Role of the N-terminal zinc finger of human immunodeficiency virus type 1 nucleocapsid protein in virus structure and replication

被引:119
作者
Tanchou, V [1 ]
Decimo, D [1 ]
Péchoux, C [1 ]
Lener, D [1 ]
Rogemond, V [1 ]
Berthoux, L [1 ]
Ottmann, M [1 ]
Darlix, JL [1 ]
机构
[1] Ecole Normale Super Lyon, INSERM, U412, Unite Virol Humaine,LaboRetro, F-69364 Lyon 07, France
关键词
D O I
10.1128/JVI.72.5.4442-4447.1998
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
Nucleocapsid protein (NCp7) of human immunodeficiency virus type 1 is found covering the genomic RNA in the interior of the viral particle. It is a highly basic protein with two zinc fingers of the form CX2CX4HX4C which exhibit strong affinity for a zinc cation. To study the structure-function relationship of the N-terminal zinc finger of NCp7, this domain was either deleted or changed to CX2CX4 (C) under bar X4C. We examined virus formation and structure as well as proviral DNA synthesis, Our data show that these two NC mutations result in the formation of particles with an abnormal core morphology and impair the end of proviral DNA synthesis, leading to noninfectious viruses.
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页码:4442 / 4447
页数:6
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