Discussion: Collectively, the alternative approach suggests that the known capsid-interacting proteins are unlikely to determine CsA-dependence of the A92E mutant.
Discussion: The CA mutants A92E and G94D were originally isolated as CypA-independe
Discussion: We expected a reversal of A92E phenotype when the putative restriction factor is depleted.
Discussion: We grouped cell lines based on their permissivity to HIV-1-A92E infection and then compared the mean levels of gene expression in permissive versus non-permissive cell types to generate a ranked list of candidate genes.
Discussion: We identified another human T cell line, CEM, in which the A92E mutant requires CsA for infection.
Rhesus TRIM5alpha disrupts the HIV-1 capsid at the inter-hexamer interfaces.
Result: Several CA mutants, including A92E, which was used in our previous structural study, and the E45A mutant, which produces hyperstable capsids, were analyzed.
Result: The effect of TRIM5alpharh CC-SPRY binding to A92E CA tubular assemblies was similar to that observed with wild-type CA.
Target cell type-dependent modulation of human immunodeficiency virus type 1 capsid disassembly by cyclophilin A.
Abstract: In HeLa cells, however, treatment with Cs or Cs analogues minimally inhibits the early phase of HIV-1 infection but selects for a Cs-dependent virus with a change (A92E) in CA.
Abstract: Reducing the binding of CypA to the A92E mutant capsid, either by Cs treatment or by an additional P90A change in the CA protein, increased the amount of particulate capsids and viral infectivity in HeLa cells.
Abstract: The A92E change impaired CA-CA interactions in vitro and decreased the amount of particulate capsids in the cytosol
Cyclophilin A-dependent restriction of human immunodeficiency virus type 1 capsid mutants for infection of nondividing cells.
Abstract: The HIV-1 CA mutants A92E, T54A, and R132K were impaired for infection of aphidicolin-arrested HeLa cells, but not HOS cells.
A mutation in alpha helix 3 of CA renders human immunodeficiency virus type 1 cyclosporin A resistant and dependent: rescue by a second-site substitution in a distal region of CA.
Abstract: A105T rescued the impaired single-cycle infectivity and replication defects of both T54A and A92E mutants.
Abstract: Interestingly, CsA stimulates the replication of HIV-1 mutants containing either the A92E or G94D substitution in some human cell lines.
Abstract: Previous studies have identified two mutations, A92E and G94D, in the CypA-binding loop of CA that confer the ability of HIV-1 to replicate in the presence of CsA.
Analysis of human cell heterokaryons demonstrates that target cell restriction of cyclosporine-resistant human immunodeficiency virus type 1 mutants is genetically dominant.
Abstract: Analysis of heterokaryons between CsA-dependent HeLa-P4 cells and CsA-independent 293T cells indicated that the CsA-dependent infection by A92E and G94D mutants is due to a dominant cellular restriction.
Abstract: Here, we show that infection by the A92E and G94D mutants is restricted at an early post-entry stage of the HIV-1 life cycle.
Abstract: Little is known about this cell-dependent phenotype of the A92E and G94D mutants, except that it is not dependent on expression of the host factor TRIM5alpha.
Abstract: Two CA mutants, A92E and G94D, previously were identified by selection for growth of wild-type HIV-1 in cultures of CD4(+) HeLa cell cultures c
HIV mutation literature information.
PMID: 
2014
PloS one
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