Characterization of Borrelia burgdorferi glycoconjugates and surface carbohydrates.
Borrelia burgdorferi glycoconjugates with different oligosaccharide structures were characterized by a blotting technique with peroxidase-labelled lectins. The localization of surface carbohydrates was studied using electron microscopy with lectin-gold complexes. A high-mannose glycan structure was detected in 83 kDa glycoprotein (major extracellular protein); at least four carbohydrates (glucose or mannose, galactose, N-acetylgalactosamine and N-acetylglucosamine) were present in other Borrelia glycoconjugates. N-acetylneuraminic (sialic) acid was detected on the Borrelia surface. Two sialidases with different specificities were used in an attempt to cleave off the Borrelia N-acetylneuraminic acid. The attempt was successful by using Vibrio cholerae sialidase which has a broad substrate specificity, while the mumps-virus sialidase with restricted substrate specificity had no effect. Endogenous activity of N-acetylneuraminidase was not demonstrated in B. burgdorferi K 5 and B 31 strains.
Hulínská
D
D
Institute of Hygiene and Epidemiology, Prague.
Volf
P
P
Grubhoffer
L
L
D000818:Animals; D015748:Borrelia burgdorferi Group / Q000737:chemistry* / Q000201:enzymology / Q000648:ultrastructure; D002241:Carbohydrates / Q000032:analysis*; D004591:Electrophoresis, Polyacrylamide Gel; D006001:Glycoconjugates / Q000032:analysis*; D006801:Humans; D015151:Immunoblotting; D007150:Immunohistochemistry; D037102:Lectins; D008854:Microscopy, Electron; D019158:N-Acetylneuraminic Acid; D009439:Neuraminidase / Q000032:analysis; D012794:Sialic Acids / Q000032:analysis
D002241:Carbohydrates; D006001:Glycoconjugates; D037102:Lectins; D012794:Sialic Acids; D009439:Neuraminidase; D019158:N-Acetylneuraminic Acid