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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
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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