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The ability of multimerized cyclophilin A to restrict retrovirus infection
- Source :
- Virology. 367(1)
- Publication Year :
- 2007
-
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.
- Subjects :
- Feline immunodeficiency virus
Anti-HIV Agents
viruses
Recombinant Fusion Proteins
Molecular Sequence Data
Heterologous
Biology
Coiled-coil domain
Article
Cell Line
03 medical and health sciences
Cyclophilin A
Retrovirus
Virology
Restriction
Animals
Humans
Amino Acid Sequence
Peptide sequence
TRIM5
Cyclophilin
Retroviral capsid
030304 developmental biology
Coiled coil
0303 health sciences
030302 biochemistry & molecular biology
Proteins
biology.organism_classification
FIV
Multimerization
3. Good health
Capsid
HIV-1
Aotidae
Capsid Proteins
TRIMCyp
Dimerization
Transcription Factors
Subjects
Details
- ISSN :
- 00426822
- Volume :
- 367
- Issue :
- 1
- Database :
- OpenAIRE
- Journal :
- Virology
- Accession number :
- edsair.doi.dedup.....fa4aae26fe67fb692fb76556c5b645f0