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Importance of the N ‐glycan in the V3 loop of HIV‐1 envelope protein for CXCR‐4‐ but not CCR‐5‐dependent fusion
Author(s) -
Nakayama Emi E,
Shioda Tatsuo,
Tatsumi Masashi,
Xin Xiaomi,
Yu Deshan,
Ohgimoto Shinji,
Kato Atsushi,
Sakai Yuko,
Ohnishi Yukano,
Nagai Yoshiyuki
Publication year - 1998
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/s0014-5793(98)00375-5
Subject(s) - glycan , context (archaeology) , v3 loop , viral envelope , human immunodeficiency virus (hiv) , glycoprotein , biology , chemistry , microbiology and biotechnology , biochemistry , virology , peptide sequence , gene , paleontology
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.