Conservation of the D-mannose-adhesion protein among type 1 fimbriated members of the family Enterobacteriaceae.

Journal Article (Journal Article)

A variety of genera and species of the family Enterobacteriaceae bear surface fimbriae that enable them to bind to D-mannose residues on eukaryotic cells. Until recently, it was thought that the D-mannose binding site was located in the major structural subunit (FimA), of relative molecular mass (Mr) 17,000 (17 K), of these organelles in Escherichia coli. New evidence indicates that this binding site resides instead in a minor protein Mr 28-31 K (FimH) located at the tips and at long intervals along the length of the fimbriae, and is reminiscent of the minor tip adhesion proteins of pyelonephritis-associated pili (Pap) and S fimbriae. In contrast to the antigenic heterogeneity of the major FimA subunit, the antigenic structure of FimH is conserved among different strains of E. coli. Here, we report an even broader conservation of this minor adhesion protein extending to other genera and species of type 1 fimbriated Enterobacteriaceae. Our results may have implications for the development of broadly protective vaccines against Gram-negative bacillary infections in animals and perhaps in man.

Full Text

Duke Authors

Cited Authors

  • Abraham, SN; Sun, D; Dale, JB; Beachey, EH

Published Date

  • December 15, 1988

Published In

Volume / Issue

  • 336 / 6200

Start / End Page

  • 682 - 684

PubMed ID

  • 2904657

International Standard Serial Number (ISSN)

  • 0028-0836

Digital Object Identifier (DOI)

  • 10.1038/336682a0


  • eng

Conference Location

  • England