Cyclophilin interactions with incoming human immunodeficiency virus type 1 capsids with opposing effects on infectivity in human cells

Cyclophilin A (CypA) is a peptidyl-prolyl isomerase that binds to the capsid protein (CA) of human immunodeficiency virus type 1 (HIV-1) and by doing so facilitates HIV-1 replication. Although CypA is incorporated into HIV-1 virions by virtue of CypA-Gag interactions that occur during virion assembl...

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Vydané v:Journal of virology Ročník 79; číslo 1; s. 176
Hlavní autori: Hatziioannou, Theodora, Perez-Caballero, David, Cowan, Simone, Bieniasz, Paul D
Médium: Journal Article
Jazyk:English
Vydavateľské údaje: United States 01.01.2005
Predmet:
Animals
Antiviral Restriction Factors
Capsid - metabolism
Capsid Proteins - genetics
Capsid Proteins - metabolism
Carrier Proteins - metabolism
Cell Line
Cyclophilin A - genetics
Cyclophilin A - metabolism
Cyclosporine - metabolism
HeLa Cells
HIV-1 - genetics
HIV-1 - metabolism
HIV-1 - pathogenicity
Humans
Jurkat Cells
Mutation
Peptidylprolyl Isomerase - genetics
Peptidylprolyl Isomerase - metabolism
Tripartite Motif Proteins
Ubiquitin-Protein Ligases
Virion - metabolism
Virus Replication
ISSN:0022-538X
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Popis
Shrnutí:Cyclophilin A (CypA) is a peptidyl-prolyl isomerase that binds to the capsid protein (CA) of human immunodeficiency virus type 1 (HIV-1) and by doing so facilitates HIV-1 replication. Although CypA is incorporated into HIV-1 virions by virtue of CypA-Gag interactions that occur during virion assembly, in this study we show that the CypA-CA interaction that occurs following the entry of the viral capsid into target cells is the major determinant of CypA's effects on HIV-1 replication. Specifically, by using normal and CypA-deficient Jurkat cells, we demonstrate that the presence of CypA in the target and not the virus-producing cell enhances HIV-1 infectivity. Moreover, disruption of the CypA-CA interaction with cyclosporine A (CsA) inhibits HIV-1 infectivity only if the target cell expresses CypA. The effect of CsA on HIV-1 infection of human cells varies according to which particular cell line is used as a target, and CA mutations that confer CsA resistance and dependence exert their effects only if target cells, and not if virus-producing cells, are treated with CsA. The differential effects of CsA on HIV-1 infection in different human cells appear not to be caused by polymorphisms in the recently described retrovirus restriction factor TRIM5alpha. We speculate that CypA and/or CypA-related proteins affect the fate of incoming HIV-1 capsid either directly or by modulating interactions with unidentified host cell factors.
Bibliografia:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
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ISSN:0022-538X
DOI:10.1128/JVI.79.1.176-183.2005