BIROn - Birkbeck Institutional Research Online

    Structural basis of the interaction of the pyelonephritic e. coli adhesin to its human kidney receptor

    Dodson, K.W. and Pinkner, J.S. and Rose, T. and Magnusson, G. and Hultgren, S.J. and Waksman, Gabriel (2001) Structural basis of the interaction of the pyelonephritic e. coli adhesin to its human kidney receptor. Cell 105 (6), pp. 733-743. ISSN 0092-8674.

    Full text not available from this repository.

    Abstract

    PapG is the adhesin at the tip of the P pilus that mediates attachment of uropathogenic Escherichia coli to the uroepithelium of the human kidney. The human specific allele of PapG binds to globoside (GbO4), which consists of the tetrasaccharide GalNAcβ1-3Galα1-4Galβ1-4Glc linked to ceramide. Here, we present the crystal structures of a binary complex of the PapG receptor binding domain bound to GbO4 as well as the unbound form of the adhesin. The biological importance of each of the residues involved in binding was investigated by site-directed mutagenesis. These studies provide a molecular snapshot of a host-pathogen interaction that determines the tropism of uropathogenic E. coli for the human kidney and is critical to the pathogenesis of pyelonephritis.

    Metadata

    Item Type: Article
    School: Birkbeck Schools and Departments > School of Science > Biological Sciences
    Depositing User: Sarah Hall
    Date Deposited: 29 Apr 2019 14:38
    Last Modified: 29 Apr 2019 15:13
    URI: http://eprints.bbk.ac.uk/id/eprint/27348

    Statistics

    Downloads
    Activity Overview
    0Downloads
    43Hits

    Additional statistics are available via IRStats2.

    Archive Staff Only (login required)

    Edit/View Item Edit/View Item