論文

査読有り 国際誌
2013年12月15日

GANP interacts with APOBEC3G and facilitates its encapsidation into the virions to reduce HIV-1 infectivity.

Journal of immunology (Baltimore, Md. : 1950)
  • Kazuhiko Maeda
  • ,
  • Sarah Ameen Almofty
  • ,
  • Shailendra Kumar Singh
  • ,
  • Mohammed Mansour Abbas Eid
  • ,
  • Mayuko Shimoda
  • ,
  • Terumasa Ikeda
  • ,
  • Atsushi Koito
  • ,
  • Phuong Pham
  • ,
  • Myron F Goodman
  • ,
  • Nobuo Sakaguchi

191
12
開始ページ
6030
終了ページ
6039
記述言語
英語
掲載種別
研究論文(学術雑誌)
DOI
10.4049/jimmunol.1302057

The ssDNA-dependent deoxycytidine deaminase apolipoprotein B mRNA-editing, enzyme-catalytic, polypeptide-like 3G (A3G) is a potent restrictive factor against HIV-1 virus lacking viral-encoded infectivity factor (Vif) in CD4(+) T cells. A3G antiretroviral activity requires its encapsulation into HIV-1 virions. In this study, we show that germinal center-associated nuclear protein (GANP) is induced in activated CD4(+) T cells and physically interacts with A3G. Overexpression of GANP augments the A3G encapsidation into the virion-like particles and ΔVif HIV-1 virions. GANP is encapsidated in HIV-1 virion and modulates A3G packaging into the cores together with cellular RNAs, including 7SL RNA, and with unspliced HIV-1 genomic RNA. GANP upregulation leads to a significant increase in A3G-catalyzed G→A hypermutation in the viral genome and suppression of HIV-1 infectivity in a single-round viral infection assay. Conversely, GANP knockdown caused a marked increase in HIV-1 infectivity in a multiple-round infection assay. The data suggest that GANP is a cellular factor that facilitates A3G encapsidation into HIV-1 virions to inhibit viral infectivity.

リンク情報
DOI
https://doi.org/10.4049/jimmunol.1302057
PubMed
https://www.ncbi.nlm.nih.gov/pubmed/24198285
PubMed Central
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4086635
ID情報
  • DOI : 10.4049/jimmunol.1302057
  • PubMed ID : 24198285
  • PubMed Central 記事ID : PMC4086635

エクスポート
BibTeX RIS