Premium
Effect of various glycosidase treatments on the resistance of the HIV‐1 envelope to degradation
Author(s) -
Papandreou Marie-Jeanne,
Fenouillet Emmanuel
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)00273-1
Subject(s) - proteases , glycoprotein , glycan , chemistry , cleavage (geology) , endoglycosidase , sialic acid , biochemistry , viral envelope , glycosylation , neuraminidase , sialidase , enzyme , biology , paleontology , fracture (geology)
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.