Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 103, Issue 14, Pages 5514-5519Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0509996103
Keywords
B30.2(SPRY) domain; tripartite motif; HIV-1; RING, B-box, and coiled-coil protein; innate immunity
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Funding
- NHLBI NIH HHS [HL 54785, P50 HL054785] Funding Source: Medline
- NIAID NIH HHS [R01 AI063987, AI 28691, P30 AI028691, R01 AI045405, AI 45405, R37 AI045405, AI 063987] Funding Source: Medline
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The host restriction factor TRIM5 alpha mediates species-specific, early blocks to retrovirus infection; susceptibility to these blocks is determined by viral capsid sequences. Here we demonstrate that TRIM5 alpha variants from Old World monkeys specifically associate with the HIV type 1 (HIV-1) capsid and that this interaction depends on the TRIM5 alpha B30.2 domain. Human and New World monkey TRIM5 alpha proteins associated less efficiently with the HIV-1 capsid, accounting for the lack of restriction in cells of these species. After infection, the expression of a restricting TRIM5 alpha in the target cells correlated with a decrease in the amount of particulate capsid in the cytosol. In some cases, this loss of particulate capsid was accompanied by a detectable increase in soluble capsid protein. Inhibiting the proteasome did not abrogate restriction. Thus, TRIM5 alpha restricts retroviral infection by specifically recognizing the capsid and promoting its rapid, premature disassembly.
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