SIALYLOLIGOSACCHARIDE CHAINS OF LAMININ AS AN EXTRACELLULAR-MATRIX TARGET FOR S FIMBRIAE OF ESCHERICHIA-COLI

Citation
R. Virkola et al., SIALYLOLIGOSACCHARIDE CHAINS OF LAMININ AS AN EXTRACELLULAR-MATRIX TARGET FOR S FIMBRIAE OF ESCHERICHIA-COLI, Infection and immunity, 61(10), 1993, pp. 4480-4484
Citations number
35
Language
INGLESE
art.tipo
Note
Categorie Soggetti
Immunology,"Infectious Diseases
Journal title
ISSN journal
0019-9567
Volume
61
Issue
10
Year of publication
1993
Pages
4480 - 4484
Database
ISI
SICI code
0019-9567(1993)61:10<4480:SCOLAA>2.0.ZU;2-E
Abstract
S fimbriae purified from recombinant Escherichia coli HB101(pANN801-13 ) bound strongly to extracellular matrices of cultured endothelial and epithelial cells; only poor binding was seen with the fimbriae purifi ed from the sfaS mutant strain HB101(pANN801-1321). E. coli HB101(pANN 801-13) adhered strongly to laminin immobilized on glass; no adhesion was seen to type I, III, IV, or V collagen. Strain HB101(pANN801-1321) failed to adhere to any of the target proteins. Adhesion to laminin o f strain HB101(pANN801-13) was inhibited by sialyl-alpha-2,3-lactose a s well as by periodate oxidation and neuraminidase treatment of lamini n. In Western blotting, the purified S fimbriae recognized more strong ly the A chain than the B chains of laminin.