2004
Vpx proteins of SIVmac239 and HIV-2ROD interact with the cytoskeletal protein α-actinin 1
Mueller S, Jung R, Weiler S, Lang S. Vpx proteins of SIVmac239 and HIV-2ROD interact with the cytoskeletal protein α-actinin 1. Journal Of General Virology 2004, 85: 3291-3303. PMID: 15483243, DOI: 10.1099/vir.0.80198-0.Peer-Reviewed Original ResearchMeSH KeywordsActininAmino Acid SequenceAnimalsBiological TransportChlorocebus aethiopsCOS CellsCytoplasmHIV-2Molecular Sequence DataProlineProtein Structure, TertiaryRetroviridae ProteinsSequence AlignmentSimian immunodeficiency virusTransfectionTwo-Hybrid System TechniquesViral Regulatory and Accessory ProteinsConceptsPre-integration complexNuclear localization signalNuclear importProline-rich C-terminal domainClassical import pathwayEfficient nuclear importTwo-hybrid screenAlpha-actinin 1Α-actinin 1C-terminal domainLoss of interactionImport pathwayLocalization signalCellular proteinsNuclear localizationSequence elementsCytoskeletal proteinsVpx geneVpx proteinsQuiescent cellsAA proteinViral proteinsProteinVirion particlesRed-capped mangabeys
2002
The First HxRxG Motif in Simian Immunodeficiency Virus mac239 Vpr Is Crucial for G2/M Cell Cycle Arrest
Mueller S, Lang S. The First HxRxG Motif in Simian Immunodeficiency Virus mac239 Vpr Is Crucial for G2/M Cell Cycle Arrest. Journal Of Virology 2002, 76: 11704-11709. PMID: 12388729, PMCID: PMC136740, DOI: 10.1128/jvi.76.22.11704-11709.2002.Peer-Reviewed Original ResearchConceptsCell cycle arrestCell cycle arrest functionCycle arrestArrest functionVpr mutantsAlpha-helical domainAlpha-helical regionG2/M cell cycle arrestLong terminal repeatM cell cycle arrestNuclear importArrest of cellsSIV long terminal repeatTranscriptional transactivationPreintegration complexSecond motifFunctional domainsReduced transactivationVpr proteinTerminal repeatAmino acidsTransactivationSingle substitutionMotifMutants
2000
Simian Immunodeficiency Virus Containing Mutations in N-Terminal Tyrosine Residues and in the PxxP Motif in Nef Replicates Efficiently in Rhesus Macaques
Carl S, Iafrate A, Lang S, Stolte N, Stahl-Hennig C, Mätz-Rensing K, Fuchs D, Skowronski J, Kirchhoff F. Simian Immunodeficiency Virus Containing Mutations in N-Terminal Tyrosine Residues and in the PxxP Motif in Nef Replicates Efficiently in Rhesus Macaques. Journal Of Virology 2000, 74: 4155-4164. PMID: 10756028, PMCID: PMC111930, DOI: 10.1128/jvi.74.9.4155-4164.2000.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBinding SitesCD4 AntigensCell Line, TransformedCOS CellsDown-RegulationGene Products, nefHistocompatibility Antigens Class IHumansMacaca mulattaMutagenesisP21-Activated KinasesPhosphorylationProtein Serine-Threonine KinasesSimian immunodeficiency virusSrc Homology DomainsTyrosineViral LoadVirus ReplicationConceptsAbility of NefTyrosine-based endocytosis signalTyrosine residuesHigh viral loadCellular signal transductionTyrosine kinase SrcNef functionViral loadEndocytosis signalEndocytic machineryPXXP motifN-terminal tyrosine residueCell surface expressionKinase SrcKinase assaysSignal transductionProline residuesClass I major histocompatibility complexN-terminal tyrosineI major histocompatibility complexLigand domainCombined mutationsNef interactionsMajor histocompatibility complexMutations
1999
The Acidic Region and Conserved Putative Protein Kinase C Phosphorylation Site in Nef Are Important for SIV Replication in Rhesus Macaques
Carl S, Iafrate A, Lang S, Stahl-Hennig C, Kuhn E, Fuchs D, Mätz-Rensing K, Haaft P, Heeney J, Skowronski J, Kirchhoff F. The Acidic Region and Conserved Putative Protein Kinase C Phosphorylation Site in Nef Are Important for SIV Replication in Rhesus Macaques. Virology 1999, 257: 138-155. PMID: 10208928, DOI: 10.1006/viro.1999.9645.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsCD4 AntigensCOS CellsGene Products, nefHistocompatibility Antigens Class IHIV-1Hydrogen-Ion ConcentrationMacaca mulattaMolecular Sequence DataMutagenesis, Site-DirectedNef Gene Products, Human Immunodeficiency VirusPhosphorylationProtein Kinase CSimian immunodeficiency virusSurface PropertiesVirus ReplicationConceptsProtein kinase C phosphorylation sitesKinase C phosphorylation sitesC phosphorylation sitesPhosphorylation sitesPutative protein kinase C phosphorylation sitePotential protein kinase C phosphorylation sitesAcidic regionWild-type activityPKC phosphorylation sitesJurkat T cellsSignal transductionAbility of NefReplication assaysFunctional relevanceCell culture systemMutant virusNef functionPathogenic SIVmac239 cloneAcidic chargeReduced infectivityReplicationCulture systemNefRapid reversionRhesus macaques
1997
Association of simian immunodeficiency virus Nef with cellular serine/threonine kinases is dispensable for the development of AIDS in rhesus macaques
Lang S, Lafrate A, Stahl-Hennig C, Kuhn E, Nisslein T, Kaup F, Haupt M, Hunsmann G, Skowronski J, Kirchhoff F. Association of simian immunodeficiency virus Nef with cellular serine/threonine kinases is dispensable for the development of AIDS in rhesus macaques. Nature Medicine 1997, 3: 860-865. PMID: 9256276, DOI: 10.1038/nm0897-860.Peer-Reviewed Original ResearchConceptsCellular serine/threonine kinaseSerine/threonine kinaseThreonine kinaseTyrosine kinase SrcPutative SH3Simian immunodeficiency virus NefKinase SrcMutant formsEfficient replicationKinaseInduction of AIDSSimian immunodeficiency virusNef geneCD4 downregulationSIVmac NefRhesus macaquesRapid deathNef sequencesSH3NefSrcGenesDomainDifferent time pointsPathogenicity