The ADAR1 editing enzyme is encapsidated into HIV-1 virions

被引：12

作者：

Orecchini, Elisa ^{[1
]}

Federico, Maurizio ^{[2
]}

Doria, Margherita ^{[3
]}

Arenaccio, Claudia ^{[2
]}

Giuliani, Erica ^{[3
]}

Ciafre, Silvia Anna ^{[1
]}

Michienzi, Alessandro ^{[1
]}

机构：

[1] Univ Roma Tor Vergata, Dept Biomed & Prevent, I-00133 Rome, Italy

[2] Ist Super Sanita, Natl AIDS Ctr, I-00161 Rome, Italy

[3] IRCCS, Lab Immunoinfectivol, Bambino Gesu Childrens Hosp, I-00165 Rome, Italy

来源：

VIROLOGY | 2015年 / 485卷

关键词：

ADAR1; HIV-1; p55; Gag; Encapsidation; IMMUNODEFICIENCY-VIRUS TYPE-1; GENOMIC RNA; GAG; PARTICLES; PKR; EXPRESSION; INTERACTS; RELEASE; CELLS;

D O I：

10.1016/j.virol.2015.07.027

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

Adenosine deaminase acting on RNA1 (ADAR1) was previously reported to affect HIV-1 replication. We report data showing that ADAR1 interacts with the HIV-1 p55 Gag protein, the major structural protein of the immature virus capsid. Furthermore, we found that the endogenous ADAR1 is incorporated into virions purified from the supernatant of primary HIV-1-infected CD4(+) T lymphocytes. Additional experiments demonstrated that the expression of the p55 Gag protein is sufficient for ADAR1 incorporation into virus-like particles (VLPs). Overall, our data originally support the evidence that ADAR1 can be part of the cell protein array uploaded in HIV-1 particles. (C) 2015 Elsevier Inc. All rights reserved.

引用

页码：475 / 480

页数：6

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