PMID- 23637418
OWN - NLM
STAT- MEDLINE
DCOM- 20130812
LR  - 20211021
IS  - 1098-5514 (Electronic)
IS  - 0022-538X (Print)
IS  - 0022-538X (Linking)
VI  - 87
IP  - 13
DP  - 2013 Jul
TI  - Virus-specific effects of TRIM5alpha(rh) RING domain functions on restriction of 
      retroviruses.
PG  - 7234-45
LID - 10.1128/JVI.00620-13 [doi]
AB  - The tripartite motif protein TRIM5alpha restricts particular retrovirus infections by 
      binding to the incoming capsid and inhibiting the early stage of virus infection. 
      The TRIM5alpha RING domain exhibits E3 ubiquitin ligase activity and assists the 
      higher-order association of TRIM5alpha dimers, which promotes capsid binding. We 
      characterized a panel of RING domain mutants of the rhesus monkey TRIM5alpha 
      (TRIM5alpha(rh)) protein. The RING domain function that significantly contributed to 
      retroviral restriction depended upon the restricted virus. The E3 ubiquitin 
      ligase activity of the RING domain contributes to the potency of HIV-1 
      restriction. Nonetheless, TRIM5alpha(rh) mutants without detectable E3 ubiquitin 
      ligase activity still blocked reverse transcription and inhibited HIV-1 infection 
      at a moderate level. When TRIM5alpha(rh) capsid binding was weakened by substitution 
      with a less efficient B30.2/SPRY domain, the promotion of higher-order 
      association by the RING domain was more important to HIV-1 restriction than its 
      E3 ubiquitin ligase activity. For the restriction of N-tropic murine leukemia 
      virus (N-MLV) and equine infectious anemia virus (EIAV) infection, promotion of 
      higher-order association represented the major contribution of the RING domain. 
      Thus, both identity of the target virus and the B30.2/SPRY domain-mediated 
      affinity for the viral capsid determine the relative contribution of the two 
      known RING domain functions to TRIM5alpha restriction of retrovirus infection.
FAU - Li, Xing
AU  - Li X
AD  - Department of Cancer Immunology and AIDS, Dana-Farber Cancer Institute, Harvard 
      Medical School, Boston, Massachusetts, USA.
FAU - Kim, Jonghwa
AU  - Kim J
FAU - Song, Byeongwoon
AU  - Song B
FAU - Finzi, Andres
AU  - Finzi A
FAU - Pacheco, Beatriz
AU  - Pacheco B
FAU - Sodroski, Joseph
AU  - Sodroski J
LA  - eng
GR  - R01 AI063987/AI/NIAID NIH HHS/United States
GR  - AI063987/AI/NIAID NIH HHS/United States
GR  - AI06354/AI/NIAID NIH HHS/United States
PT  - Comparative Study
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
PT  - Research Support, Non-U.S. Gov't
DEP - 20130501
PL  - United States
TA  - J Virol
JT  - Journal of virology
JID - 0113724
RN  - 0 (Proteins)
RN  - 147336-22-9 (Green Fluorescent Proteins)
RN  - EC 2.3.2.27 (TRIM5(alpha) protein, rhesus monkey)
RN  - EC 2.3.2.27 (Ubiquitin-Protein Ligases)
SB  - IM
MH  - Animals
MH  - Blotting, Western
MH  - Capsid/*metabolism
MH  - Cell Line
MH  - Dogs
MH  - Green Fluorescent Proteins/metabolism
MH  - *HIV-1
MH  - Humans
MH  - *Infectious Anemia Virus, Equine
MH  - *Leukemia Virus, Murine
MH  - Macaca mulatta
MH  - Microscopy, Fluorescence
MH  - Proteins/genetics/*metabolism
MH  - Retroviridae Infections/genetics/*metabolism
MH  - Species Specificity
MH  - Ubiquitin-Protein Ligases/metabolism
PMC - PMC3700309
EDAT- 2013/05/03 06:00
MHDA- 2013/08/13 06:00
PMCR- 2014/01/01
CRDT- 2013/05/03 06:00
PHST- 2013/05/03 06:00 [entrez]
PHST- 2013/05/03 06:00 [pubmed]
PHST- 2013/08/13 06:00 [medline]
PHST- 2014/01/01 00:00 [pmc-release]
AID - JVI.00620-13 [pii]
AID - 00620-13 [pii]
AID - 10.1128/JVI.00620-13 [doi]
PST - ppublish
SO  - J Virol. 2013 Jul;87(13):7234-45. doi: 10.1128/JVI.00620-13. Epub 2013 May 1.