2024
Rab6a enables BICD2/dynein-mediated trafficking of human papillomavirus from the trans-Golgi network during virus entry.
Choi J, Speckhart K, Tsai B, DiMaio D. Rab6a enables BICD2/dynein-mediated trafficking of human papillomavirus from the trans-Golgi network during virus entry. MBio 2024, e0281124. PMID: 39431827, DOI: 10.1128/mbio.02811-24.Peer-Reviewed Original ResearchRab proteinsDNA virusesVirus entryHPV traffickingIntra-Golgi transportTrans-Golgi networkIntracellular vesicular transportMotor protein complexInfected cellsIntra-GolgiL2 capsid proteinRab GTPasesDynein adaptorsNon-enveloped DNA virusesRetrograde traffickingGolgi apparatusPotential targetProtein complexesVesicular transportRab6ADyneinTGNCapsid proteinRabCellular enzymes
2023
HPV is a cargo for the COPI sorting complex during virus entry
Harwood M, Woo T, Takeo Y, DiMaio D, Tsai B. HPV is a cargo for the COPI sorting complex during virus entry. Science Advances 2023, 9: eadc9830. PMID: 36662862, PMCID: PMC9858521, DOI: 10.1126/sciadv.adc9830.Peer-Reviewed Original ResearchConceptsCoat protein complex ITrans-Golgi networkProtein complex IGene knockdown strategyVirus entryCOPI complexProtein complexesCellular fractionationUnbiased proteomicsRetrograde traffickingCytoplasmic segmentGolgi stacksCellular cargoL2 mutantKnockdown strategyGolgi apparatusComplex IIncoming virusCell surfaceGolgiHost factorsCargoComplexesMutantsEndosomes
2020
Cell-penetrating peptide inhibits retromer-mediated human papillomavirus trafficking during virus entry
Zhang P, Moreno R, Lambert PF, DiMaio D. Cell-penetrating peptide inhibits retromer-mediated human papillomavirus trafficking during virus entry. Proceedings Of The National Academy Of Sciences Of The United States Of America 2020, 117: 6121-6128. PMID: 32123072, PMCID: PMC7084110, DOI: 10.1073/pnas.1917748117.Peer-Reviewed Original ResearchConceptsEssential protein-protein interactionsCellular protein complexesProtein-protein interactionsIntracellular virus traffickingRetrograde transport pathwaySites of replicationCell-penetrating sequenceProtein complexesCellular proteinsVirus replicationHPV16 pseudovirus infectionVirus traffickingL2 capsid proteinsAspects of infectionCapsid proteinHPV entryViral genomeViral proteinsIncoming virionsViral componentsHuman papillomavirus infectionProteinAntiviral targetDose-dependent blockVirus entry
2015
Direct Binding of Retromer to Human Papillomavirus Type 16 Minor Capsid Protein L2 Mediates Endosome Exit during Viral Infection
Popa A, Zhang W, Harrison MS, Goodner K, Kazakov T, Goodwin EC, Lipovsky A, Burd CG, DiMaio D. Direct Binding of Retromer to Human Papillomavirus Type 16 Minor Capsid Protein L2 Mediates Endosome Exit during Viral Infection. PLOS Pathogens 2015, 11: e1004699. PMID: 25693203, PMCID: PMC4334968, DOI: 10.1371/journal.ppat.1004699.Peer-Reviewed Original ResearchConceptsTrans-Golgi networkRetromer cargoTransmembrane proteinGolgi apparatusDirect bindingCoat protein complexCellular transmembrane proteinsVirus entryMinor capsid proteinCarboxy-terminal segmentProtein complexesL2 minor capsid proteinMinor capsid protein L2Early endosomesVesicular transportRetromerPlasma membraneEndosomal membranesBinding motifProtein L2Capsid proteinEndosomesL2 proteinViral componentsProtein
2000
E2F-Rb Complexes Assemble and Inhibit cdc25A Transcription in Cervical Carcinoma Cells following Repression of Human Papillomavirus Oncogene Expression
Wu L, Goodwin E, Naeger L, Vigo E, Galaktionov K, Helin K, DiMaio D. E2F-Rb Complexes Assemble and Inhibit cdc25A Transcription in Cervical Carcinoma Cells following Repression of Human Papillomavirus Oncogene Expression. Molecular And Cellular Biology 2000, 20: 7059-7067. PMID: 10982822, PMCID: PMC86242, DOI: 10.1128/mcb.20.19.7059-7067.2000.Peer-Reviewed Original ResearchMeSH KeywordsBinding SitesBovine papillomavirus 1Carcinoma, Squamous CellCarrier ProteinsCdc25 PhosphatasesCell CycleCell Cycle ProteinsCell Transformation, NeoplasticCell Transformation, ViralConsensus SequenceCysteine EndopeptidasesDNA, NeoplasmDNA-Binding ProteinsE2F Transcription FactorsE2F4 Transcription FactorFemaleGene Expression Regulation, NeoplasticGene Expression Regulation, ViralGenes, RetinoblastomaHumansMacromolecular SubstancesMultienzyme ComplexesNeoplasm ProteinsPapillomaviridaePapillomavirus InfectionsPhosphoproteinsPromoter Regions, GeneticProteasome Endopeptidase ComplexProtein BindingProteinsRecombinant Fusion ProteinsRetinoblastoma ProteinRetinoblastoma-Binding Protein 1Retinoblastoma-Like Protein p130Transcription Factor DP1Transcription FactorsTransfectionTumor Cells, CulturedTumor Virus InfectionsUterine Cervical NeoplasmsViral ProteinsConceptsCdc25A promoterE6/E7 repressionCervical carcinoma cellsE2F siteBovine papillomavirus E2 proteinE2 proteinE7 repressionWild-type E2 proteinE2F-responsive promotersRb tumor suppressor pathwayPapillomavirus E2 proteinCarcinoma cellsE2F-Rb complexesCell cycle genesHuman papillomavirus oncogene expressionHuman papillomavirus (HPV) E6/E7 oncogenesTumor suppressor pathwayMechanism of repressionHPV E6/E7 expressionCell cycle progressionCdc25A transcriptionDramatic growth arrestE2F complexesConsensus E2FProtein complexes
1992
A glutamine residue in the membrane-associating domain of the bovine papillomavirus type 1 E5 oncoprotein mediates its binding to a transmembrane component of the vacuolar H(+)-ATPase
Goldstein D, Kulke R, Dimaio D, Schlegel R. A glutamine residue in the membrane-associating domain of the bovine papillomavirus type 1 E5 oncoprotein mediates its binding to a transmembrane component of the vacuolar H(+)-ATPase. Journal Of Virology 1992, 66: 405-413. PMID: 1370089, PMCID: PMC238300, DOI: 10.1128/jvi.66.1.405-413.1992.Peer-Reviewed Original ResearchConceptsK proteinGrowth factor receptorE5 oncoproteinGlutamine residuesRandom hydrophobic sequencesSpecific amino acid residuesMembrane-associated domainMajor transforming proteinK protein componentCarboxyl-terminal domainEndoplasmic reticulum membraneFactor receptorBovine papillomavirus type 1Colony-stimulating factor 1 receptorTransformation-defective mutantsAmino acid residuesPotential binding sitesPlatelet-derived growth factor receptorAmino acid substitutionsPapillomavirus type 1Hydrophilic amino acidsE5 dimerE5 mutantsFactor 1 receptorProtein complexes