EXPRESSION OF BINDING OF PLASMINOGEN, THROMBOSPONDIN, VITRONECTIN, AND FIBRINOGEN, AND ADHESIVE PROPERTIES BY ESCHERICHIA-COLI STRAINS ISOLATED FROM PATIENTS WITH COLONIC DISEASES

Citation
W. Shen et al., EXPRESSION OF BINDING OF PLASMINOGEN, THROMBOSPONDIN, VITRONECTIN, AND FIBRINOGEN, AND ADHESIVE PROPERTIES BY ESCHERICHIA-COLI STRAINS ISOLATED FROM PATIENTS WITH COLONIC DISEASES, Gut, 36(3), 1995, pp. 401-406
Citations number
38
Categorie Soggetti
Gastroenterology & Hepatology
Journal title
GutACNP
ISSN journal
00175749
Volume
36
Issue
3
Year of publication
1995
Pages
401 - 406
Database
ISI
SICI code
0017-5749(1995)36:3<401:EOBOPT>2.0.ZU;2-E
Abstract
Escherichia coli strains isolated from patients with colonic disorders (n = 27) and strains isolated from the rectal mucosa of healthy subje cts (n = 24) were compared with respect to expression of cell surface hydrophobicity, carriage of intestinal virulence factors, adhesion to tissue culture cells, and expression of binding of extracellular matri x proteins and plasma proteins. Strains isolated hom patients with col onic disease did not express a more hydrophobic cell surface than stra ins from healthy subjects. Few strains from both groups carried genes encoding for recognised virulence factors of E coli. Only one strain, carrying the eae gene induced actin polymerisation in tissue culture c ells. Strains from patients with colonic diseases adhered to HT29 cell s, which are of intestinal origin, to a higher extent than E coli from healthy subjects. Significantly more strains from patients with colon ic disorders than E coli from healthy subjects expressed binding of fi bronectin, collagens, laminin, vitronectin, plasminogen, throbospondin , and fibrinogen. Expression of binding of these proteins may influenc e the pathogenesis of colonic disease by mediating binding to ulcerate d tissue, preventing complement induced lysis of bacteria and by exert ing proteolytic activity. There was no correlation between serotype, e xpression of cell surface hydrophobicity, and binding of extracellular matrix and plasma proteins.