title: Population variability of the FimH type 1 fimbrial adhesin in Klebsiella pneumoniae.
abstract: 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.
authors.affiliation: Department of Bacteriology, Mycology and Parasitology, Statens Serum Institut, 2300 Copenhagen S, Denmark.
authors.forename: Steen G
authors.initials: SG
authors.lastname: Stahlhut
authors.forename: Sujay
authors.initials: S
authors.lastname: Chattopadhyay
authors.forename: Carsten
authors.initials: C
authors.lastname: Struve
authors.forename: Scott J
authors.initials: SJ
authors.lastname: Weissman
authors.forename: Pavel
authors.initials: P
authors.lastname: Aprikian
authors.forename: Stephen J
authors.initials: SJ
authors.lastname: Libby
authors.forename: Ferric C
authors.initials: FC
authors.lastname: Fang
authors.forename: Karen Angeliki
authors.initials: KA
authors.lastname: Krogfelt
authors.forename: Evgeni V
authors.initials: EV
authors.lastname: Sokurenko
mesh_terms: D018829:Adhesins, Bacterial / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D000595:Amino Acid Sequence; D001422:Bacterial Adhesion; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D014644:Genetic Variation; D007710:Klebsiella Infections / Q000382:microbiology*; D007711:Klebsiella pneumoniae / Q000145:classification / Q000235:genetics* / Q000302:isolation & purification / Q000502:physiology; D008969:Molecular Sequence Data; D009154:Mutation; D010802:Phylogeny; D016415:Sequence Alignment
chemical_list: D018829:Adhesins, Bacterial; D001426:Bacterial Proteins