Abstract: Here we show that HIV-1 capsid mutants N74D and P90A, which are impaired for interaction with cofactors cleavage and polyadenylation specificity factor subunit 6 (CPSF6) and cyclophilins (Nup358 and CypA), respectively, cannot replicate in primary human monocyte-derived macrophages because they trigger innate sensors leading to nuclear translocation of NF-kappaB and IRF3, the production of soluble type 1 IFN and induction of an antiviral state.
Introduction: Consistently, double mutation of P90A and RT D185E, but not IN D116N, suppressed IP10 induction.
Introduction: Intriguingly, both N74D and P90A PMID: 21593146
2011
Journal of virology
Abstract: Two capsid missense mutant viruses, N74D and P90A, were largely insensitive to NUP153 depletion, as was wild-type HIV-1 when cyclophilin A was depleted simultaneously or when infection was conducted in the presence of cyclosporine A.
Abstract: HIV-1 cyclophilin-binding mutants CA G89V and P90A favored integration in genomic regions with a higher density of transcription units and associated features than wild type virus.
Result: As expected, the CypA insensitive mutants G89V or P90A did not respond significantly to Cs treatment or CypA depletion by RNAi respectively (Figure 6A, B).
Result: Because G89V and P90A influence targeting in the same direction, we infer that disruption of normal CypA interactions, and possibly Nup358 interactions, result in increased frequency of integration in regions with high densities of transcription units.
Result: Hierarchical clustering of the CA mutants based on these data separated t
Target cell type-dependent modulation of human immunodeficiency virus type 1 capsid disassembly by cyclophilin A.
Abstract: In Jurkat T lymphocytes, disrupting CypA-CA interaction either by cyclosporine (Cs) treatment or by alteration (e.g., P90A) of the CA inhibits HIV-1 infection.
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: To understand these phenomena, we examined the effects of the P90A and A92E changes in the HIV-1 CA protein on the stability of
HIV mutation literature information.
PMID: 
2013
Nature
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