Premium
Nucleolin and the Packaging Signal, ψ, Promote the Budding of Human Immunodeficiency Virus Type‐1 (HIV‐1)
Author(s) -
Ueno Tomonori,
Tokunaga Kenzo,
Sawa Hirofumi,
Maeda Masae,
Chiba Joe,
Kojima Asato,
Hasegawa Hideki,
Shoya Yuko,
Sata Tetsutaro,
Kurata Takeshi,
Takahashi Hidehiro
Publication year - 2004
Publication title -
microbiology and immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.664
H-Index - 70
eISSN - 1348-0421
pISSN - 0385-5600
DOI - 10.1111/j.1348-0421.2004.tb03496.x
Subject(s) - nucleolin , group specific antigen , biology , budding , rna , virology , rna binding protein , zinc finger , virus , microbiology and biotechnology , genetics , gene , nucleolus , cytoplasm , transcription factor
Gag proteins of human immunodeficiency virus type 1 (HIV‐1) play a pivotal role in the budding of the virion, in which the zinc finger motifs of the gag proteins recognize the packaging signal of genomic RNA. Nucleolin, an RNA‐binding protein, is identified as a cellular protein that binds to murine leukemia virus (MuLV) gag proteins and regulates the viral budding, suggesting that HIV‐1 gag proteins, the packaging signal, ψ and nucleolin affect the budding of HIV‐1. Here we report that nucleolin enhances the release of HIV‐1 virions which contain ψ. Furthermore, nucleolin and gag proteins form a complex incorporated into virions, and nucleolin promotes the infectivity of HIV‐1. Our results suggest that an empty particle which contains neither nucleolin nor the genomic RNA is eliminated during the budding process, and this mechanism is beneficial for escape from the host immune response against HIV‐1.