Result: Of interest, we observed that the capsid mutants containing the N74D change, either alone or in combination with the V86M and/or H87Q capsid changes, exhibited increased infectivity (4.9- to 13.9-fold increase) in the marmoset B-LCLs compared to WT viruses.
Result: The V86M and H87Q capsid mutants also exhibited increased infectivity in the marmoset cells compared to WT viruses, although the escape was not as efficient as that of the N74D mutant.
Discussion: In our study, we found that the N74D and, to a lesser degree, the V86M and H87Q
The V86M mutation in HIV-1 capsid confers resistance to TRIM5alpha by abrogation of cyclophilin A-dependent restriction and enhancement of viral nuclear import.
Abstract: CONCLUSIONS: Our study shows that V86M de-couples the two functions associated with CA-CypA binding.
Abstract: Finally, qPCR experiments show that V86M increases HIV-1 transport to the nucleus of cells expressing restrictive TRIM5alpha.
Abstract: However, V86M HIV-1 does not seem to be resistant to R332G-R335G TRIM5alphahu in a spreading infection context.
Abstract: However, V86M does not seem to relieve restriction of a spreading HIV-1 infection by TRIM5alphahu mutants, underscoring context-specific restriction mechanisms.
Abstract: NMR experiments reveal that V86M alters CypA interactions with, and isomerisation of CA.
HIV mutation literature information.
PMID: 
2016
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