in vitro mutagenesis of non-conserved amino acid residues. Using a set of monoclonal antibodies, several regions or amino acid residues involved in the formation of serotype-specific antigenic determinants were located. The haemagglutinating activity of the hybrid and mutant proteins revealed several amino acid residues involved in the formation of the receptor binding site. A clear correlation was found between the receptor binding site and the serotype-specific antigenic determinants.
两种K88血清型，即K88ab和K88ac，在抗原性和黏附特性方面存在差异。通过构建和分析K88杂交蛋白（其中K88ab和K88ac菌毛亚基FaeG的不同部分进行了交换）以及对非保守氨基酸残基进行体外诱变，研究了血清型特异性表位的结构决定因素以及参与菌毛-受体相互作用的氨基酸残基的特性。使用一组单克隆抗体，确定了几个参与血清型特异性抗原决定簇形成的区域或氨基酸残基。杂交蛋白和突变蛋白的血凝活性揭示了几个参与受体结合位点形成的氨基酸残基。发现受体结合位点与血清型特异性抗原决定簇之间存在明显的相关性。
