Tanchou V, Decimo D, Péchoux C, Lener D, Rogemond V, Berthoux L, Ottmann M, Darlix J L
LaboRetro, Unité de Virologie Humaine INSERM U412, Ecole Normale Supérieure de Lyon, France.
J Virol. 1998 May;72(5):4442-7. doi: 10.1128/JVI.72.5.4442-4447.1998.
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 CX2CX4CX4C. 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.
1型人类免疫缺陷病毒的核衣壳蛋白(NCp7)被发现覆盖在病毒颗粒内部的基因组RNA上。它是一种高度碱性的蛋白质,具有两个CX2CX4HX4C形式的锌指结构,对锌阳离子表现出很强的亲和力。为了研究NCp7 N端锌指的结构-功能关系,该结构域要么被删除,要么被改变为CX2CX4CX4C。我们检查了病毒的形成、结构以及前病毒DNA的合成。我们的数据表明,这两种NC突变导致形成具有异常核心形态的颗粒,并损害前病毒DNA合成的末端,从而产生无感染性的病毒。