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J Bacteriol. 1994 February; 176(3): 748-755

research-article

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 and D L Hasty

Department of Anatomy, University of Tennessee, Memphis 38163.

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 delta fim 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.

J Bacteriol. 1994 February; 176(3): 748-755




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