title: Long polar fimbriae of enterohemorrhagic Escherichia coli O157:H7 bind to extracellular matrix proteins.
abstract: Adherence to intestinal cells is a key process in infection caused by enterohemorrhagic Escherichia coli (EHEC). Several adhesion factors that mediate the binding of EHEC to intestinal cells have been described, but the receptors involved in their recognition are not fully characterized. Extracellular matrix (ECM) proteins might act as receptors involved in the recognition of enteric pathogens, including EHEC. In this study, we sought to characterize the binding of EHEC O157:H7 to ECM proteins commonly present in the intestine. We found that EHEC prototype strains as well as other clinical isolates adhered more abundantly to surfaces coated with fibronectin, laminin, and collagen IV. Further characterization of this phenotype, by using antiserum raised against the LpfA1 putative major fimbrial subunit and by addition of mannose, showed that a reduced binding of EHEC to ECM proteins was observed in a long polar fimbria (lpf) mutant. We also found that the two regulators, H-NS and Ler, had an effect in EHEC Lpf-mediated binding to ECM, supporting the roles of these tightly regulated fimbriae as adherence factors. Purified Lpf major subunit bound to all of the ECM proteins tested. Finally, increased bacterial adherence was observed when T84 cells, preincubated with ECM proteins, were infected with EHEC. Taken together, these findings suggest that the interaction of Lpf and ECM proteins contributes to the EHEC colonization of the gastrointestinal tract.
authors.affiliation: Centro de Estudios Moleculares, Departamento de Pediatría, Hospital Dr. Luis Calvo Mackenna, Santiago, Chile. mfarfan@med.uchile.cl
authors.forename: Mauricio J
authors.initials: MJ
authors.lastname: Farfan
authors.forename: Lidia
authors.initials: L
authors.lastname: Cantero
authors.forename: Roberto
authors.initials: R
authors.lastname: Vidal
authors.forename: Douglas J
authors.initials: DJ
authors.lastname: Botkin
authors.forename: Alfredo G
authors.initials: AG
authors.lastname: Torres
mesh_terms: D000906:Antibodies / Q000276:immunology; D001422:Bacterial Adhesion; D001426:Bacterial Proteins / Q000378:metabolism; D045744:Cell Line, Tumor; D024141:Collagen Type IV / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000378:metabolism; D004797:Enzyme-Linked Immunosorbent Assay; D019453:Escherichia coli O157 / Q000235:genetics / Q000378:metabolism* / Q000648:ultrastructure; D029968:Escherichia coli Proteins / Q000235:genetics / Q000378:metabolism; D016326:Extracellular Matrix Proteins / Q000378:metabolism*; D005353:Fibronectins / Q000378:metabolism; D036781:Fimbriae Proteins / Q000276:immunology / Q000378:metabolism; D010861:Fimbriae, Bacterial / Q000276:immunology / Q000378:metabolism*; D006801:Humans; D007413:Intestinal Mucosa / Q000378:metabolism; D007422:Intestines / Q000382:microbiology; D007797:Laminin / Q000378:metabolism; D011994:Recombinant Proteins / Q000378:metabolism; D015534:Trans-Activators / Q000378:metabolism
chemical_list: D000906:Antibodies; D001426:Bacterial Proteins; D024141:Collagen Type IV; D004268:DNA-Binding Proteins; D029968:Escherichia coli Proteins; D016326:Extracellular Matrix Proteins; D005353:Fibronectins; C031908:H-NS protein, bacteria; D007797:Laminin; C465556:Ler protein, E coli; D011994:Recombinant Proteins; D015534:Trans-Activators; D036781:Fimbriae Proteins