HIV-1 capsids enter the FG phase of nuclear pores like a transport receptor.

ABSTRACT: HIV-1 infection requires nuclear entry of the viral genome. Previous evidence suggests that this entry proceeds through nuclear pore complexes (NPCs), with the 120 × 60 nm capsid squeezing through an approximately 60-nm-wide central channel¹ and crossing the permeability barrier of the NPC. This barrier can be described as an FG phase² that is assembled from cohesively interacting phenylalanine-glycine (FG) repeats³ and is selectively permeable to cargo captured by nuclear transport receptors (NTRs). Here we show that HIV-1 capsid assemblies can target NPCs efficiently in an NTR-independent manner and bind directly to several types of FG repeats, including barrier-forming cohesive repeats. Like NTRs, the capsid readily partitions into an in vitro assembled

SUBMITTER: Fu L 

PROVIDER: S-EPMC10881386 | biostudies-literature | 2024 Feb

REPOSITORIES: biostudies-literature