title: A conserved residue in the tip proteins of CS1 and CFA/I pili of enterotoxigenic Escherichia coli that is essential for adherence.
abstract: Enterotoxigenic Escherichia coli associated with human diarrheal disease utilize any of a limited group of serologically distinguishable pili for attachment to intestinal cells. These include CS1 and CFA/I pili. We show here that chemical modification of arginyl residues in CS1 pili abolishes CS1-mediated agglutination of bovine erythrocytes, which serves as a model system for attachment. Alanine substitution of the single arginyl residue in CooA, the major pilin, had no effect on the assembly of pili or on hemagglutination. In contrast, substitution of alanine for R181 in CooD, the minor pilin associated with the pilus tip, abolished hemagglutination, and substitution of R20 reduced hemagglutination. Neither of these substitutions affected CS1 pilus assembly. This shows that CooD is essential for CS1-mediated attachment and identifies specific residues that are involved in receptor binding but not in pilus assembly. In addition to mediating agglutination of bovine erythrocytes, CFA/I also mediates agglutination of human erythrocytes. Substitution of R181 by alanine in the CooD homolog, CfaE, abolished both of these reactions. We conclude that the same region of the pilus tip protein is involved in adherence of CS1 and CFA/I pili, although their receptor specificities differ. This suggests that the region of the pilus tip adhesin protein that includes R181 might be an appropriate target for therapeutic intervention or for a vaccine to protect against human diarrhea caused by enterotoxigenic E. coli strains that have serologically different pili.
authors.affiliation: Department of Microbiology, Emory University School of Medicine, Atlanta, GA, 30322, USA.
authors.forename: H
authors.initials: H
authors.lastname: Sakellaris
authors.forename: G P
authors.initials: GP
authors.lastname: Munson
authors.forename: J R
authors.initials: JR
authors.lastname: Scott
mesh_terms: D000595:Amino Acid Sequence; D001120:Arginine / Q000502:physiology; D001422:Bacterial Adhesion / Q000502:physiology*; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000502:physiology*; D017124:Conserved Sequence; D004926:Escherichia coli / Q000737:chemistry / Q000502:physiology*; D029968:Escherichia coli Proteins; D036781:Fimbriae Proteins; D010861:Fimbriae, Bacterial / Q000737:chemistry / Q000502:physiology*; D006386:Hemagglutination Tests; D008854:Microscopy, Electron; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed
chemical_list: D001426:Bacterial Proteins; C088904:CooA protein, E coli; D029968:Escherichia coli Proteins; C022924:colonization factor antigens; D036781:Fimbriae Proteins; D001120:Arginine