2024
HIV-1 usurps mixed-charge domain-dependent CPSF6 phase separation for higher-order capsid binding, nuclear entry and viral DNA integration
Jang S, Bedwell G, Singh S, Yu H, Arnarson B, Singh P, Radhakrishnan R, Douglas A, Ingram Z, Freniere C, Akkermans O, Sarafianos S, Ambrose Z, Xiong Y, Anekal P, Llopis P, KewalRamani V, Francis A, Engelman A. HIV-1 usurps mixed-charge domain-dependent CPSF6 phase separation for higher-order capsid binding, nuclear entry and viral DNA integration. Nucleic Acids Research 2024, 52: 11060-11082. PMID: 39258548, PMCID: PMC11472059, DOI: 10.1093/nar/gkae769.Peer-Reviewed Original ResearchConceptsHIV-1 infectionHIV-1Viral DNA integrationCPSF6 knockout cellsActivity in vitroHIV-1 pathogenesisHIV-1 integrationDNA integrityLiquid-liquid phase separationViral infectionNuclear specklesInfectionCapsids in vitroCPSF6NS depletionNuclear entryCapsid bindingCapsid-binding proteinKnockout cellsBinding proteinSR proteinsNuclear rimCo-aggregationDisordered regions
2023
The capsid lattice engages a bipartite NUP153 motif to mediate nuclear entry of HIV-1 cores
Shen Q, Kumari S, Xu C, Jang S, Shi J, Burdick R, Levintov L, Xiong Q, Wu C, Devarkar S, Tian T, Tripler T, Hu Y, Yuan S, Temple J, Feng Q, Lusk C, Aiken C, Engelman A, Perilla J, Pathak V, Lin C, Xiong Y. The capsid lattice engages a bipartite NUP153 motif to mediate nuclear entry of HIV-1 cores. Proceedings Of The National Academy Of Sciences Of The United States Of America 2023, 120: e2202815120. PMID: 36943880, PMCID: PMC10068764, DOI: 10.1073/pnas.2202815120.Peer-Reviewed Original ResearchConceptsHIV-1 capsidC-terminal tail regionTriple arginine motifNuclear pore complexPhenylalanine-glycine motifsBipartite motifNuclear importPore complexNuclear poresNuclear entryNup153Capsid latticeInteraction moduleProtein latticeCA assemblyCA hexamersIntact capsidsNucleoporinsHIV-1 coreMotifCapsidTail regionIntact formInfection studiesMechanistic evidenceEnrich and switch: IP6 and maturation of HIV-1 capsid
Wu C, Xiong Y. Enrich and switch: IP6 and maturation of HIV-1 capsid. Nature Structural & Molecular Biology 2023, 30: 239-241. PMID: 36849641, PMCID: PMC10033439, DOI: 10.1038/s41594-023-00940-w.Commentaries, Editorials and LettersModeling HIV-1 nuclear entry with nucleoporin-gated DNA-origami channels
Shen Q, Feng Q, Wu C, Xiong Q, Tian T, Yuan S, Shi J, Bedwell G, Yang R, Aiken C, Engelman A, Lusk C, Lin C, Xiong Y. Modeling HIV-1 nuclear entry with nucleoporin-gated DNA-origami channels. Nature Structural & Molecular Biology 2023, 30: 425-435. PMID: 36807645, PMCID: PMC10121901, DOI: 10.1038/s41594-023-00925-9.Peer-Reviewed Original ResearchConceptsNuclear pore complexHIV-1 nuclear entryNuclear entryNuclear importNPC central channelPore complexHost nucleusCapsid dockingVirus genomeAffinity gradientNup153Central channelMechanistic insightsMolecular interactionsCapsidNucleoporinsNup358Nup62GenomeNucleusVirusDockingVirus-1 infectionImportComplexes
2019
The Polar Region of the HIV-1 Envelope Protein Determines Viral Fusion and Infectivity by Stabilizing the gp120-gp41 Association
Lu W, Chen S, Yu J, Behrens R, Wiggins J, Sherer N, Liu S, Xiong Y, Xiang S, Wu L. The Polar Region of the HIV-1 Envelope Protein Determines Viral Fusion and Infectivity by Stabilizing the gp120-gp41 Association. Journal Of Virology 2019, 93: 10.1128/jvi.02128-18. PMID: 30651369, PMCID: PMC6430531, DOI: 10.1128/jvi.02128-18.Peer-Reviewed Original ResearchConceptsHIV-1 fusionHIV-1 infectivityPR mutationsHIV-1 membrane fusionViral entryHIV-1 Env precursorEnv trimersMembrane fusionHIV-1 envelope proteinHIV-1 isolatesViral fusionHIV-1 Env trimersHIV-1 EnvGp120-gp41 associationTransmembrane unitViral envelope glycoproteinsHIV-1Cell-cell fusionViral fusogenicityPolar amino acidsEnv expressionVirus bindingEnvelope glycoproteinFusion inhibitorsTarget cells
2007
Characterization of a Novel Cullin5 Binding Domain in HIV-1 Vif
Xiao Z, Xiong Y, Zhang W, Tan L, Ehrlich E, Guo D, Yu X. Characterization of a Novel Cullin5 Binding Domain in HIV-1 Vif. Journal Of Molecular Biology 2007, 373: 541-550. PMID: 17869271, DOI: 10.1016/j.jmb.2007.07.029.Peer-Reviewed Original ResearchConceptsVif functionHCCH motifA3GPotential new targetsA3G degradationE3 ubiquitin ligaseUbiquitin-proteasome machineryHIV-1 VifAnti-viral drug developmentBC boxCul5 boxUbiquitin ligaseNovel motifProteasomal degradationCys residuesNew targetsDrug developmentMotifCullin5ResiduesStructural requirementsVif
2000
Crystal structure of an adenine bulge in the RNA chain of a DNA·RNA hybrid, d(CTCCTCTTC)·r(gaagagagag)11Edited by I. Tinoco
Sudarsanakumar C, Xiong Y, Sundaralingam M. Crystal structure of an adenine bulge in the RNA chain of a DNA·RNA hybrid, d(CTCCTCTTC)·r(gaagagagag)11Edited by I. Tinoco. Journal Of Molecular Biology 2000, 299: 103-112. PMID: 10860725, DOI: 10.1006/jmbi.2000.3730.Peer-Reviewed Original Research