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

被引：32

作者：

Nakayama, EE

Shioda, T

Tatsumi, M

Xin, XM

Yu, DS

Ohgimoto, S

Kato, A

Sakai, Y

Ohnishi, Y

Nagai, Y

机构：

[1] Univ Tokyo, Inst Med Sci, Dept Viral Infect, Minato Ku, Tokyo 108, Japan

[2] Univ Tokyo, Inst Med Sci, Dept Infect Dis, Tokyo, Japan

[3] Natl Inst Infect Dis, Dept Vet Sci, Tokyo, Japan

来源：

FEBS LETTERS | 1998年 / 426卷 / 03期

基金：

日本科学技术振兴机构;

关键词：

human immunodeficiency virus type 1; third variable loop; N-glycan; site directed mutagenesis; CXCR-4;

D O I：

10.1016/S0014-5793(98)00375-5

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

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 contest of the peptide backbone. (C) 1998 Federation of European Biochemical Societies.

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收藏

页码：367 / 372

页数：6

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