title: Basement membrane carbohydrate as a target for bacterial adhesion: binding of type I fimbriae of Salmonella enterica and Escherichia coli to laminin.
abstract: Adherence of type-1-fimbriate Salmonella enterica and Escherichia coli to immobilized proteins of the extracellular matrix and reconstituted basement membranes was studied. The type-1-fimbriate strain SH401 of S. enterica serovar Enteritidis showed good adherence to laminin, whereas the adherence to fibronectin, type I, type III, type IV or type V collagens was poor. Only minimal adherence to the matrix proteins was seen with a non-fimbriate strain of S. enterica serovar Typhimurium. A specific and mannoside-inhibitable adhesion to laminin was exhibited by the recombinant E. coli strain HB101(pISF101) possessing fim genes of Typhimurium. Adherence to laminin of strain SH401 was inhibited by Fab fragments against purified SH401 fimbriae, and a specific binding to laminin, of the purified fimbriae, was demonstrated using fimbriae-coated fluorescent microparticles. Periodate treatment of laminin abolished the bacterial adhesion as well as the fimbrial binding. Specific adhesion to immobilized laminin was also shown by the type-1-fimbriate E. coli strain 2131 and the recombinant strain E. coli HB101(pPKL4) expressing the cloned type-1-fimbriae genes of E. coli. Adhesion to laminin of strain HB101(pPKL4) was inhibited by mannoside, and no adherence was seen with the fimH mutant E. coli HB101(pPKL5/pPKL53) lacking the fimbrial lectin subunit. The type-1 fimbriate strains also adhered to reconstituted basement membranes from mouse sarcoma cells and human placenta. Adhesion of strains HB101(pISF101) and HB101(pPKL4) to both basement membrane preparations was inhibited by mannoside. We conclude that type-1 fimbriae of S. enterica and E. coli bind to oligomannoside chains of the laminin network in basement membranes.
authors.affiliation: Department of General Microbiology, University of Helsinki, Finland.
authors.forename: M
authors.initials: M
authors.lastname: Kukkonen
authors.forename: T
authors.initials: T
authors.lastname: Raunio
authors.forename: R
authors.initials: R
authors.lastname: Virkola
authors.forename: K
authors.initials: K
authors.lastname: Lähteenmäki
authors.forename: P H
authors.initials: PH
authors.lastname: Mäkelä
authors.forename: P
authors.initials: P
authors.lastname: Klemm
authors.forename: S
authors.initials: S
authors.lastname: Clegg
authors.forename: T K
authors.initials: TK
authors.lastname: Korhonen
mesh_terms: D018830:Adhesins, Escherichia coli; D001422:Bacterial Adhesion; D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D001485:Basement Membrane / Q000378:metabolism*; D004926:Escherichia coli / Q000378:metabolism*; D036781:Fimbriae Proteins; D010861:Fimbriae, Bacterial / Q000378:metabolism*; D007797:Laminin / Q000378:metabolism*; D008358:Mannose / Q000378:metabolism*; D009844:Oligosaccharides / Q000378:metabolism*; D011993:Recombinant Fusion Proteins / Q000378:metabolism; D012477:Salmonella enteritidis / Q000235:genetics / Q000378:metabolism*; D012486:Salmonella typhimurium / Q000235:genetics / Q000378:metabolism*
chemical_list: D018830:Adhesins, Escherichia coli; D001426:Bacterial Proteins; D007797:Laminin; D009844:Oligosaccharides; D011993:Recombinant Fusion Proteins; C058769:fimH protein, E coli; D036781:Fimbriae Proteins; D008358:Mannose