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Effect of sialic acid removal on the antibody response to the third variable domain of human immunodeficiency virus type‐1 envelope glycoprotein
Author(s) -
Benjouad Abdelaziz,
Mabrouk Kamel,
Gluckman Jean Claude,
Fenouillet Emmanuel
Publication year - 1994
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 - 10.1016/0014-5793(94)80465-6
Subject(s) - immunogenicity , sialic acid , glycoprotein , v3 loop , antibody , chemistry , avidity , viral envelope , virology , biochemistry , epitope , biology , immunology
The gp160 envelope glycoprotein of human immunodeficiency virus type‐1 (HIV‐1) is an essential component of current vaccine trials. The giycans of gp160, part of which are highly sialylated, have been shown to influence gp160 immunogenicity. Here, using a panel of synthetic V3 peptides, we characterized the anti‐V3 antibodies generated in rabbits immunized by desialylated recombinant gp160 LAI . Amino acid residues flanking the GPGR tip of V3 were necessary for the recognition by anti‐V3 antibodies raised against either the native or desialylated gp160. Both types of antibodies reacted to V3 peptides of MN and SF2 strains and with a North American/European V3 consensus peptide, while anti‐desialylated gp 160 LAI antibodies reacted in addition to the V3 of CDC4, WMJ2 and NY5 strains. Yet, the V3 peptides did not significantly differ in their secondary structure, as determined by circular dichroism. The titer and avidity for V3 MN of anti‐desialylated gp160 LAI , antibodies were significantly lower than those of anti‐native gp160 LAI , which likely accounts for the inability of anti‐desialylated gp160 LAI sera to neutralize HIV‐1 MN ‐mduced syncytia. These results indicate that V3 immunogenicity may be influenced by subtle directed changes in the gp160 glycosylation pattern.