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Volume 140, Issue 9

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

Abstract

The porcine brush border glycoproteins of 210 and 240 kDa, recognized by K88ac fimbriae, contained -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 -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 of the erythrocytes of the hamster was inhibited by the anti- peanut lectin and the lectins of and . 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.

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Keyword(s): E. coli K88ac fimbriae , lectin binding , O-glycan moieties and pig intestinal receptors
© Society for General Microbiology 1994
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1994-09-01
2025-05-16
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/content/journal/micro/10.1099/13500872-140-9-2467
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Characterization of O-glycan moieties of the 210 and 240 kDa pig intestinal receptors for Escherichia coli K88ac fimbriae
Microbiology 140, 2467 (1994); https://doi.org/10.1099/13500872-140-9-2467
/content/journal/micro/10.1099/13500872-140-9-2467
/content/journal/micro/10.1099/13500872-140-9-2467
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