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'Hôte C, Berger S, Bourgerie S, Duval-Ifiah Y, Julien R, Karamanos Y. Infect Immun 1995; 63: 1927-1932) it clearly appeared that these lectins could be used as probes to detect O-glycans on fibrinogens of other species. The conclusion of the present study is that many mammalian fibrinogens contain complex O-glycans on B beta and gamma chains. In addition, the combined use of the biotinylated K99 lectin and the Peanut agglutinin demonstrated the presence of sialylated T-antigens on the A alpha chains of all the fibrinogens examined. These lectins can now be used to determine differences on the glycosylation status of fibrinogens within one species and also to detect O-glycans on other glycoproteins.
L'Hôte
C
C
Institut de Biotechnologie, Université de Limoges, France.
Berger
S
S
Karamanos
Y
Y
D000818:Animals; D000954:Antigens, Surface / Q000378:metabolism*; D015295:Antigens, Tumor-Associated, Carbohydrate / Q000032:analysis* / Q000378:metabolism; D001427:Bacterial Toxins; D001710:Biotin; D004926:Escherichia coli / Q000276:immunology*; D005340:Fibrinogen / Q000737:chemistry* / Q000378:metabolism; D006031:Glycosylation; D037102:Lectins / Q000378:metabolism*; D008322:Mammals / Q000378:metabolism*; D019887:Peanut Agglutinin; D011134:Polysaccharides / Q000032:analysis* / Q000378:metabolism; D011499:Protein Processing, Post-Translational
D000954:Antigens, Surface; D015295:Antigens, Tumor-Associated, Carbohydrate; D001427:Bacterial Toxins; C031429:K99 antigen; D037102:Lectins; D019887:Peanut Agglutinin; D011134:Polysaccharides; C016467:Thomsen-Friedenreich antigen; D001710:Biotin; D005340:Fibrinogen