Effects of glycosylation on the conformation and antigenicity of influenza C viral glycoproteins.
The antigenicity of influenza C viral glycoprotein gp88 was compared with that of its non-glycosylated counterpart T76 by immunoprecipitation utilizing monoclonal antibodies against gp88. Of the three monoclonal antibodies tested, an antibody designated Q-5 was found to precipitate gp88 but not T76, indicating the requirement for glycosylation for the binding of Q-5 to gp88. However, the antigenic determination recognized by Q-5 did not appear to be carbohydrates since trypsin-treatment of gp88 eliminated its reactivity with this antibody. These results suggest that glycosylation is important in determining the antigenicity of gp88 presumably by influencing the folding of the glycoproteins.
Hongo
S
S
Sugawara
K
K
Homma
M
M
Nakamura
K
K
D000911:Antibodies, Monoclonal / Q000276:immunology; D000956:Antigens, Viral / Q000276:immunology*; D000939:Epitopes / Q000276:immunology; D006023:Glycoproteins / Q000276:immunology*; D006027:Glycosides / Q000276:immunology; D009982:Gammainfluenzavirus / Q000276:immunology*; D019158:N-Acetylneuraminic Acid; D009844:Oligosaccharides / Q000276:immunology; D009975:Orthomyxoviridae / Q000276:immunology*; D011487:Protein Conformation; D012794:Sialic Acids / Q000276:immunology; D014764:Viral Proteins / Q000276:immunology*
D000911:Antibodies, Monoclonal; D000956:Antigens, Viral; D000939:Epitopes; D006023:Glycoproteins; D006027:Glycosides; D009844:Oligosaccharides; D012794:Sialic Acids; D014764:Viral Proteins; D019158:N-Acetylneuraminic Acid