Importance of the N‐glycan in the V3 loop of HIV‐1 envelope protein for CXCR‐4‐ but not CCR‐5‐dependent fusion

FEBS Letters

Xin, Xiaomi²  Shioda, Tatsuo²  Tatsumi, Masashi¹  Nakayama, Emi E²  Nagai, Yoshiyuki²  Yu, Deshan²  Kato, Atsushi²  Ohgimoto, Shinji²  Ohnishi, Yukano²  Sakai, Yuko² 

[1] Department of Veterinary Science, National Institute of Infectious Diseases, Tokyo, Japan;Department of Viral Infection, Institute of Medical Science, University of Tokyo, 4-6-1 Shiroganedai, Minato-ku, Tokyo 108, Japan

关键词: Human immunodeficiency virus type 1;    Third variable loop;    N-Glycan;    Site directed mutagenesis;    CXCR-4;   

DOI  :  10.1016/S0014-5793(98)00375-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The V3 region of HIV-1 envelope protein possesses a single N-linked sugar chain, which is conserved in most HIV-1 strains. We studied its role in the life cycle of HIV-1 strains with different co-receptor usage. Removal of the glycan appeared to cause a marked reduction of CXCR-4- but not CCR-5-dependent virus entry. A basic amino acid substitution at the 11th position of V3 markedly compensated for the removal of the N-glycan. These results indicate that the N-glycan plays an important role for CXCR-4-dependent virus entry and that this role is exerted in a particular context of the peptide backbone.

【 授权许可】

Unknown