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Instruments / Technical Area	Publication Details	Published	Actions
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
	Cytoplasmic CPSF6 regulates HIV-1 capsid trafficking and infection in a cyclophilin A-dependent manner Zhou Zhong , Jiying Ning , Emerson A. Boggs , Sooin Jang , Callen Wallace , Cheryl Telmer , Marcel P. Bruchez , Jinwoo Ahn , Alan N. Engelman , Peijun Zhang , Simon C. Watkins , Zandrea Ambrose Mbio 12 DOI: 10.1128/mBio.03142-20 Open Access Show Abstract ▼ Abstract: Human immunodeficiency virus type 1 (HIV-1) capsid binds host proteins during infection, including cleavage and polyadenylation specificity factor 6 (CPSF6) and cyclophilin A (CypA). We observe that HIV-1 infection induces higher-order CPSF6 formation, and capsid-CPSF6 complexes cotraffic on microtubules. CPSF6-capsid complex trafficking is impacted by capsid alterations that reduce CPSF6 binding or by excess cytoplasmic CPSF6 expression, both of which are associated with decreased HIV-1 infection. Higher-order CPSF6 complexes bind and disrupt HIV-1 capsid assemblies in vitro. Disruption of HIV-1 capsid binding to CypA leads to increased CPSF6 binding and altered capsid trafficking, resulting in reduced infectivity. Our data reveal an interplay between CPSF6 and CypA that is important for cytoplasmic capsid trafficking and HIV-1 infection. We propose that CypA prevents HIV-1 capsid from prematurely engaging cytoplasmic CPSF6 and that differences in CypA cellular localization and innate immunity may explain variations in HIV-1 capsid trafficking and uncoating in CD4+ T cells and macrophages.	Apr 2021

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