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. 1995 May;63(5):1927–1932. doi: 10.1128/iai.63.5.1927-1932.1995

Use of porcine fibrinogen as a model glycoprotein to study the binding specificity of the three variants of K88 lectin.

C L'Hôte 1, S Berger 1, S Bourgerie 1, Y Duval-Iflah 1, R Julien 1, Y Karamanos 1
PMCID: PMC173245  PMID: 7729904

Abstract

Known glycoproteins were used to determine the differences occurring in the binding specificities of the three variants of the K88 lectin in an approach essentially based on lectin blotting. During the screening, it was demonstrated that each variant of the K88 lectin biotinylated via its amino groups (NbioK88) exhibited a characteristic binding to the three chains of porcine fibrinogen. NbioK88ab weakly bound to A alpha chains, NbioK88ac bound to B beta and gamma chains, and NbioK88ad bound only to the gamma chain. To validate this model, the oligosaccharide moieties of porcine fibrinogen were analyzed with glycosidases and by lectin blotting and sugar composition. Both the B beta chain and gamma chain carry biantennary N-glycans of the N-acetyllactosamine type that are not recognized by K88 lectins. A alpha chains are substituted by sialylated T antigen. O-glycans were also detected on B beta and gamma chains of porcine fibrinogen and contribute to the recognition of these chains by K88ac and K88ad fimbriae.

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Selected References

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