Characterization of O-glycan moieties of the 210 and 240 kDa pig intestinal receptors for Escherichia coli K88ac fimbriae

• Published in: Microbiology (Society for General Microbiology) 1994-09, Vol.140 (9), p.2467-2473
• Main Authors: Seignole, Didier, Grange, Philippe, Duval-Iflah, Yvonne, Mouricout, Michele
• Format: Article
• Language: English
• Subjects: alpha-L-Fucosidase - pharmacology; Animals; Bacterial Adhesion - drug effects; Bacteriology; Biological and medical sciences; Carbohydrate Sequence; Cricetinae; Escherichia coli; Fimbriae, Bacterial - metabolism; Fundamental and applied biological sciences. Psychology; Glycoproteins - chemistry; Glycoproteins - metabolism; Glycosylation; Hemagglutination - drug effects; In Vitro Techniques; Jejunum - metabolism; Jejunum - microbiology; Lectins - chemistry; Lectins - pharmacology; Life Sciences; Microbiology; Microbiology and Parasitology; Microvilli - metabolism; Molecular Sequence Data; Molecular Weight; Neuraminidase - pharmacology; Oligosaccharides - chemistry; Oligosaccharides - metabolism; Pathogenicity, virulence, toxins, bacteriocins, pyrogens, host-bacteria relations, miscellaneous strains; Polysaccharides - chemistry; Polysaccharides - metabolism; Swine
• ISSN: 1350-0872; 1465-2080
• DOI: 10.1099/13500872-140-9-2467

1 Biotechnologie, Faculté des Sciences, Université de Limoges, 123 avenue A. Thomas, 87060, Limoges cedex, France 2 INRA, UEPSD, Jouy en Josas 78350, France ABSTRACT The porcine brush border glycoproteins of 210 and 240 kDa, recognized by Escherichia coli K88ac fimbriae, contained O -linked oligosaccharides. The carbohydrate moieties were analysed by deglycosylation, lectin-binding and agglutination assays. Neuraminidase susceptibility of the 210 kDa receptor suggested that a sialoglycoprotein may act as receptor for the K88ac fimbriae. In contrast, K88ac-binding to the 210 and 240 kDa glycoproteins totally disappeared after fucosidase treatment, indicating the critical role of fucosyl residues at the receptor sites. Among the oligosaccharides extracted from these O -glycoproteins, K88ac fimbriae showed affinity for neutral sugar chains while sialylated species were not recognized. Our data suggest a possible role of the polypeptide backbone in the definition of receptor sites. Specific agglutination by K88ac-fimbriated E. coli of the erythrocytes of the hamster Mesocricetus auratus was inhibited by the anti- T peanut lectin and the lectins of Datura stramonium, Aleuria aurantia and Maackia amurensis. Hence, we propose that Galβ1-3GalNAc- and Fuc 1-2Galβ1-3/4GIcNAc- are the main sequences mediating K88ac fimbrial binding. These structures were not detected in the non-adhesive piglet brush borders characterized by a high carbohydrate content. Additional oligosaccharides probably masked the underlying receptor structures. Author for correspondence: Michèle Mouricout. Tel: [phone]. Fax: [phone]. Keywords: pig intestinal receptors, O -glycan moieties, E. coli K88ac fimbriae, lectin binding