Abstract: Selective deglycosylation of HIV-1 envelope proteins enhances their ability to elicit a protective immune response in people. Glycosylation can reduce or prevent immunological recognition of envelope protein domains. Selective deglycosylation exposes these domains and improves the opportunity for a protective immune response. Deglycosylation which produces substantial conformational changes (as determined by loss of infectivity) should be avoided. Recombinant HIV-1 envelope glycoproteins are generated which have primary amino acid sequence mutation(s) in consensus sequence(s) for N-linked glycosylation (sugar attachment), so as to prevent glycosylation at that site(s). The position of such genetic deglycosylation is important and should be between the C terminus of gp120 and the Cys at the N-terminal side of the cysteine loop containing the hyper-variable region 3 (V3) (this Cys is generally positioned about at residue 296, counting from the N-terminus of gp120).