2024
Rhabdomyolysis in Severe Fever With Thrombocytopenia Syndrome: Associations With Acute Kidney Injury and Mortality
Zhang Z, Hu X, Du Q, Liu J, Chen X, Mo P, Luo M, Jiang Q, Deng L, Xiong Y. Rhabdomyolysis in Severe Fever With Thrombocytopenia Syndrome: Associations With Acute Kidney Injury and Mortality. Journal Of Medical Virology 2024, 96: e70095. PMID: 39624019, DOI: 10.1002/jmv.70095.Peer-Reviewed Original ResearchConceptsAcute kidney injuryKidney injuryRhabdomyolysis groupLaboratory parametersClinical characteristicsLevels of laboratory parametersThrombocytopenia syndromeMultivariate binary logistic regression analysisCumulative survival rateHigh viral loadMortality of patientsSevere feverBinary logistic regression analysisLogistic regression analysisAbdominal painConsecutive patientsSFTS patientsSerum levelsViral loadChest distressAdverse outcomesRhabdomyolysisSurvival ratePatientsSystem injuryHIV-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 regionsClinical characteristics and influencing factors of severe fever with thrombocytopenia syndrome complicated by viral myocarditis: a retrospective study
Du Q, Yu J, Chen Q, Chen X, Jiang Q, Deng L, Li A, Xiong Y. Clinical characteristics and influencing factors of severe fever with thrombocytopenia syndrome complicated by viral myocarditis: a retrospective study. BMC Infectious Diseases 2024, 24: 240. PMID: 38389047, PMCID: PMC10885462, DOI: 10.1186/s12879-024-09096-4.Peer-Reviewed Original ResearchConceptsNT-proBNPConsciousness disorderClinical characteristicsViral myocarditisMultivariate analysisThrombocytopenia syndromeElevated platelet countElevated NT-proBNPIndependent risk factorRate of hypotensionSevere feverValues of LDHElevated LDHAbdominal painCardiac ultrasonographyMethodsRetrospective analysisPlatelet countD-dimerRetrospective studyLaboratory findingsClinical manifestationsAtrial fibrillationAbnormal electrocardiogramClinical dataRisk factors
2023
Function and Cryo-EM structures of broadly potent bispecific antibodies against multiple SARS-CoV-2 Omicron sublineages
Ren P, Hu Y, Peng L, Yang L, Suzuki K, Fang Z, Bai M, Zhou L, Feng Y, Zou Y, Xiong Y, Chen S. Function and Cryo-EM structures of broadly potent bispecific antibodies against multiple SARS-CoV-2 Omicron sublineages. Signal Transduction And Targeted Therapy 2023, 8: 281. PMID: 37518189, PMCID: PMC10387464, DOI: 10.1038/s41392-023-01509-1.Peer-Reviewed Original ResearchThe 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 evidenceModeling 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
2006
Zinc chelation inhibits HIV Vif activity and liberates antiviral function of the cytidine deaminase APOBEC3G
Xiao Z, Ehrlich E, Luo K, Xiong Y, Yu X. Zinc chelation inhibits HIV Vif activity and liberates antiviral function of the cytidine deaminase APOBEC3G. The FASEB Journal 2006, 21: 217-222. PMID: 17135358, DOI: 10.1096/fj.06-6773com.Peer-Reviewed Original ResearchConceptsTetrakis (2-pyridylmethyl) ethylenediamineVif functionZinc chelationE3 ubiquitin ligaseCytidine deaminase APOBEC3GCellular antiviral proteinsLentiviral Vif proteinsAPOBEC3G degradationSubstrate receptorHIV-1 VifMembrane-permeable zinc chelatorVif actsUbiquitin ligaseProteasomal degradationNovel drug designAntiviral functionAntiviral proteinVif proteinAntiviral activityVif activityAPOBEC3GAPOBEC3 proteinsNew targetsInfectivity assaysZinc chelator