The specificity of TRIM5 alpha-mediated restriction is influenced by its coiled-coil domain.

Details

Serval ID
serval:BIB_04923548617A
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
The specificity of TRIM5 alpha-mediated restriction is influenced by its coiled-coil domain.
Journal
Journal of Virology
Author(s)
Maillard Pierre V., Ecco Gabriela, Ortiz Millan, Trono Didier
ISSN
1098-5514[electronic], 0022-538X[linking]
Publication state
Published
Issued date
2010
Volume
84
Number
11
Pages
5790-5801
Language
english
Abstract
Retroviruses are both powerful evolutionary forces and dangerous threats to genome integrity. As such, they have imposed strong selective pressure on their hosts, notably triggering the emergence of restriction factors, such as TRIM5 alpha, that act as potent barriers to their cross-species transmission. TRIM5 alpha orthologues from different primates have distinct retroviral restriction patterns, largely dictated by the sequence of their C-terminal PRYSPRY domain, which binds the capsid protein of incoming virions. Here, by combining genetic and functional analyses of human and squirrel monkey TRIM5 alpha, we demonstrate that the coiled-coil domain of this protein, thus far essentially known for mediating oligomerization, also conditions the spectrum of antiretroviral activity. Furthermore, we identify three coiled-coil residues responsible for this effect, one of which has been under positive selection during primate evolution, notably in New World monkeys. These results indicate that the PRYSPRY and coiled-coil domains cooperate to determine the specificity of TRIM5 alpha-mediated capture of retroviral capsids, shedding new light on this complex event.
Keywords
Murine Leukemia-Virus, Trim Family Proteins, Amino-Acid Sites, Retroviral Restriction, Monkey TRIM5-Alpha, Old-World, Positive Selection, Rhesus TRIM5-Alpha, Cyclophilin-A, HIV-1
Pubmed
Web of science
Open Access
Yes
Create date
28/05/2010 9:01
Last modification date
20/08/2019 12:26
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