HIV-1 capsid shape, orientation, and entropic elasticity regulate translocation into the nuclear pore complex.

ABSTRACT: Nuclear import and uncoating of the viral capsid are critical steps in the HIV-1 life cycle that serve to transport and release genomic material into the nucleus. Viral core import involves translocating the HIV-1 capsid at the nuclear pore complex (NPC). Notably, the central channel of the NPC appears to often accommodate and allow passage of intact HIV-1 capsid, though mechanistic details of the process remain to be fully understood. Here, we investigate the molecular interactions that operate in concert between the HIV-1 capsid and the NPC that regulate capsid translocation through the central channel. To this end, we develop a "bottom-up" coarse-grained (CG) model of the human NPC from recently released cryo-electron tomography structure and then construct composite membrane-embedded C

SUBMITTER: Hudait A 

PROVIDER: S-EPMC10823262 | biostudies-literature | 2024 Jan

REPOSITORIES: biostudies-literature