2023
Structural basis for recruitment of host CypA and E3 ubiquitin ligase by maedi-visna virus Vif
Hu Y, Gudnadóttir R, Knecht K, Arizaga F, Jónsson S, Xiong Y. Structural basis for recruitment of host CypA and E3 ubiquitin ligase by maedi-visna virus Vif. Science Advances 2023, 9: eadd3422. PMID: 36638173, PMCID: PMC9839330, DOI: 10.1126/sciadv.add3422.Peer-Reviewed Original ResearchConceptsMVV VifCryo-electron microscopy structureE3 ubiquitin ligase complexLentiviral VifUbiquitin ligase complexHost cofactorsUbiquitin-proteasome pathwayDistinct interaction modesUnique structural elementsLentiviral Vif proteinsEvolutionary relationshipsMicroscopy structureLigase complexCellular proteinsE3 ubiquitinAntiviral APOBEC3Structural basisFunctional analysisMolecular mechanismsMaedi-visna virusRecruitment mechanismsVif proteinCofactorProteinCypA
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