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Thromb Haemost 1996; 76(05): 710-714
DOI: 10.1055/s-0038-1650648
Original Article
Schattauer GmbH Stuttgart

O-glycosylation of Fibrinogen from Different Mammalian Species as Revealed by the Binding of Escherichia coli Biotinylated Lectins

Corine L’Hôte
The Institut de Biotechnologie, Université de Limoges, Limoges, France
,
Sylvie Berger
The Institut de Biotechnologie, Université de Limoges, Limoges, France
,
Yannis Karamanos
The Institut de Biotechnologie, Université de Limoges, Limoges, France
› Author Affiliations
Further Information

Publication History

Received 19 April 1996

Accepted after revision 25 July 1996

Publication Date:
11 July 2018 (online)

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Summary

After the demonstration that neither N-glycans nor neuraminic acid are involved in the binding of K88 lectins to the Bp and y chains of porcine fibrinogen and that their recognition was due to O-glycans (L’Hôte C, Berger S, Bourgerie S, Duval-Iflah 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 βp and γ 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± 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

 

  • References

  • 1 Berger S, Karamanos Y, Schoentgen F, Julien R. Characterization and used of biotinylated Escherichia coli K99 lectin. Biochim Biophys Acta 1994; 1206: 197-202
    CrossrefPubMedGoogle Scholar
  • 2 Burnette NW. “Western blotting”: Electrophoretic transfer of proteins from sodium dodecyl sulfate-polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein A. AnalBiochem 1981; 112: 195-203
    PubMedGoogle Scholar
  • 3 Bogli C, Hofer A, Furlan M. Isolation of fibrinogen Aa-chain by affinity chromatography on concanavalinA-Sepharose. Thromb Haemost 1988; 60: 308-310
    Article in Thieme ConnectPubMedGoogle Scholar
  • 4 Bourgerie S, Karamanos Y, Berger S, Julien R. Use of resorufin-labelled N-glycopeptide in a high-performance liquid chromatography assay to monitor endoglycosidase activities during cultivation of Flavobacterium meningosepticum. Glycoconjugate J 1992; 9: 162-167
    CrossrefPubMedGoogle Scholar
  • 5 Da Silva CML, Toshiaki T, McBroom V, Rice KG. Tyrosine derivatization and preparative purification of the sialyl and asialyl N-linked oligosaccharides from porcine fibrinogen. Arch Biochem Biophys 1994; 312: 151-157
    CrossrefPubMedGoogle Scholar
  • 6 Damm JBL, Bergwerff AA, Hard K, Kamerling JP, Vliegenthart JFG. Sialic acid patterns in N-linked carbohydrate chains. Structural analysis of N-acetyl-/A-glycolyl-neuraminic-acid-containing N-linked carbohydrate chains of bovine fibrinogen. Reel Trav Chim Pays Bas 1989; 108: 351-359
    PubMedGoogle Scholar
  • 7 Damm JBL, Voshol H, Hard K, Kamerling JP, Vliegenthart JFG. Analysis of N-acetyl-4-O-acetylneuraminic-acid-containing N-linked carbohydrate chains released by peptide-N4-(N-acetyl-p-glucosaminyl) asparagine amidase F. Application to the structure determination of the carbohydrate chains of equine fibrinogen. Eur J Biochem 1989; 180: 101-110
    CrossrefPubMedGoogle Scholar
  • 8 Debeire P, Montreuil J, Moczar E, van Halbeek H. Vliegenthart JFG. Primary structure of two major glycans of bovine fibrinogen. Eur J Biochem 1985; 151: 607-611
    CrossrefPubMedGoogle Scholar
  • 9 Doolittle RF, Watt KWK, Cottrell BA, Strong DD, Riley M. The amino acid sequence of the a-chain of human fibrinogen. Nature 1979; 280: 464-468
    CrossrefPubMedGoogle Scholar
  • 10 Gilman PB, Keane P, Martinez J. The role of the carbohydrate moiety in the biological properties of fibrinogen. J Biol Chem 1984; 259: 3248-3253
    PubMedGoogle Scholar
  • 11 Guinee PAM, Jansen WH, Agtenberg CM. Detection of the K99 antigen by means of agglutination and immunoelectrophoresis in Escherichia coli isolate from calves its correlation with enterotoxigenicity. Infect Immun 1976; 13: 1269-1377
    PubMedGoogle Scholar
  • 12 Haselbeck A, Schickaneder E, von der Eltz H, Wolfgang H. Structural characterization of glycoprotein carbohydrate chains by using digoxigenin-labeled lectins on blots. Anal Biochem 1990; 191: 25-30
    CrossrefPubMedGoogle Scholar
  • 13 Kehl M, Lottspeich F, Henschen A. High-performance liquid chromatography of proteins as applied to fibrinogen chains. Hoppe-Seyler’s Z. Physiol. Chem 1982; 363: 1501-1505
    CrossrefPubMedGoogle Scholar
  • 14 Kottgen E, Hell B, Muller C, Tauber R. Demonstration of glycosylation variants of human fibrinogen, using the new technique of Glycoprotein Lectin Immunosorbent Assay (GLIA). Biol Chem Hoppe-Seyler 1988; 369: 1157-1166
    PubMedGoogle Scholar
  • 15 Kyogashima M, Ginsburg V, Krivan HC. Escherichia coli K99 binds to N-glycolylsialoparagloboside and N-glycolyl-GM3 found in piglet small intestine. Arch Biochem Biophys 1989; 270: 391-397
    CrossrefPubMedGoogle Scholar
  • 16 L’Hote C. Recherche de la specificite des lectines bacteriennes K88ab, K88ac et K88ad: Contribution a la connaissance de la glycosylation du fibrinogene. These de Doctorat Universite de Limoges; 117
  • 17 L’Hote C, Berger S, Bourgerie S, Duval-Iflah Y, Julien R, Karamanos Y. Use of porcine fibrinogen as a model glycoprotein to study the binding specificity of the three variants of K88 lectin. Infect Immun 1995; 63: 192732
    PubMedGoogle Scholar
  • 18 Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970; 227: 680-685
    CrossrefPubMedGoogle Scholar
  • 19 Langer BG, Weisel JW, Dinauer PA, Nagaswami C, Bell WR. Deglyco-sylation of fibrinogen accelerates polymerisation and increases lateral aggregation of fibrin fibers. J Biol Chem 1988; 263: 15056-15063
    PubMedGoogle Scholar
  • 20 Leary JJ, Brigatti DJ, Ward DC. Rapid and sensitive colorimetric method for visualizing biotin-labeled DNA probes hybridized to DNA or RNA immobilized on nitrocellulose: Bio-blots. Proc Natl Acad Sci USA 1983; 80: 4045-4049
    CrossrefPubMedGoogle Scholar
  • 21 Li WP, Zuber C, Roth J. Use of Phaseolus vulgaris leukoagglutinating lectin in histochemical and blotting techniques: a comparison of digoxige-nin- and biotin-labelled lectins. Histochemistry 1993; 100: 347-356
    CrossrefPubMedGoogle Scholar
  • 22 Lindahl M, Carlstedt I. Binding of K99 fimbriae of enterotoxigenic Escherichia coli to pig small intestinal mucin glycopeptides. J Gen Microbiol 1990; 136: 1609-1614
    CrossrefPubMedGoogle Scholar
  • 23 Lowry OH, Rosenbough NJ, Farra L, Randall RI. Protein measurement with the Folin phenol reagent. J Biol Chem 1951; 193: 265-275
    PubMedGoogle Scholar
  • 24 Montreuil J, Bouquelet S, Debray H, Fournet B, Spik G, Strecker G. Glycoproteins. In Carbohydrate Analysis: A practical Approach Chaplin V, and Kennedy JF. Eds IRL; Oxford: 1986: 143-228
  • 25 Ouadia A, Karamanos Y, Julien R. Detection of ganglioside N-glycolyl-neuraminyl-lactosyl-ceramide by biotinylated Escherichia coli K99 lectin. Glycoconjugate J 1992; 9: 21-26
    CrossrefPubMedGoogle Scholar
  • 26 Parekh RB, Dwek RA, Sutton BJ, Fernandes DL, Leung A, Stanwoth D, Rademacher TW, Mizuochi T, Taniguchi T, Matsuta K, Takeuchi F, Nagano Y, Miuamoto T, Kobata A. Association of rheumatoid arthritis and primary osteoarthritis with changes in the glycosylation pattern of total serum IgG. Nature 1985; 316: 452-457
    CrossrefPubMedGoogle Scholar
  • 27 Plummer TH, Tarentino AL. Purification of the oligosaccharide-cleaving enzyme of Flavobacterium meningosepticum. Gly cobiology 1991; 1: 257-263
    PubMedGoogle Scholar
  • 28 Seignole D, Mouricout M, Duval-Iflah Y, Quintard B, Julien R. Adhesion of K99 fimbriated Escherichia coli to pig intestinal epithelium: correlation of adhesive and non-adhesive phenotypes with the sialoglycolipid content. J Gen Microbiol 1991; 137: 1591-1601
    CrossrefPubMedGoogle Scholar
  • 29 Teneberg S, Willemsen P, de Graaf FK, Karlsson KA. Receptor-active gly-colipid of epithelial cells of the small intestine of young and adult pigs in relation to susceptibility to infection with Escherichia coli K99. FEBS Lett 1990; 263: 10-14
    CrossrefPubMedGoogle Scholar
  • 30 Townsend RR, Hilliker E, Li YT, Laine RA, Bell WR, Lee YC. Carbohydrate structure of human fibrinogen. ‘H-NMR to characterize glycosidase-treated gly copeptides. J Biol Chem 1982; 257: 9704-9710
    PubMedGoogle Scholar
  • 31 Watt KWK, Cottrell BA, Strong DD, Doolittle RF. Amino acid sequence studies on the a chain of human fibrinogen. Overlapping sequences providing the complete sequence. Biochemistry 1979; 18: 5410-5416
    CrossrefPubMedGoogle Scholar
  • 32 Watt KWK, Tagaki T, Doolittle RF. Amino acid sequence of the β chain of human fibrinogen. Biochemistry 1979; 18: 68-76
    CrossrefPubMedGoogle Scholar