Linked Life Data

21568899

Source:http://linkedlifedata.com/resource/pubmed/id/21568899

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
17
pubmed:dateCreated
2011-6-8
pubmed:abstractText
Tripartite motif protein 5-alpha (TRIM5?) is a cytoplasmic protein that efficiently recognizes the incoming capsid (CA) protein of retroviruses and potently inhibits virus infection in a species-specific manner. Through directly recognizing and interacting with HIV CA, TRIM5? is capable of disrupting the ordered process of viral uncoating, eventually interfering with HIV-1 reverse transcription and virus replication. TRIM5? protein contains four domains: RING domain, B-box 2 domain, coiled-coil domain, and B30.2 domain (SPRY) domain. All of the domains are necessary for efficient retrovirus restriction and the B30.2 domain has been shown to be the determinant of the specificity of restriction. Species-specific innate resistance against viral infections offers novel avenues for antiviral therapeutics. Various mutants of TRIM5? have been described which differently affect the HIV-1 reverse transcription process. This makes the establishment of new and improved models for HIV replication and AIDS pathogenesis by monitoring endogenous TRIM5? an attractive approach. TRIM5?-mediated restriction is modulated by the host protein Cyclophilin A (Cyp A) which could effectively interact with the CA of HIV-1. Here we will review the structure and roles of TRIM5? protein, the interaction between Cyp A and TRIM5?, as well as gene therapy strategies associated with TRIM5? to inhibit HIV-1 infection.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1875-533X
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
18
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2649-54
pubmed:meshHeading
pubmed:year
2011
pubmed:articleTitle
Retroviral restriction factors TRIM5?: therapeutic strategy to inhibit HIV-1 replication.
pubmed:affiliation
Department of Medicinal Chemistry, School of Pharmaceutical Sciences, Shandong University, 250012, Jinan, Shandong, PR China.
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't