2024
A substitution at the cytoplasmic tail of the spike protein enhances SARS-CoV-2 infectivity and immunogenicity
Li Y, Zhang X, Tai W, Zhuang X, Shi H, Liao S, Yu X, Mei R, Chen X, Huang Y, Liu Y, Liu J, Liu Y, Zhu Y, Wang P, Tian M, Yu G, Li L, Cheng G. A substitution at the cytoplasmic tail of the spike protein enhances SARS-CoV-2 infectivity and immunogenicity. EBioMedicine 2024, 110: 105437. PMID: 39531918, DOI: 10.1016/j.ebiom.2024.105437.Peer-Reviewed Original ResearchS proteinCytoplasmic tailFERM-binding motifTrans-complementation systemSpike proteinAmino acid substitutionsProline-to-leucine substitutionSystematic bioinformatics analysisHigh-frequency mutationsSARS-CoV-2 virionsBinding motifAcid substitutionsSARS-CoV-2Natural selectionBioinformatics analysisEzrin/radixin/moesin proteinsMolecular mechanismsMutationsOmicron variantProteinVaccine developmentMRNA vaccinesGlobal disseminationSARS-CoV-2 Omicron sublineagesSublineages
2020
Roles of Symbiotic Microorganisms in Arboviral Infection of Arthropod Vectors
Yin C, Sun P, Yu X, Wang P, Cheng G. Roles of Symbiotic Microorganisms in Arboviral Infection of Arthropod Vectors. Trends In Parasitology 2020, 36: 607-615. PMID: 32386795, DOI: 10.1016/j.pt.2020.04.009.Peer-Reviewed Original Research
2018
Zika Virus Non-structural Protein 4A Blocks the RLR-MAVS Signaling
Ma J, Ketkar H, Geng T, Lo E, Wang L, Xi J, Sun Q, Zhu Z, Cui Y, Yang L, Wang P. Zika Virus Non-structural Protein 4A Blocks the RLR-MAVS Signaling. Frontiers In Microbiology 2018, 9: 1350. PMID: 29988497, PMCID: PMC6026624, DOI: 10.3389/fmicb.2018.01350.Peer-Reviewed Original ResearchMelanoma differentiation-associated protein 5Zika virusImmune responseNon-structural protein 4AReceptor-mediated immune responsesToll-like receptor-mediated immune responsesRe-emerging flavivirusGuillain-Barre syndromeAntiviral immune responseType I interferon inductionHost immune systemI interferon inductionMammalian host immune systemProtein 4AN-terminal caspase activationMolecular mechanismsNeonatal microcephalyZIKV pathogenesisZIKV replicationImmune evasionImmune systemHuman trophoblastsReceptor signalingSubsequent inductionProtein 5Foot-and-mouth disease virus capsid protein VP2 activates the cellular EIF2S1-ATF4 pathway and induces autophagy via HSPB1
Sun P, Zhang S, Qin X, Chang X, Cui X, Li H, Zhang S, Gao H, Wang P, Zhang Z, Luo J, Li Z. Foot-and-mouth disease virus capsid protein VP2 activates the cellular EIF2S1-ATF4 pathway and induces autophagy via HSPB1. Autophagy 2018, 14: 336-346. PMID: 29166823, PMCID: PMC5902195, DOI: 10.1080/15548627.2017.1405187.Peer-Reviewed Original ResearchConceptsCapsid protein VP2FMDV infectionProtein VP2Polyglutamine expansion proteinsMacroautophagy/autophagyMammalian cell linesPrecise molecular mechanismsFMDV capsid proteinsNatural host cellsInhibition of autophagyCloven-hoofed animalsAutophagy inductionMolecular mechanismsAutophagy processHost cellsAkt-mTORMouth disease virusCapsid proteinViral replicationAutophagyFMDV replicationHSPB1InfectionCell linesVP2