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Journal of Bacteriology, March 2009, p. 1941-1950, Vol. 191, No. 6
0021-9193/09/$08.00+0     doi:10.1128/JB.00601-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Population Variability of the FimH Type 1 Fimbrial Adhesin in Klebsiella pneumoniae{triangledown}

Steen G. Stahlhut,1,{dagger} Sujay Chattopadhyay,2,{dagger} Carsten Struve,1 Scott J. Weissman,2 Pavel Aprikian,2 Stephen J. Libby,3 Ferric C. Fang,2,3 Karen Angeliki Krogfelt,1* and Evgeni V. Sokurenko2

Department of Bacteriology, Mycology and Parasitology, Statens Serum Institut, 2300 Copenhagen S, Denmark,1 Departments of Microbiology,2 Laboratory Medicine University of Washington School of Medicine, Seattle, Washington 981953

Received 30 April 2008/ Accepted 16 December 2008

FimH is an adhesive subunit of type 1 fimbriae expressed by different enterobacterial species. The enteric bacterium Klebsiella pneumoniae is an environmental organism that is also a frequent cause of sepsis, urinary tract infection (UTI), and liver abscess. Type 1 fimbriae have been shown to be critical for the ability of K. pneumoniae to cause UTI in a murine model. We show here that the K. pneumoniae fimH gene is found in 90% of strains from various environmental and clinical sources. The fimH alleles exhibit relatively low nucleotide and structural diversity but are prone to frequent horizontal-transfer events between different bacterial clones. Addition of the fimH locus to multiple-locus sequence typing significantly improved the resolution of the clonal structure of pathogenic strains, including the K1 encapsulated liver isolates. In addition, the K. pneumoniae FimH protein is targeted by adaptive point mutations, though not to the same extent as FimH from uropathogenic Escherichia coli or TonB from the same K. pneumoniae strains. Such adaptive mutations include a single amino acid deletion from the signal peptide that might affect the length of the fimbrial rod by affecting FimH translocation into the periplasm. Another FimH mutation (S62A) occurred in the course of endemic circulation of a nosocomial uropathogenic clone of K. pneumoniae. This mutation is identical to one found in a highly virulent uropathogenic strain of E. coli, suggesting that the FimH mutations are pathoadaptive in nature. Considering the abundance of type 1 fimbriae in Enterobacteriaceae, our present finding that fimH genes are subject to adaptive microevolution substantiates the importance of type 1 fimbria-mediated adhesion in K. pneumoniae.

* Corresponding author. Mailing address: Department of Bacteriology, Mycology and Parasitology, Statens Serum Institut, Artillerivej 5, 2300 Copenhagen S, Denmark. Phone: 45 32683745. Fax: 45 32688238. E-mail: kak{at}ssi.dk

{triangledown} Published ahead of print on 16 January 2009.

{dagger} S.G.S. and S.C. contributed equally to this work.

Journal of Bacteriology, March 2009, p. 1941-1950, Vol. 191, No. 6
0021-9193/09/$08.00+0     doi:10.1128/JB.00601-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Stahlhut, S. G., Tchesnokova, V., Struve, C., Weissman, S. J., Chattopadhyay, S., Yakovenko, O., Aprikian, P., Sokurenko, E. V., Krogfelt, K. A. (2009). Comparative Structure-Function Analysis of Mannose-Specific FimH Adhesins from Klebsiella pneumoniae and Escherichia coli. J. Bacteriol. 191: 6592-6601 [Abstract] [Full Text]  


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