Differential glycosylation of envelope gp120 affects reactivity with HIV-1 specific antibodies

Cellular entry of human immunodeficiency virus type 1 (HIV-1) depends on envelope glycoprotein (gp120/gp41) interactions with host-cell receptors. Approximately one-half of molecular mass of gp120 consists of N-glycans which may act as antigenic determinants as well as a shield against immune recognition. We have shown that glycosylation of subtype B HIV-1 gp120 varies according to the producing cell type and the differential glycosylation affects reactivities with serum antibodies of persons infected with HIV-1 subtype B. Here we studied reactivities of above proteins with panel of monoclonal gp120-specific broadly neutralizing antibodies and sera from persons infected with HIV-1 subtype A/C.