@article{mbs:/content/journal/micro/10.1099/13500872-140-9-2467, author = "Seignole, Didier and Grange, Philippe and Duval-Iflah, Yvonne and Mouricout, Michèle", title = "Characterization of O-glycan moieties of the 210 and 240 kDa pig intestinal receptors for Escherichia coli K88ac fimbriae", journal= "Microbiology", year = "1994", volume = "140", number = "9", pages = "2467-2473", doi = "https://doi.org/10.1099/13500872-140-9-2467", url = "https://www.microbiologyresearch.org/content/journal/micro/10.1099/13500872-140-9-2467", publisher = "Microbiology Society", issn = "1465-2080", type = "Journal Article", keywords = "pig intestinal receptors", keywords = "E. coli K88ac fimbriae", keywords = "lectin binding", keywords = "O-glycan moieties", 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 Fucα1-2Galβ1-3/4GIcNAc- 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.", }