Relationships between the anti-HIV V3-derived peptide SPC3 and lymphocyte membrane properties involved in virus entry:: SPC3 interferes with CXCR4

被引：16

作者：

Barbouche, R ^{[1
]}

Papandréou, MJ ^{[1
]}

Miquelis, R ^{[1
]}

Guieu, R ^{[1
]}

Fenouillet, E ^{[1
]}

机构：

[1] CNRS, Fac Med N, F-13015 Marseille, France

来源：

FEMS MICROBIOLOGY LETTERS | 2000年 / 183卷 / 02期

关键词：

anti-human immunodeficiency virus peptide coreceptor; V-3; loop; CXCR4; internalization; human immunodeficiency virus entry;

D O I：

10.1016/S0378-1097(99)00653-9

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

SPC3 is a multiple antigen peptide derived from the V-3 loop of human immunodeficiency virus (HIV) envelope (Env). II exerts a potent anti-HIV activity whereas it alters neither Env expression nor binding to CD4. Here, SPC3 binding characteristics, its subsequent intracellular fate and the fact that it inhibited SDF(1)alpha binding to the lymphocyte surface provided strong arguments to conclude that it exerts its anti-HIV activity through interference with the CXCR4 coreceptor. In contrast, it interferes with none of the other major surface proteins and mechanisms involving V-3 and implicated in infection, as shown here. This work identifies the target mechanism of SPC3. (C) 2000 Federation of European Microbiological Societies. Published by Elsevier Science B.V. All rights reserved.

引用

页码：235 / 240

页数：6

共 19 条

[1] IDENTIFICATION OF THE U-937 MEMBRANE-ASSOCIATED PROTEINASE INTERACTING WITH THE V3 LOOP OF HIV-1 GP120 AS CATHEPSIN-G [J].