Premium
A novel lectin‐independent interaction of P fimbriae of Escherichia coli with immobilized fibronectin
Author(s) -
Westerlund Benita,
Kuusela Pentti,
Vartio Tapio,
van Die Irma,
Korhonen Timo K.
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)80129-2
Subject(s) - fimbria , fibronectin , lectin , escherichia coli , recombinant dna , microbiology and biotechnology , chemistry , biochemistry , binding site , biology , gene , extracellular matrix
Binding of P fimbriae of uropathogenic Escherichia coli to purified human plasma fibronectin and human placental type IV collagen was studied. In an enzyme immunoassay, purified P fimbriae bound strongly to immobilized intact fibronectin and to the aminoterminal 30‐kDa fragment and the 120–140‐kDa carboxyterminal fragments of fibronectin. Binding to the gelatin‐binding 40‐kDa fragment of fibronectin was considerably weaker. No binding to immobilized type IV collagen was seen. The interaction between P fimbriae and immobilized fibronectin was not inhibited by α‐D‐Gal‐(1‐4)‐β‐D‐Gal‐1‐ O ‐Me, a receptor analog of P fimbriae. Moreover, a mutated P fimbria lacking the lectin activity behaved similarly in the adherence assays. Recombinant strains expressing the corresponding cloned fimbriae genes bound to immobilized fibronectin, but no binding to soluble 125 I‐labelled fibronectin was found. The results suggest that P fimbriae interact with immobilized fibronectin and that the binding mechanism does not involve the lectin activity of the fimbriae.