Effect of various glycosidase treatments on the resistance of the HIV-1 envelope to degradation.
Using a CD4-binding assay to assess the conformation of the human immunodeficiency virus envelope glycoprotein (CHO+ Env), we studied the effect of treatment with various glycosidases on the stability of Env in denaturing environments and in biological media: cleavage from Env of either high-mannose-type glycans (HMT- Env) by endoglycosidase H or sialic acid residues (Sial- Env) by sialidase did not alter Env stability whereas its complete deglycosylation (CHO- Env) by N-glycanase had a large effect. The influence of glycan removal on Env sensitivity to proteases was also studied. Thrombin cleavage within V3 was affected by N-glycanase treatment; both HMT- Env and CHO- Env displayed an increased sensitivity to other endoproteases. Thus, partial deglycosylation increases Env sensitivity to proteases but only its total deglycosylation alters its stability.
Papandreou
M J
MJ
CNRS, UMR 6560, IFR Jean Roche, Faculté de Médecine Nord, Marseille, France.
Fenouillet
E
E
D000818:Animals; D001665:Binding Sites; D001769:Blood; D015704:CD4 Antigens / Q000378:metabolism; D016466:CHO Cells; D006224:Cricetinae; D015686:Gene Products, env / Q000378:metabolism*; D006026:Glycoside Hydrolases / Q000378:metabolism*; D006031:Glycosylation; D006868:Hydrolysis; D013917:Thrombin / Q000378:metabolism
D015704:CD4 Antigens; D015686:Gene Products, env; D006026:Glycoside Hydrolases; D013917:Thrombin