9CNU

HIV-2 CA hexamer bound with Nup153 peptide; assembled with liposome templating

Summary for 9CNU

• Entry DOI: 10.2210/pdb9cnu/pdb
• EMDB information: 45760
• Descriptor: Capsid protein p24, Nuclear pore complex protein Nup153, INOSITOL HEXAKISPHOSPHATE (3 entities in total)
• Functional Keywords: hiv-2, capsid, ip6, nup153, viral protein
• Biological source: Human immunodeficiency virus 2; More
• Total number of polymer chains: 2
• Total formula weight: 31026.92

Authors

Cook, M.,Freniere, C.,Xiong, Y. (deposition date: 2024-07-15, release date: 2025-03-05)

Primary citation

Cook, M.,Freniere, C.,Wu, C.,Lozano, F.,Xiong, Y.
Structural insights into HIV-2 CA lattice formation and FG-pocket binding revealed by single-particle cryo-EM.
Cell Rep, 44:115245-115245, 2025

PubMed Abstract: One of the striking features of human immunodeficiency virus (HIV) is the capsid, a fullerene cone comprised of pleomorphic capsid protein (CA) that shields the viral genome and recruits cofactors. Despite significant advances in understanding the mechanisms of HIV-1 CA assembly and host factor interactions, HIV-2 CA assembly remains poorly understood. By templating the assembly of HIV-2 CA on functionalized liposomes, we report high-resolution structures of the HIV-2 CA lattice, including both CA hexamers and pentamers, alone and with peptides of host phenylalanine-glycine (FG)-motif proteins Nup153 and CPSF6. While the overall fold and mode of FG-peptide binding is conserved with HIV-1, this study reveals distinctive features of the HIV-2 CA lattice, including differing structural character at regions of host factor interactions and divergence in the mechanism of formation of CA hexamers and pentamers. This study extends our understanding of HIV capsids and highlights an approach facilitating the study of lentiviral capsid biology.

PubMed: 39864060
DOI: 10.1016/j.celrep.2025.115245

Experimental method

ELECTRON MICROSCOPY (2.99 Å)