Characterization of the antigenic and adhesive properties of FaeG, the major subunit of K88 fimbriae.
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.
Department of Molecular Microbiology, Faculty of Biology, Vrije Universiteit, de Boelelaan Amsterdam, The Netherlands.
D
D
Bakker
P T
PT
Willemsen
L H
LH
Simons
F G
FG
van Zijderveld
F K
FK
de Graaf
D000595:Amino Acid Sequence; D000911:Antibodies, Monoclonal; D000942:Antigens, Bacterial / Q000235:genetics / Q000276:immunology*; D000954:Antigens, Surface / Q000235:genetics / Q000276:immunology*; D001483:Base Sequence; D000939:Epitopes; D004926:Escherichia coli / Q000737:chemistry* / Q000235:genetics / Q000276:immunology; D029968:Escherichia coli Proteins; D036781:Fimbriae Proteins; D010861:Fimbriae, Bacterial / Q000737:chemistry* / Q000276:immunology; D006384:Hemagglutination; D008969:Molecular Sequence Data; D009154:Mutation
D000911:Antibodies, Monoclonal; D000942:Antigens, Bacterial; D000954:Antigens, Surface; D000939:Epitopes; D029968:Escherichia coli Proteins; C026888:K88 antigen, E coli; D036781:Fimbriae Proteins