Identification of the glycoprotein 41TM cytoplasmic tail domains of human immunodeficiency virus type 1 that interact with Pr55Gag particles

被引：29

作者：

Hourioux, C

Brand, D

Sizaret, PY

Lemiale, F

Lebigot, S

Barin, F

Roingeard, P

机构：

[1] Univ Tours, Fac Med, Biol Cellulaire Lab, EA 2639, F-37032 Tours, France

[2] Univ Tours, Fac Med, Virol Lab, EA 2639, Tours, France

来源：

AIDS RESEARCH AND HUMAN RETROVIRUSES | 2000年 / 16卷 / 12期

关键词：

D O I：

10.1089/088922200414983

中图分类号：

R392 [医学免疫学]; Q939.91 [免疫学];

学科分类号：

100102 ;

摘要：

We investigated the protein/protein interactions that occur during human immunodeficiency virus (HIV-1) budding. We evaluated the binding to Pr55(Gag) particles of peptides mapping to the cytoplasmic tail of gp41(TM) and of host-cell proteins, in a cell-free, in vitro assay. Host-cell proteins and irrelevant viral envelope peptides did not bind. Peptides corresponding to a large central domain of the gp41(TM) cytoplasmic tail (93 residues) bound to Pr55(Gag) particles. This demonstrates that a Gag/Env interaction is responsible for the specific incorporation of the Env glycoprotein into nascent HIV-1 virions, and defines more accurately the gp41(TM) domain involved in this interaction.

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页码：1141 / 1147

页数：7

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