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.