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
2017
Single methyl groups can act as toggle switches to specify transmembrane Protein-protein interactions
He L, Steinocher H, Shelar A, Cohen EB, Heim EN, Kragelund BB, Grigoryan G, DiMaio D. Single methyl groups can act as toggle switches to specify transmembrane Protein-protein interactions. ELife 2017, 6: e27701. PMID: 28869036, PMCID: PMC5597333, DOI: 10.7554/elife.27701.Peer-Reviewed Original ResearchConceptsProtein-protein interactionsErythropoietin receptorTransmembrane proteinTransmembrane protein-protein interactionsTMD interactionsModel transmembrane proteinMouse erythropoietin receptorHuman erythropoietin receptorSingle methyl groupGrowth factor independenceSide chain methyl groupsCellular processesMouse cellsFactor independenceChain methyl groupsIntrinsic specificityToggle switchTraptamersMethyl groupProteinReceptor activitySpecific positionsReceptorsSpecificityOligomerizationTwo transmembrane dimers of the bovine papillomavirus E5 oncoprotein clamp the PDGF β receptor in an active dimeric conformation
Karabadzhak AG, Petti LM, Barrera FN, Edwards APB, Moya-Rodríguez A, Polikanov YS, Freites JA, Tobias DJ, Engelman DM, DiMaio D. Two transmembrane dimers of the bovine papillomavirus E5 oncoprotein clamp the PDGF β receptor in an active dimeric conformation. Proceedings Of The National Academy Of Sciences Of The United States Of America 2017, 114: e7262-e7271. PMID: 28808001, PMCID: PMC5584431, DOI: 10.1073/pnas.1705622114.Peer-Reviewed Original ResearchConceptsTransmembrane domainE5 proteinE5 dimerPlatelet-derived growth factor β receptorGrowth factor β receptorActive dimeric conformationPDGF β-receptorTransmembrane dimerProtein bindsMembrane environmentReceptor dimerizationDimeric conformationAtom molecular dynamics simulationsBiochemical experimentsMouse cellsMolecular mechanismsActive dimerΒ receptorBovine papillomavirusProteinSpecific interactionsMembrane modelingReceptor activationDimerizationComplexes
1999
The Bovine Papillomavirus E5 Protein Requires a Juxtamembrane Negative Charge for Activation of the Platelet-Derived Growth Factor β Receptor and Transformation of C127 Cells
Klein O, Kegler-Ebo D, Su J, Smith S, DiMaio D. The Bovine Papillomavirus E5 Protein Requires a Juxtamembrane Negative Charge for Activation of the Platelet-Derived Growth Factor β Receptor and Transformation of C127 Cells. Journal Of Virology 1999, 73: 3264-3272. PMID: 10074180, PMCID: PMC104090, DOI: 10.1128/jvi.73.4.3264-3272.1999.Peer-Reviewed Original ResearchConceptsPlatelet-derived growth factor beta receptorPDGF beta receptorGrowth factor beta receptorE5 proteinBovine papillomavirus E5 proteinCell transformationHomodimeric transmembrane proteinSustained receptor activationC127 mouse fibroblastsExtracellular juxtamembrane regionBeta receptorsE5 dimerE5 mutantsDouble mutantJuxtamembrane regionTransmembrane proteinC127 cellsC-terminusAcidic residuesE5 geneMutantsPosition 33Mouse fibroblastsProteinSalt bridge
1998
Bovine papillomavirus E5 protein induces oligomerization and trans-phosphorylation of the platelet-derived growth factor β receptor
Lai C, Henningson C, DiMaio D. Bovine papillomavirus E5 protein induces oligomerization and trans-phosphorylation of the platelet-derived growth factor β receptor. Proceedings Of The National Academy Of Sciences Of The United States Of America 1998, 95: 15241-15246. PMID: 9860953, PMCID: PMC28027, DOI: 10.1073/pnas.95.26.15241.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SubstitutionAnimalsBovine papillomavirus 1CattleCell LineCell Line, TransformedCross-Linking ReagentsDimerizationHumansKineticsMacromolecular SubstancesMiceOncogene Proteins, ViralPhosphorylationProtein-Tyrosine KinasesReceptor, Platelet-Derived Growth Factor betaReceptors, Platelet-Derived Growth FactorRecombinant ProteinsSequence DeletionTransfectionConceptsBovine papillomavirus E5 proteinE5 proteinPDGF beta receptorCellular platelet-derived growth factor (PDGF) beta receptorKinase-negative mutant receptorPlatelet-derived growth factor beta receptorPlatelet-derived growth factor β receptorChemical cross-linking experimentsGrowth factor β receptorConstitutive tyrosine phosphorylationGrowth factor beta receptorLigand-independent fashionCross-linking experimentsReceptor tyrosine kinasesStable complexesExtracts of cellsPDGF beta-receptor activationIntramolecular autophosphorylationBeta receptorsCoimmunoprecipitation experimentsTransmembrane proteinReceptor activationTyrosine phosphorylationReceptor dimerizationMutant receptorsA single amino acid substitution in a WW‐like domain of diverse members of the PDGF receptor subfamily of tyrosine kinases causes constitutive receptor activation
Irusta P, DiMaio D. A single amino acid substitution in a WW‐like domain of diverse members of the PDGF receptor subfamily of tyrosine kinases causes constitutive receptor activation. The EMBO Journal 1998, 17: 6912-6923. PMID: 9843497, PMCID: PMC1171039, DOI: 10.1093/emboj/17.23.6912.Peer-Reviewed Original ResearchMeSH KeywordsAlanineAmino Acid SequenceAmino Acid SubstitutionAnimalsBinding SitesCell Line, TransformedCloning, MolecularDimerizationEnzyme ActivationHumansInterleukin-3LigandsMiceMolecular Sequence DataMutagenesis, Site-DirectedPeptidesPhosphorylationPolymerase Chain ReactionReceptor Protein-Tyrosine KinasesReceptor, Platelet-Derived Growth Factor betaReceptors, Platelet-Derived Growth FactorSequence Homology, Amino AcidStructure-Activity RelationshipTyrosineValineConceptsTyrosine kinase activityKinase activityTyrosine kinasePlatelet-derived growth factor beta receptorCytoplasmic juxtamembrane domainPDGF receptorSignal transduction proteinsWW-like domainTransmembrane receptor tyrosine kinaseProtein-protein interactionsBa/F3 cellsGST fusion proteinSingle amino acid substitutionConstitutive receptor activationGrowth factor beta receptorAbsence of ligandReceptor tyrosine kinasesAmino acid substitutionsSequence PPXYTransduction proteinsWW domainsCellular functionsJuxtamembrane regionTyrosine phosphorylationAlanine substitutionsVIROCRINE TRANSFORMATION: The Intersection Between Viral Transforming Proteins and Cellular Signal Transduction Pathways
DiMaio D, Lai C, Klein O. VIROCRINE TRANSFORMATION: The Intersection Between Viral Transforming Proteins and Cellular Signal Transduction Pathways. Annual Review Of Microbiology 1998, 52: 397-421. PMID: 9891803, DOI: 10.1146/annurev.micro.52.1.397.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntigens, Polyomavirus TransformingBovine papillomavirus 1CattleCell Transformation, ViralHerpesvirus 4, HumanMiceOncogene ProteinsReceptor Protein-Tyrosine KinasesReceptor, Platelet-Derived Growth Factor betaReceptors, ErythropoietinReceptors, Platelet-Derived Growth FactorReceptors, Tumor Necrosis FactorSignal TransductionViral Envelope ProteinsViral Matrix ProteinsViral ProteinsConceptsCellular signal transduction pathwaysSignal transduction pathwaysTransduction pathwaysPlatelet-derived growth factor beta receptorPolyoma virus middle T antigenCellular signal transductionViral transforming proteinsCellular signaling pathwaysViral transformationMiddle T antigenGrowth factor beta receptorReceptor tyrosine kinasesTransforming proteinSignal transductionE5 proteinTumor necrosis factor receptorErythropoietin receptorTyrosine kinaseSignaling pathwaysCell transformationDiverse virusesNecrosis factor receptorViral oncoproteinsSpleen focusT antigenOncogenic activation of the PDGF β receptor by the transmembrane domain of p185neu*
Petti L, Irusta P, DiMaio D. Oncogenic activation of the PDGF β receptor by the transmembrane domain of p185neu*. Oncogene 1998, 16: 843-851. PMID: 9484775, DOI: 10.1038/sj.onc.1201590.Peer-Reviewed Original ResearchConceptsBa/F3 cellsTransmembrane domainBa/F3 hematopoietic cellsF3 cellsWild-type PDGF receptorNovel tyrosine phosphorylated proteinsIL-3-independent growthTyrosine phosphorylated proteinsDistinct signaling pathwaysWild-type PDGFLevels of phosphotyrosineWild-type receptorIL-3Β receptorPDGF β-receptorPhosphorylated proteinsTyrosine autophosphorylationOncogenic formsKinase activityMouse C127Receptor homodimerizationOncogenic activationSignaling pathwaysChimeric receptorsFoci formation
1997
Identification of amino acids in the transmembrane and juxtamembrane domains of the platelet-derived growth factor receptor required for productive interaction with the bovine papillomavirus E5 protein
Petti L, Reddy V, Smith S, DiMaio D. Identification of amino acids in the transmembrane and juxtamembrane domains of the platelet-derived growth factor receptor required for productive interaction with the bovine papillomavirus E5 protein. Journal Of Virology 1997, 71: 7318-7327. PMID: 9311809, PMCID: PMC192076, DOI: 10.1128/jvi.71.10.7318-7327.1997.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBovine papillomavirus 1CattleCell LineCell MembraneErbB ReceptorsHumansInterleukin-3KineticsLeucineLysineMiceMolecular Sequence DataMutagenesis, Site-DirectedOncogene Proteins v-sisOncogene Proteins, ViralPoint MutationPolymerase Chain ReactionProtein Structure, SecondaryRatsReceptor, ErbB-2Receptor, Platelet-Derived Growth Factor betaReceptors, Platelet-Derived Growth FactorReceptors, VirusRecombinant Fusion ProteinsRetroviridae Proteins, OncogenicSequence AlignmentThreonineTransfectionConceptsBovine papillomavirus E5 proteinE5 proteinTransmembrane domainPDGF beta receptorAmino acidsCellular platelet-derived growth factor (PDGF) beta receptorReceptor mutantsJuxtamembrane domainPlatelet-derived growth factor beta receptorPutative transmembrane domainsMurine Ba/F3 cellsCarboxyl-terminal domainBa/F3 cellsV-sisReceptor tyrosine phosphorylationExtracellular juxtamembrane domainGrowth factor beta receptorSpecific amino acidsProductive interactionReceptor activationPlatelet-derived growth factor receptorAcidic amino acidsComplex formationThreonine residuesBeta receptors
1995
Mutational analysis of the interaction between the bovine papillomavirus E5 transforming protein and the endogenous beta receptor for platelet-derived growth factor in mouse C127 cells
Nilson L, Gottlieb R, Polack G, DiMaio D. Mutational analysis of the interaction between the bovine papillomavirus E5 transforming protein and the endogenous beta receptor for platelet-derived growth factor in mouse C127 cells. Journal Of Virology 1995, 69: 5869-5874. PMID: 7543592, PMCID: PMC189463, DOI: 10.1128/jvi.69.9.5869-5874.1995.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBinding SitesBovine papillomavirus 1Cell LineDNA Mutational AnalysisDown-RegulationFrameshift MutationKineticsMiceMolecular Sequence DataMutagenesisMutagenesis, Site-DirectedOncogene Proteins, ViralPhosphotyrosinePoint MutationProtein-Tyrosine KinasesReceptor, Platelet-Derived Growth Factor betaReceptors, Platelet-Derived Growth FactorRecombinant ProteinsTyrosineConceptsMouse C127 cellsE5 proteinReceptor tyrosine phosphorylationTyrosine phosphorylationPDGF beta receptorC127 cellsPDGF receptorWild-type E5 proteinBovine papillomavirus E5 proteinCarboxyl-terminal cysteine residueCell transformationPlatelet-derived growth factor beta receptorMembrane-associated proteinsSustained receptor activationPDGF receptor activationMutation of glutamineTransformation-competent mutantsGrowth factor beta receptorBovine papillomavirus E5Carboxyl-terminal positionBeta receptorsHigh-level expressionPlatelet-derived growth factorStable complex formationReceptor activationLigand-Independent Activation of the Platelet-Derived Growth Factor β Receptor: Requirements for Bovine Papillomavirus E5-Induced Mitogenic Signaling
Drummond-Barbosa D, Vaillancourt R, Kazlauskas A, DiMaio D. Ligand-Independent Activation of the Platelet-Derived Growth Factor β Receptor: Requirements for Bovine Papillomavirus E5-Induced Mitogenic Signaling. Molecular And Cellular Biology 1995, 15: 2570-2581. PMID: 7739538, PMCID: PMC230487, DOI: 10.1128/mcb.15.5.2570.Peer-Reviewed Original ResearchConceptsE5 proteinPDGF beta receptorTyrosine phosphorylationMitogenic signalsMitogenic signalingReceptor mutantsSH2 domain-containing proteinsPlatelet-derived growth factor beta receptorPDGF beta receptor tyrosine kinaseDomain-containing proteinsPhosphorylation of substratesInterleukin-3Tyrosine phosphorylation sitesGrowth factor β receptorBa/F3 cellsReceptor tyrosine phosphorylationGrowth factor beta receptorLigand-independent activationReceptor tyrosine kinasesTyrosine kinase activityBovine papillomavirus E5Beta receptorsComplex formationPhosphorylation sitesReceptor autophosphorylationAn intact PDGF signaling pathway is required for efficient growth transformation of mouse C127 cells by the bovine papillomavirus E5 protein.
Riese D, DiMaio D. An intact PDGF signaling pathway is required for efficient growth transformation of mouse C127 cells by the bovine papillomavirus E5 protein. Oncogene 1995, 10: 1431-9. PMID: 7731695.Peer-Reviewed Original ResearchConceptsBPV E5 proteinPDGF beta receptorE5 proteinE5 geneC127 cellsBovine papillomavirus E5 proteinPDGF beta-receptor genePlatelet-derived growth factor beta receptorGrowth transformationBovine papillomavirus type 1 E5 proteinC127 cell linesMembrane-associated proteinsMouse C127 cellsHeterologous cell typesV-sis oncogeneDNA synthesisGrowth factor beta receptorStable growth transformationBeta receptor geneCell linesBeta receptorsBPV E5Reduced DNA synthesisMouse C127Genetic support
1994
Specific interaction between the bovine papillomavirus E5 transforming protein and the beta receptor for platelet-derived growth factor in stably transformed and acutely transfected cells
Petti L, DiMaio D. Specific interaction between the bovine papillomavirus E5 transforming protein and the beta receptor for platelet-derived growth factor in stably transformed and acutely transfected cells. Journal Of Virology 1994, 68: 3582-3592. PMID: 8189497, PMCID: PMC236862, DOI: 10.1128/jvi.68.6.3582-3592.1994.Peer-Reviewed Original ResearchConceptsPDGF beta receptorE5 proteinPlatelet-derived growth factorEGF receptorEpidermal growth factorGrowth factor receptorCOS cellsTumorigenic transformationBovine fibroblastsPDGF receptorHeterologous cell systemFactor receptorNIH 3T3 cellsGrowth factorBovine papillomavirus E5Beta receptorsMembrane proteinsTransient overexpressionRodent fibroblastsCell typesProteinBovine papillomavirusPotential targetSpecific interactionsEpithelial cells
1993
Hierarchy of polyadenylation site usage by bovine papillomavirus in transformed mouse cells
Andrews E, DiMaio D. Hierarchy of polyadenylation site usage by bovine papillomavirus in transformed mouse cells. Journal Of Virology 1993, 67: 7705-7710. PMID: 7901430, PMCID: PMC238246, DOI: 10.1128/jvi.67.12.7705-7710.1993.Peer-Reviewed Original ResearchAnimalsAntisense Elements (Genetics)Base SequenceBovine papillomavirus 1Cell Transformation, ViralCells, CulturedCloning, MolecularConsensus SequenceDNA, ComplementaryMiceMolecular Sequence DataMutagenesisPoly APolymerase Chain ReactionRegulatory Sequences, Nucleic AcidRNA Processing, Post-TranscriptionalRNA, MessengerSequence Analysis, DNAPlatelet-derived growth factor receptor can mediate tumorigenic transformation by the bovine papillomavirus E5 protein.
Nilson L, DiMaio D. Platelet-derived growth factor receptor can mediate tumorigenic transformation by the bovine papillomavirus E5 protein. Molecular And Cellular Biology 1993, 13: 4137-4145. PMID: 8321218, PMCID: PMC359963, DOI: 10.1128/mcb.13.7.4137.Peer-Reviewed Original ResearchConceptsE5 proteinPDGF receptorPlatelet-derived growth factorBovine papillomavirus E5 proteinTumorigenic transformationMouse mammary gland cellsMurine mammary epithelial cell lineBovine papillomavirus type 1 E5 proteinPDGF receptor genesBPV E5 proteinMammary epithelial cell lineSustained proliferative signalEpidermal growth factor receptor (EGFR) pathwayPlatelet-derived growth factor receptorMammary gland cellsStable complexesGrowth factor receptor pathwayPDGF beta receptorTransforming proteinNMuMG cellsCellular proteinsGrowth factor receptorTyrosine phosphorylationEpithelial cell lineFibroblast transformation
1992
Stable association between the bovine papillomavirus E5 transforming protein and activated platelet-derived growth factor receptor in transformed mouse cells.
Petti L, DiMaio D. Stable association between the bovine papillomavirus E5 transforming protein and activated platelet-derived growth factor receptor in transformed mouse cells. Proceedings Of The National Academy Of Sciences Of The United States Of America 1992, 89: 6736-6740. PMID: 1323117, PMCID: PMC49578, DOI: 10.1073/pnas.89.15.6736.Peer-Reviewed Original ResearchConceptsE5 proteinPlatelet-derived growth factorGrowth factor receptor activationPDGF receptorMouse C127 cellsBovine papillomavirus E5Platelet-derived growth factor receptorShorter proteinTransforming proteinCoimmunoprecipitation analysisGrowth factor receptorReceptor transmitsStable associationC127 cellsTumorigenic transformationMouse cellsProteinBovine papillomavirusFactor receptorDistinct mechanismsStable complexesGrowth factorReceptor activationImportant targetBeta receptorsLocalization of bovine papillomavirus type 1 E5 protein to transformed basal keratinocytes and permissive differentiated cells in fibropapilloma tissue.
Burnett S, Jareborg N, DiMaio D. Localization of bovine papillomavirus type 1 E5 protein to transformed basal keratinocytes and permissive differentiated cells in fibropapilloma tissue. Proceedings Of The National Academy Of Sciences Of The United States Of America 1992, 89: 5665-5669. PMID: 1319069, PMCID: PMC49353, DOI: 10.1073/pnas.89.12.5665.Peer-Reviewed Original Research
1991
Tumorigenic transformation of murine keratinocytes by the E5 genes of bovine papillomavirus type 1 and human papillomavirus type 16
Leptak C, Cajal S, Kulke R, Horwitz B, Riese D, Dotto G, DiMaio D. Tumorigenic transformation of murine keratinocytes by the E5 genes of bovine papillomavirus type 1 and human papillomavirus type 16. Journal Of Virology 1991, 65: 7078-7083. PMID: 1658398, PMCID: PMC250837, DOI: 10.1128/jvi.65.12.7078-7083.1991.Peer-Reviewed Original ResearchConceptsBovine papillomavirus type 1E5 genePapillomavirus type 1Human Papillomavirus Type 16 E5 GeneTumorigenic transformationHost epithelial cellsExpression vectorRecombinant virusesRetroviral expression vectorMurine keratinocytesBiological propertiesTumorigenic cellsMurine epidermal keratinocytesGenesMurine fibroblastsFrameshift mutationCultured linesHuman papillomavirus type 16Cell linesEpithelial cellsPapillomavirus type 16Epidermal keratinocytesRetrovirusesCellsKeratinocytesBiological properties of the deer papillomavirus E5 gene in mouse C127 cells: growth transformation, induction of DNA synthesis, and activation of the platelet-derived growth factor receptor
Kulke R, DiMaio D. Biological properties of the deer papillomavirus E5 gene in mouse C127 cells: growth transformation, induction of DNA synthesis, and activation of the platelet-derived growth factor receptor. Journal Of Virology 1991, 65: 4943-4949. PMID: 1651413, PMCID: PMC248956, DOI: 10.1128/jvi.65.9.4943-4949.1991.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBlotting, NorthernCell Transformation, ViralCloning, MolecularDeerDNAGene ExpressionGenes, ViralIn Vitro TechniquesMiceMolecular Sequence DataOncogene Proteins, ViralPapillomaviridaePlatelet-Derived Growth FactorReceptors, Cell SurfaceReceptors, Platelet-Derived Growth FactorRNA, ViralViral Structural ProteinsConceptsMouse C127 cellsE5 proteinC127 cellsE5 genePlatelet-derived growth factor beta receptorPDGF receptorBovine papillomavirus type 1 E5 proteinConstitutive tyrosine phosphorylationDNA synthesisGrowth factor beta receptorBovine papillomavirus type 1Platelet-derived growth factor receptorTransformation of fibroblastsPapillomavirus type 1Sequence similarityGrowth factor receptorTyrosine phosphorylationBiological activityShort regionFoci formationProteinFactor receptorReceptor formsB chainGrowth transformation
1989
Open reading frames E6 and E7 of bovine papillomavirus type 1 are both required for full transformation of mouse C127 cells
Neary K, DiMaio D. Open reading frames E6 and E7 of bovine papillomavirus type 1 are both required for full transformation of mouse C127 cells. Journal Of Virology 1989, 63: 259-266. PMID: 2535732, PMCID: PMC247680, DOI: 10.1128/jvi.63.1.259-266.1989.Peer-Reviewed Original ResearchConceptsBovine papillomavirus type 1Open reading frames E6Mouse C127 cellsFull-length viral genomesAnchorage-independent growthPapillomavirus type 1Focus-forming activityC127 cellsORF E6First methionine codonViral genomeColony formationRetrovirus long terminal repeatsSeries of mutationsE6/E7Second ATG codonLong terminal repeatBPV1 genomeMethionine codonATG codonNumber plasmidE5 geneSpecific proteinsSimultaneous disruptionE6 protein