9CNT

HIV-2 CA pentamer; assembled via liposome templating

9CNT の概要

• エントリーDOI: 10.2210/pdb9cnt/pdb
• EMDBエントリー: 45759
• 分子名称: Capsid protein p24, INOSITOL HEXAKISPHOSPHATE (2 entities in total)
• 機能のキーワード: hiv-2, capsid, ip6, viral protein
• 由来する生物種: Human immunodeficiency virus 2
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 108558.03

構造登録者

Cook, M.,Freniere, C.,Xiong, Y. (登録日: 2024-07-15, 公開日: 2025-03-05)

主引用文献

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

実験手法

ELECTRON MICROSCOPY (2.97 Å)