In vitro assembly of the feline immunodeficiency virus Gag polyprotein

被引:22
|
作者
Affranchino, Jose L. [1 ]
Gonzalez, Silvia A. [1 ]
机构
[1] Univ Belgrano UB, Fac Ciencias Exactas & Nat, CONICET, Virol Lab, Buenos Aires, DF, Argentina
关键词
Feline immunodeficiency virus; Gag polyprotein; In vitro assembly; Lentiviruses; ROUS-SARCOMA-VIRUS; TYPE-1; GAG; MATRIX PROTEIN; DOMAINS; IDENTIFICATION; PARTICLES; BINDING; HIV; ENCAPSIDATION; ORGANIZATION;
D O I
10.1016/j.virusres.2010.03.012
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
The retroviral Gag protein is the only viral product that is necessary for the assembly of virions in mammalian cells. We have established an in vitro assembly system to study the assembly properties of purified feline immunodeficiency virus (FIV) Gag protein expressed in bacteria. Under fully defined conditions, the FIV Gag protein assembles into spherical particles of 33 nm in diameter which are morphologically similar to authentic immature particles, albeit smaller than virions. The in vitro assembly of Fly Gag into particles was found to be resistant to the addition of Triton X-100 and required the presence of RNA. Notably, we found that an amino acid substitution in the nucleocapsid domain of Gag that impairs RNA binding and blocks virion production in vivo, also abrogates Gag assembly in vitro. The development of an in vitro assembly system for FIV Gag protein will facilitate the study of the mechanisms by which this protein assembles into immature particles. (C) 2010 Elsevier B.V. All rights reserved.
引用
收藏
页码:153 / 157
页数:5
相关论文
empty
未找到相关数据