Through MD simulations we show that capsids face a significant steric barrier inside the NPC, especially when the vast amount of intrinsically disordered FG-Nups in the central channel are included. This barrier could be relieved by a crack in the NPC.

CLEM-ET data showed that morphologically intact cone-shaped capsids could be found inside the central channel of NPCs and also directly underneath in the nucleus further solidifying that capsids do not need to disassemble for nuclear entry.

@jpkreysing.bsky.social, @maziarheidari.bsky.social, Vojtech Zila, and others studied HIV-1 capsid nuclear entry in primary human macrophages using STED, CLEM-ET, cryo-ET (#TeamTomo), and MD simulations. First, 3D STED revealed capsid signal accumulation at nuclear pores.

In a great collaboration with @hummerlab.bsky.social and the Kräusslich lab: HIV capsid doesn't break at the NPC; instead, it cracks open the NPC itself! Details in Cell: authors.elsevier.com/sd/article/S... @mpibp.bsky.social @uniheidelberg.bsky.social A thread below: