2000
Rabies virus entry at the neuromuscular junction in nerve–muscle cocultures
Lewis P, Fu Y, Lentz T. Rabies virus entry at the neuromuscular junction in nerve–muscle cocultures. Muscle & Nerve 2000, 23: 720-730. PMID: 10797395, DOI: 10.1002/(sici)1097-4598(200005)23:5<720::aid-mus9>3.0.co;2-5.Peer-Reviewed Original ResearchConceptsNerve cell bodiesRabies virus entryNerve-muscle coculturesNerve terminalsNerve fibersNeuromuscular junctionRabies virusCell bodiesVirus entryMotor nerve terminalsNerve-muscle contactsNicotinic acetylcholine receptorsVirus adsorption periodAcetylcholine receptorsLucifer YellowSynapsin ISynaptic vesiclesRetrograde transportVirusProgressive increaseEarly eventsCocultureSurface of cellsMyotube surfaceNeurons
1998
Rabies Virus Entry into Endosomes in IMR-32 Human Neuroblastoma Cells
Lewis P, Fu Y, Lentz T. Rabies Virus Entry into Endosomes in IMR-32 Human Neuroblastoma Cells. Experimental Neurology 1998, 153: 65-73. PMID: 9743568, DOI: 10.1006/exnr.1998.6879.Peer-Reviewed Original ResearchConceptsIMR-32 human neuroblastoma cellsRabies virus entryHuman neuroblastoma cellsRabies virusNeuroblastoma cellsNerve terminalsCell bodiesVirus entryIMR-32 neuroblastoma cellsSynaptic vesicle markersLucifer YellowCell surfaceSynapsin ITransferrin receptorVirusTexas Red dextranEarly eventsVesicle markersVirus particlesImmunofluorescence microscopyRabies virus entry into cultured rat hippo campalneurons
Lewis P, Lentz T. Rabies virus entry into cultured rat hippo campalneurons. Brain Cell Biology 1998, 27: 559-573. PMID: 10405023, DOI: 10.1023/a:1006912610044.Peer-Reviewed Original ResearchConceptsRabies virus entryCultured hippocampal neuronsViral antigensHippocampal neuronsRabies virusVirus entryRabies virus infectionSynaptic vesicle markersAxon terminalsNerve terminalsVirus infectionLysosomotropic agent chloroquineSomatodendritic domainCell bodiesVirus-containing endosomesLucifer YellowNeuronsSynapsin IInfectionAntigenTransferrin receptorVirusWheat germ agglutininAgent chloroquineVesicle markers
1997
Rabies virus infection of IMR-32 human neuroblastoma cells and effect of neurochemical and other agents
Lentz T, Fu Y, Lewis P. Rabies virus infection of IMR-32 human neuroblastoma cells and effect of neurochemical and other agents. Antiviral Research 1997, 35: 29-39. PMID: 9224959, DOI: 10.1016/s0166-3542(97)01036-x.Peer-Reviewed Original ResearchConceptsIMR-32 human neuroblastoma cellsIMR-32 cellsHuman neuroblastoma cellsNeuroblastoma cellsNeuronal nicotinic acetylcholine receptorsCentral nervous system receptorsRabies virusRabies virus infectionLysosomotropic agentsReceptor alpha1 subunitNicotinic acetylcholine receptorsNerve cell lineAttachment of virusNeurotropic virusesCholinergic agonistsViral antigensVirus infectionHuman neuronsAcetylcholine receptorsSynthetic peptidesCell bodiesInfectionAlpha1 subunitCholinergic ligandsBinding receptors
1996
Rabies virus binding to the nicotinic acetylcholine receptor α subunit demonstrated by virus overlay protein binding assay
Gastka M, Horvath J, Lentz T. Rabies virus binding to the nicotinic acetylcholine receptor α subunit demonstrated by virus overlay protein binding assay. Journal Of General Virology 1996, 77: 2437-2440. PMID: 8887475, DOI: 10.1099/0022-1317-77-10-2437.Peer-Reviewed Original ResearchConceptsAlpha subunitNicotinic acetylcholine receptor α subunitAcetylcholine receptor α subunitElectric organ membranesVirus overlay proteinVirus overlay protein binding assaysTransfer of proteinsReceptor α subunitProtein binding assaysAChR alpha subunitOverlay proteinRabies virusΑ-subunitSubunitsGel electrophoresisAcetylcholine receptorsBinding assaysCuraremimetic neurotoxinsProteinMembraneVirusBindingAChRBlot
1991
Structure-function relationships of curaremimetic neurotoxin loop 2 and of a structurally similar segment of rabies virus glycoprotein in their interaction with the nicotinic acetylcholine receptor.
Lentz T. Structure-function relationships of curaremimetic neurotoxin loop 2 and of a structurally similar segment of rabies virus glycoprotein in their interaction with the nicotinic acetylcholine receptor. Biochemistry 1991, 30: 10949-57. PMID: 1932020, DOI: 10.1021/bi00109a020.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBinding, CompetitiveCell MembraneElapid VenomsElectric OrganGlycoproteinsKineticsMacromolecular SubstancesModels, StructuralMolecular Sequence DataNeurotoxinsPeptidesProtein ConformationRabies virusReceptors, NicotinicSequence Homology, Nucleic AcidTorpedoTubocurarineViral ProteinsConceptsRabies virus glycoproteinAcetylcholine receptorsVirus glycoproteinNicotinic acetylcholine receptorsTorpedo electric organ membranesElectric organ membranesD-tubocurarineToxin BReceptorsLoop 2Synthetic peptidesGlycoproteinPeptidesHigh affinityStructure-function relationshipsPhe-33GroupAcetylcholineStructural and conformational similarity between synthetic peptides of curaremimetic neurotoxins and rabies virus glycoprotein
Donnelly-Roberts D, Lentz T. Structural and conformational similarity between synthetic peptides of curaremimetic neurotoxins and rabies virus glycoprotein. Brain Research 1991, 11: 107-113. PMID: 1661807, DOI: 10.1016/0169-328x(91)90112-b.Peer-Reviewed Original ResearchConceptsLoop 2Virus glycoproteinAcetylcholine receptorsRabies virus glycoproteinBeta-sheet structureCircular dichroism spectroscopyCuraremimetic neurotoxinsAcetylcholine-binding siteSynthetic peptidesNicotinic acetylcholine receptorsDichroism spectroscopyStructural similarityConformational similarityCorresponding peptidesPolyclonal antibodiesGlycoproteinPeptides
1990
Rabies virus binding to an acetylcholine receptor α‐subunit peptide
Lentz T. Rabies virus binding to an acetylcholine receptor α‐subunit peptide. Journal Of Molecular Recognition 1990, 3: 82-88. PMID: 2361061, DOI: 10.1002/jmr.300030205.Peer-Reviewed Original ResearchConceptsNicotinic acetylcholine receptorsAcetylcholine receptorsRabies virusNeuronal nicotinic acetylcholine receptorsUseful antiviral agentsReceptor peptideBinding of virusAcetylcholine receptor αSynthetic peptidesHost cell receptorsRabies virus glycoproteinAttachment of virusViral attachment proteinAntiviral agentsAlpha 1 peptideReceptor αNeurotoxin bindsSynthetic peptide comprisingAlpha-subunit peptidesCell receptorCuraremimetic neurotoxinsReceptorsVirusSnake venomVirus glycoproteinRabies susceptibility and acetylcholine receptor
Baer G, Shaddock J, Quirion R, Dam T, Lentz T. Rabies susceptibility and acetylcholine receptor. The Lancet 1990, 335: 664-665. PMID: 1969042, DOI: 10.1016/0140-6736(90)90454-d.Peer-Reviewed Original Research
1989
Synthetic peptides of neurotoxins and rabies virus glycoprotein behave as antagonists in a functional assay for the acetylcholine receptor.
Donnelly-Roberts D, Lentz T. Synthetic peptides of neurotoxins and rabies virus glycoprotein behave as antagonists in a functional assay for the acetylcholine receptor. Chemical Biology & Drug Design 1989, 2: 221-6. PMID: 2520759.Peer-Reviewed Original ResearchConceptsLoop 2Acetylcholine receptorsLarge macromolecular complexesVirus glycoproteinCompetitive antagonist d-tubocurarineRabies virus glycoproteinSegment interactsMacromolecular complexesSynthetic peptidesNicotinic acetylcholine receptorsBC3H-1 cellsLarge moleculesFunctional assaysShort synthetic peptidesMicromolar rangeIon transportAntagonist d-tubocurarineEffective peptideBiological effectsIC50 valuesPeptidesReceptorsGlycoproteinNeurotoxinGlycoprotein peptide
1988
Synthetic peptides in the study of the interaction of rabies virus and the acetylcholine receptor.
Lentz T, Hawrot E, Donnelly-Roberts D, Wilson P. Synthetic peptides in the study of the interaction of rabies virus and the acetylcholine receptor. Advances In Biochemical Psychopharmacology 1988, 44: 57-71. PMID: 3041753.Peer-Reviewed Original ResearchConceptsSnake venom neurotoxinsAmino acid sequence similarityCentral nervous systemAcetylcholine receptorsVirus glycoproteinVenom neurotoxinsPeriod of replicationRabies virus glycoproteinRegions of virusesNervous systemGenetic driftSequence similarityVirus-receptor interactionsMolecular basisRabies virusCertain neuronal populationsDirect bindingRNA virusesNicotinic acetylcholine receptorsCell surface constituentsBlood-brain barrierCell receptorGlycoproteinBindingD-tubocurarine
1987
Synthetic peptides corresponding to sequences of snake venom neurotoxins and rabies virus glycoprotein bind to the nicotinic acetylcholine receptor
Lentz T, Hawrot E, Wilson P. Synthetic peptides corresponding to sequences of snake venom neurotoxins and rabies virus glycoprotein bind to the nicotinic acetylcholine receptor. Proteins Structure Function And Bioinformatics 1987, 2: 298-307. PMID: 3448605, DOI: 10.1002/prot.340020406.Peer-Reviewed Original ResearchConceptsLoop 2Alpha-bungarotoxin bindingAcetylcholine receptorsProtein-protein interactionsElectric organ acetylcholine receptorAlpha-subunit peptidesApparent affinityVirus glycoproteinCompetitive antagonist d-tubocurarineRabies virus glycoproteinSynthetic peptidesSnake venom neurotoxinsViral homologsAlpha subunitNative proteinNicotinic acetylcholine receptorsGlycoprotein actsGlu residuesIntact subunitVenom neurotoxinsHydrophobic subsitePosition 173Recognition sitesAntagonist d-tubocurarineArg37
1986
Binding of rabies virus to purified Torpedo acetylcholine receptor.
Lentz T, Benson R, Klimowicz D, Wilson P, Hawrot E. Binding of rabies virus to purified Torpedo acetylcholine receptor. Brain Research 1986, 387: 211-9. PMID: 3828757, DOI: 10.1016/0169-328x(86)90027-6.Peer-Reviewed Original ResearchConceptsAcetylcholine receptorsRabies virusRabies virus receptorTorpedo acetylcholine receptorReceptor concentrationNeurotransmitter receptorsVirus receptorTorpedo electric organReceptorsVirusIncubation mediumVirus interactionsVirus particlesVirus concentrationDirect bindingElectric organAtropineAcetylcholineAChR
1985
Rabies virus binding to cellular membranes measured by enzyme immunoassay
Lentz T, Chester J, Benson R, Hawrot E, Tignor G, Smith A. Rabies virus binding to cellular membranes measured by enzyme immunoassay. Muscle & Nerve 1985, 8: 336-345. PMID: 16758601, DOI: 10.1002/mus.880080411.Peer-Reviewed Original ResearchMeSH KeywordsAcetylcholinesteraseAnimalsAntibodiesBinding Sites, AntibodyBinding, CompetitiveCationsCell MembraneChick EmbryoCricetinaeDogsEmbryo, MammalianEnzyme-Linked Immunosorbent AssayGuinea PigsHumansHydrogen-Ion ConcentrationMiceMuscle Fibers, SkeletalNeuroblastomaPropiolactoneRabies virusRatsReceptors, CholinergicTemperatureTrypsinConceptsEnzyme-linked immunosorbent assayRabies virusAcetylcholine receptor contentTreatment of virusRabies virus antibodiesMost parenchymal organsReceptor contentSalivary gland membranesVirus antibodiesAcetylcholine receptorsParenchymal organsEnzyme immunoassayImmunosorbent assaySimilar developmental changesEmbryonic chick myotubesGland membranesSurface moleculesVirusMyotube membranesAntibodiesSecond antibodyInactivation of virusesChick myotubesDevelopmental changesLow levels
1984
Amino Acid Sequence Similarity Between Rabies Virus Glycoprotein and Snake Venom Curaremimetic Neurotoxins
Lentz T, Wilson P, Hawrot E, Speicher D. Amino Acid Sequence Similarity Between Rabies Virus Glycoprotein and Snake Venom Curaremimetic Neurotoxins. Science 1984, 226: 847-848. PMID: 6494916, DOI: 10.1126/science.6494916.Peer-Reviewed Original ResearchConceptsAmino acid sequence similarityAcetylcholine receptorsNeurotropic rabies virusVirus glycoproteinRabies virus glycoproteinCuraremimetic neurotoxinsHost cell receptorsSequence similarityGreater identityDirect bindingLong neurotoxinsRabies virusReceptor-binding regionRecognition sitesViral glycoproteinsGlycoproteinEntire sequenceNeurotoxinReceptors
1983
The acetylcholine receptor as a cellular receptor for rabies virus.
Lentz T, Burrage T, Smith A, Tignor G. The acetylcholine receptor as a cellular receptor for rabies virus. The Yale Journal Of Biology And Medicine 1983, 56: 315-22. PMID: 6367238, PMCID: PMC2589619.Peer-Reviewed Original ResearchConceptsAcetylcholine receptorsHost cell receptorsRabies virusSpecific host cell receptorsCell receptorTissue tropismMotor nerve endingsRabies virus pathogenesisMyasthenia gravisAutoimmune diseasesCultured muscle cellsNerve endingsTranssynaptic transferViral antigensViral immunizationVirus pathogenesisDisease processNeurotransmitter receptorsViral infectionIntact hostCellular tropismNeuromuscular junctionInfected animalsMuscle cellsVirus attachment
1982
Is the Acetylcholine Receptor a Rabies Virus Receptor?
Lentz T, Burrage T, Smith A, Crick J, Tignor G. Is the Acetylcholine Receptor a Rabies Virus Receptor? Science 1982, 215: 182-184. PMID: 7053569, DOI: 10.1126/science.7053569.Peer-Reviewed Original Research