Interactions between HIV1 Nef and vacuolar ATPase facilitate the internalization of CD4

被引：219

作者：

Lu, XB

Yu, HF

Liu, SH

Brodsky, FM

Peterlin, BM ^{[1
]}

机构：

[1] Univ Calif San Francisco, Howard Hughes Med Inst, Dept Med, San Francisco, CA 94143 USA

[2] Univ Calif San Francisco, Howard Hughes Med Inst, Dept Microbiol, San Francisco, CA 94143 USA

[3] Univ Calif San Francisco, Howard Hughes Med Inst, Dept Immunol, San Francisco, CA 94143 USA

[4] Univ Calif San Francisco, GW Hooper Fdn, Dept Microbiol & Immunol, San Francisco, CA 94143 USA

[5] Univ Calif San Francisco, GW Hooper Fdn, Dept Biopharmaceut Sci, San Francisco, CA 94143 USA

[6] Univ Calif San Francisco, GW Hooper Fdn, Dept Biopharmaceut Sci, San Francisco, CA 94143 USA

[7] Univ Calif San Francisco, GW Hooper Fdn, Dept Pharmaceut Chem, San Francisco, CA 94143 USA

来源：

IMMUNITY | 1998年 / 8卷 / 05期

关键词：

D O I：

10.1016/S1074-7613(00)80569-5

中图分类号：

R392 [医学免疫学]; Q939.91 [免疫学];

学科分类号：

100102 ;

摘要：

CD4 is the primary receptor for the human immunodeficiency virus (HIV). Nef is an accessory protein of HIV that decreases the expression of CD4 on the surface of infected cells. In this study, we identified the Nef binding protein 1 (NBP1), which interacts specifically with Nef in vitro and in vivo. Since it shares sequence similarity with the catalytic subunit of the vacuolar ATPase (V-ATPase) and complements the loss of this VMA13 gene in yeast, NBP1 is the human homolog of Vma13p. Direct interactions between Nef and NBP1 were correlated with the ability of Nef to internalize CD4. The expression of the antisense NBP1 abrogated these effects. We conclude that NBP1 helps to connect Nef with the endocytic pathway.

引用

页码：647 / 656

页数：10

共 65 条

[1] NEF INDUCES CD4 ENDOCYTOSIS - REQUIREMENT FOR A CRITICAL DILEUCINE MOTIF IN THE MEMBRANE-PROXIMAL CD4 CYTOPLASMIC DOMAIN [J].