Abstract
In owl monkeys, the typical retroviral restriction factor of primates, TRIM5α, is replaced by TRIMCyp. TRIMCyp consists of the TRIM5 RING, B-box 2 and coiled-coil domains, as well as the intervening linker regions, fused with cyclophilin A. TRIMCyp restricts infection of retroviruses, such as human immunodeficiency virus (HIV-1) and feline immunodeficiency virus (FIV), with capsids that can bind cyclophilin A. The TRIM5 coiled coil promotes the trimerization of TRIMCyp. Here we show that cyclophilin A that is oligomeric as a result of fusion with a heterologous multimer exhibits substantial antiretroviral activity. The addition of the TRIM5 RING, B-box 2 and Linker 2 to oligomeric cyclophilin A generated a protein with antiretroviral activity approaching that of wild-type TRIMCyp. Multimerization increased the binding of cyclophilin A to the HIV-1 capsid, promoting accelerated uncoating of the capsid and restriction of infection.
Original language | English (US) |
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Pages (from-to) | 19-29 |
Number of pages | 11 |
Journal | Virology |
Volume | 367 |
Issue number | 1 |
DOIs | |
State | Published - Oct 10 2007 |
Externally published | Yes |
Keywords
- Coiled-coil domain
- Cyclophilin A
- FIV
- HIV-1
- Multimerization
- Restriction
- Retroviral capsid
- TRIM5
- TRIMCyp
ASJC Scopus subject areas
- Virology