O-GLYCOSYLATION OF FIBRINOGEN FROM DIFFERENT MAMMALIAN-SPECIES AS REVEALED BY THE BINDING OF ESCHERICHIA-COLI BIOTINYLATED LECTINS

After the demonstration that neither N-glycans nor neuraminic acid are involved in the binding of K88 lectins to the B beta and gamma chains of porcine fibrinogen and that their recognition was due to O-glycans (L'Hote C, Berger S, Bourgerie S, Duval-Iflah Y, Julien R, Karamanos Y. Infect Immun 1995; 63: 1927-1932) it clearly appeared that these le ctins could be used as probes to detect O-glycans on fibrinogens of ot her species. The conclusion of the present study is that many mammalia n fibrinogens contain complex O-glycans on B beta and gamma chains. In addition, the combined use of the biotinylated K99 lectin and the Pea nut agglutinin demonstrated the presence of sialylated T-antigens on t he A alpha chains of all the fibrinogens examined. These lectins can n ow be used to determine differences on the glycosylation status of fib rinogens within one species and also to detect O-glycans on other glyc oproteins.