title: Quantitative differences in adhesiveness of type 1 fimbriated Escherichia coli due to structural differences in fimH genes.
abstract: Type 1 fimbriae are heteropolymeric surface organelles responsible for the D-mannose-sensitive (MS) adhesion of Escherichia coli. We recently reported that variation of receptor specificity of type 1 fimbriae can result solely from minor alterations in the structure of the gene for the FimH adhesin subunit. To further study the relationship between allelic variation of the fimH gene and adhesive properties of type 1 fimbriae, the fimH genes from five additional strains were cloned and used to complement the FimH deletion in E. coli KB18. When the parental and recombinant strains were tested for adhesion to immobilized mannan, a wide quantitative range in the ability of bacteria to adhere was noted. The differences in adhesion do not appear to be due to differences in the levels of fimbriation or relative levels of incorporation of FimH, because these parameters were similar in low-adhesion and high-adhesion strains. The nucleotide sequence for each of the fimH genes was determined. Analysis of deduced FimH sequences allowed identification of two sequence homology groups, based on the presence of Asn-70 and Ser-78 or Ser-70 and Asn-78 residues. The consensus sequences for each group conferred very low adhesion activity, and this low-adhesion phenotype predominated among a group of 43 fecal isolates. Strains isolated from a different host niche, the urinary tract, expressed type 1 fimbriae that conferred an increased level of adhesion. The results presented here strongly suggest that the quantitative variations in MS adhesion are due primarily to structural differences in the FimH adhesin. The observed differences in MS adhesion among populations of E. coli isolated from different host niches call attention to the possibility that phenotypic variants of FimH may play a functional role in populations dynamics.
authors.affiliation: Department of Anatomy and Neurobiology, University of Tennessee, Memphis 38163, USA.
authors.forename: E V
authors.initials: EV
authors.lastname: Sokurenko
authors.forename: H S
authors.initials: HS
authors.lastname: Courtney
authors.forename: J
authors.initials: J
authors.lastname: Maslow
authors.forename: A
authors.initials: A
authors.lastname: Siitonen
authors.forename: D L
authors.initials: DL
authors.lastname: Hasty
mesh_terms: D018829:Adhesins, Bacterial / Q000096:biosynthesis / Q000235:genetics*; D018830:Adhesins, Escherichia coli; D000595:Amino Acid Sequence; D001422:Bacterial Adhesion / Q000187:drug effects / Q000235:genetics* / Q000502:physiology; D001483:Base Sequence; D002478:Cells, Cultured; D003001:Cloning, Molecular; D016384:Consensus Sequence; D004847:Epithelial Cells; D004848:Epithelium / Q000382:microbiology; D004926:Escherichia coli / Q000235:genetics* / Q000502:physiology; D005243:Feces / Q000382:microbiology; D036781:Fimbriae Proteins; D010861:Fimbriae, Bacterial / Q000235:genetics*; D005798:Genes, Bacterial / Q000235:genetics*; D006801:Humans; D007668:Kidney / Q000166:cytology / Q000382:microbiology; D008351:Mannans / Q000378:metabolism; D008766:Methylmannosides / Q000494:pharmacology; D008969:Molecular Sequence Data; D016133:Polymerase Chain Reaction; D011994:Recombinant Proteins / Q000096:biosynthesis; D017422:Sequence Analysis, DNA; D013329:Structure-Activity Relationship; D001743:Urinary Bladder / Q000166:cytology / Q000382:microbiology
chemical_list: D018829:Adhesins, Bacterial; D018830:Adhesins, Escherichia coli; D008351:Mannans; D008766:Methylmannosides; D011994:Recombinant Proteins; C058769:fimH protein, E coli; D036781:Fimbriae Proteins; C008466:methylmannoside