FimH family of type 1 fimbrial adhesins

Functional heterogeneity due to minor sequence variations among fimH genes

E. V. Sokurenko, H. S. Courtney, D. E. Ohman, P. Klemm, D. L. Hasty

Research output: Contribution to journalArticle

128 Citations (Scopus)

Abstract

We recently reported that the type 1-fimbriated Escherichia coli strains CSH-50 and HB101(pPKL4), both K-12 derivatives, have different patterns of adhesion to yeast mannan, human plasma fibronectin, and fibronectin derivatives, suggesting functional heterogeneity of type 1 fimbriae. In this report, we provide evidence that this functional heterogeneity is due to variations in the fimH genes. We also investigated functional heterogeneity among clinical isolates and whether variation in fimH genes accounts for differences in receptor specificity. Twelve isolates obtained from human urine were tested for their ability to adhere to mannan, fibronectin, periodate-treated fibronectin, and a synthetic peptide copying the 30 amino- terminal residues of fibronectin. CSH-50 and HB101(pPKL4) were tested for comparison. Selected isolates were also tested for adhesion to purified fragments spanning the entire fibronectin molecule. Three distinct functional classes, designated M, MF, and MFP, were observed. The fimH genes were amplified by PCR from chromosomal DNA obtained from representative strains and expressed in a Δfim strain (AAEC191A) transformed with a recombinant plasmid containing the entire fim gene cluster but with a translational stop- linker inserted into the fimH gene (pPKL114). Cloned fimH genes conferred on AAEC191A(pPKL114) receptor specificities mimicking those of the parent strains from which the fimH genes were obtained, demonstrating that the FimH subunits are responsible for the functional heterogeneity. Representative fimH genes were sequenced, and the deduced amino acid sequences were compared with the previously published FimH sequence. Allelic variants exhibiting >98% homology and encoding proteins differing by as little as a single amino acid substitution confer distinct adhesive phenotypes. This unexpected adhesive diversity within the FimH family broadens the scope of potential receptors for enterobacterial adhesion and may lead to a fundamental change in our understanding of the role(s) that type 1 fimbriae may play in enterobacterial ecology or pathogenesis.

Original languageEnglish (US)
Pages (from-to)748-755
Number of pages8
JournalJournal of Bacteriology
Volume176
Issue number3
DOIs
StatePublished - Jan 1 1994

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Bacterial Adhesins
Fibronectins
Genes
Mannans
Adhesives
Amino Acid Substitution
Multigene Family
Ecology
Amino Acid Sequence
Plasmids
Yeasts
Urine
Escherichia coli
Phenotype
Polymerase Chain Reaction
Peptides
DNA

All Science Journal Classification (ASJC) codes

  • Microbiology
  • Molecular Biology

Cite this

FimH family of type 1 fimbrial adhesins : Functional heterogeneity due to minor sequence variations among fimH genes. / Sokurenko, E. V.; Courtney, H. S.; Ohman, D. E.; Klemm, P.; Hasty, D. L.

In: Journal of Bacteriology, Vol. 176, No. 3, 01.01.1994, p. 748-755.

Research output: Contribution to journalArticle

Sokurenko, E. V. ; Courtney, H. S. ; Ohman, D. E. ; Klemm, P. ; Hasty, D. L. / FimH family of type 1 fimbrial adhesins : Functional heterogeneity due to minor sequence variations among fimH genes. In: Journal of Bacteriology. 1994 ; Vol. 176, No. 3. pp. 748-755.
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