Abstract：
:HIV-1 uses the microtubule network to traffic the viral capsid core toward the nucleus. Viral nuclear trafficking and infectivity require the kinesin-1 adaptor protein FEZ1. Here, we demonstrate that FEZ1 directly interacts with the HIV-1 capsid and specifically binds capsid protein (CA) hexamers. FEZ1 contains multiple acidic, poly-glutamate stretches that interact with the positively charged central pore of CA hexamers. The FEZ1-capsid interaction directly competes with nucleotides and inositol hexaphosphate (IP6) that bind at the same location. In addition, all-atom molecular dynamic (MD) simulations establish the molecular details of FEZ1-capsid interactions. Functionally, mutation of the FEZ1 capsid-interacting residues significantly reduces trafficking of HIV-1 particles toward the nucleus and early infection. These findings support a model in which the central capsid hexamer pore is a general HIV-1 cofactor-binding hub and FEZ1 serves as a unique CA hexamer pattern sensor to recognize this site and promote capsid trafficking in the cell.
journal_name
Cell Repjournal_title
Cell reportsauthors
Huang PT,Summers BJ,Xu C,Perilla JR,Malikov V,Naghavi MH,Xiong Ydoi
10.1016/j.celrep.2019.07.079subject
Has Abstractpub_date
2019-08-27 00:00:00pages
2373-2385.e7issue
9issn
2211-1247pii
S2211-1247(19)30983-0journal_volume
28pub_type
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