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pubmed-article:9636359pubmed:abstractTextThe molecular chaperone cyclophilin A (Cyp A) modulates human immunodeficiency virus type 1 (HIV-1) infectivity through its interactions with Gag structural proteins. The molecular mechanism for CypA in HIV-1 replication is not known. We studied chaperone effects on Gag precursor processing using cyclosporin A (CsA) to bind CypA and prevent its interaction with p55Gag. CsA treatment inhibited p55Gag processing in extracellular virus-like particles produced from COS cells. We confirmed the effect of CsA on Gag processing by examining virions produced from CEMx174 cells infected with HIV-1LAI. Particles accumulated in the presence of CsA displayed mostly immature virion morphology and lacked condensed capsids. CsA has a direct effect on HIV-1 Gag processing that implicates CypA as having an important role in the maturation of HIV-1 particles.lld:pubmed
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pubmed-article:9636359pubmed:dateRevised2007-11-14lld:pubmed
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pubmed-article:9636359pubmed:articleTitleCyclophilin a modulates processing of human immunodeficiency virus type 1 p55Gag: mechanism for antiviral effects of cyclosporin A.lld:pubmed
pubmed-article:9636359pubmed:affiliationDepartment of Pathology and Laboratory Medicine, University of Wisconsin, Madison 53706, USA.lld:pubmed
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