Effect of sialic acid removal on the antibody response to the third variable domain of human immunodeficiency virus type‐1 envelope glycoprotein

FEBS Letters

Gluckman, Jean Claude¹  Mabrouk, Kamel²  Benjouad, Abdelaziz¹  Fenouillet, Emmanuel¹ 

[1] Laboratoire de Biologie et Génétique des Pathologies Immunitaires, CNRS URA 1463, Faculté de Médecine Pitié-Salpêtrière, 75651 Paris Cedex 13, France;Laboratoire de Biochimie, CNRS URA 1455, Faculté de Médecine Nord, 13916 Marseille Cedex 15, France

关键词: HIV;    V3;    Glycosylation;    Antigenicity;    Neutralizing antibody;   

DOI  :  10.1016/0014-5793(94)80465-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown