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.
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Hongo
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Sugawara
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Homma
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Nakamura
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