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	Multidisciplinary studies with mutated HIV-1 capsid proteins reveal structural mechanisms of lattice stabilization Anna T. Gres , Karen A. Kirby , William M. Mcfadden , Haijuan Du , Dandan Liu , Chaoyi Xu , Alexander J. Bryer , Juan R. Perilla , Jiong Shi , Christopher Aiken , Xiaofeng Fu , Peijun Zhang , Ashwanth C. Francis , Gregory B. Melikyan , Stefan G. Sarafianos Nature Communications 14 DOI: 10.1038/s41467-023-41197-7 Open Access Show Abstract ▼ Abstract: HIV-1 capsid (CA) stability is important for viral replication. E45A and P38A mutations enhance and reduce core stability, thus impairing infectivity. Second-site mutations R132T and T216I rescue infectivity. Capsid lattice stability was studied by solving seven crystal structures (in native background), including P38A, P38A/T216I, E45A, E45A/R132T CA, using molecular dynamics simulations of lattices, cryo-electron microscopy of assemblies, time-resolved imaging of uncoating, biophysical and biochemical characterization of assembly and stability. We report pronounced and subtle, short- and long-range rearrangements: (1) A38 destabilized hexamers by loosening interactions between flanking CA protomers in P38A but not P38A/T216I structures. (2) Two E45A structures showed unexpected stabilizing CANTD-CANTD inter-hexamer interactions, variable R18-ring pore sizes, and flipped N-terminal β-hairpin. (3) Altered conformations of E45Aa α9-helices compared to WT, E45A/R132T, WTPF74, WTNup153, and WTCPSF6 decreased PF74, CPSF6, and Nup153 binding, and was reversed in E45A/R132T. (4) An environmentally sensitive electrostatic repulsion between E45 and D51 affected lattice stability, flexibility, ion and water permeabilities, electrostatics, and recognition of host factors.	Sep 2023
Krios I-Titan Krios I at Diamond Krios II-Titan Krios II at Diamond Krios IV-Titan Krios IV at Diamond	Structure of native HIV-1 cores and their interactions with IP6 and CypA Tao Ni , Yanan Zhu , Zhengyi Yang , Chaoyi Xu , Yuriy Chaban , Tanya Nesterova , Jiying Ning , Till Böcking , Michael W. Parker , Christina Monnie , Jinwoo Ahn , Juan R. Perilla , Peijun Zhang Science Advances 7 DOI: 10.1126/sciadv.abj5715 Diamond Proposal Number(s): [21004, 20223] Open Access Show Abstract ▼ Abstract: The viral capsid plays essential roles in HIV replication and is a major platform engaging host factors. To overcome challenges in study native capsid structure, we used the perfringolysin O to perforate the membrane of HIV-1 particles, thus allowing host proteins and small molecules to access the native capsid while improving cryo–electron microscopy image quality. Using cryo–electron tomography and subtomogram averaging, we determined the structures of native capsomers in the presence and absence of inositol hexakisphosphate (IP6) and cyclophilin A and constructed an all-atom model of a complete HIV-1 capsid. Our structures reveal two IP6 binding sites and modes of cyclophilin A interactions. Free energy calculations substantiate the two binding sites at R18 and K25 and further show a prohibitive energy barrier for IP6 to pass through the pentamer. Our results demonstrate that perfringolysin O perforation is a valuable tool for structural analyses of enveloped virus capsids and interactions with host cell factors.	Nov 2021

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