2019
Chapter Eight Illuminating the virus life cycle with single-molecule FRET imaging
Lu M, Ma X, Mothes W. Chapter Eight Illuminating the virus life cycle with single-molecule FRET imaging. Advances In Virus Research 2019, 105: 239-273. PMID: 31522706, PMCID: PMC7246055, DOI: 10.1016/bs.aivir.2019.07.004.Peer-Reviewed Original ResearchMeSH KeywordsEnv Gene Products, Human Immunodeficiency VirusFluorescence Resonance Energy TransferHIV-1Protein ConformationSingle Molecule ImagingVirus InternalizationConceptsVirus life cycleMolecular mechanismsViral proteinsSingle-molecule FRETBiological moleculesPrecise molecular mechanismsFörster resonance energy transfer (FRET) imagingLife cycleConformational dynamicsReal-time imagingEnergetics of transitionsNovel antiviral therapiesStructural intermediatesConformational changesConformational statesNative stateSmFRETRelevant conditionsElegant experimental designsAsymmetric intermediatesIntermediatesViral fusionViral glycoproteinsStructural methodsIntact virionsAssociating HIV-1 envelope glycoprotein structures with states on the virus observed by smFRET
Lu M, Ma X, Castillo-Menendez LR, Gorman J, Alsahafi N, Ermel U, Terry DS, Chambers M, Peng D, Zhang B, Zhou T, Reichard N, Wang K, Grover JR, Carman BP, Gardner MR, Nikić-Spiegel I, Sugawara A, Arthos J, Lemke EA, Smith AB, Farzan M, Abrams C, Munro JB, McDermott AB, Finzi A, Kwong PD, Blanchard SC, Sodroski JG, Mothes W. Associating HIV-1 envelope glycoprotein structures with states on the virus observed by smFRET. Nature 2019, 568: 415-419. PMID: 30971821, PMCID: PMC6655592, DOI: 10.1038/s41586-019-1101-y.Peer-Reviewed Original ResearchConceptsSingle-molecule fluorescence resonance energy transferCryo-electron microscopy studiesHigh-resolution structuresFluorescence resonance energy transferState 1 conformationProline substitutionConformational statesResonance energy transferDisulfide bondsCell entryIntermediate conformationsReceptor moleculesGlycoprotein structureStructural studiesIntact virionsViral EnvCD4 receptor moleculeIntact virusConformationState 2TrimerState 1
2018
HIV-1 Env trimer opens through an asymmetric intermediate in which individual protomers adopt distinct conformations
Ma X, Lu M, Gorman J, Terry DS, Hong X, Zhou Z, Zhao H, Altman RB, Arthos J, Blanchard SC, Kwong PD, Munro JB, Mothes W. HIV-1 Env trimer opens through an asymmetric intermediate in which individual protomers adopt distinct conformations. ELife 2018, 7: e34271. PMID: 29561264, PMCID: PMC5896952, DOI: 10.7554/elife.34271.Peer-Reviewed Original ResearchMeSH KeywordsCD4 AntigensEnv Gene Products, Human Immunodeficiency VirusFluorescence Resonance Energy TransferHIV AntibodiesHIV Envelope Protein gp120HIV-1HumansProtein BindingProtein ConformationProtein MultimerizationProtein SubunitsVirion
2014
Conformational dynamics of single HIV-1 envelope trimers on the surface of native virions
Munro JB, Gorman J, Ma X, Zhou Z, Arthos J, Burton DR, Koff WC, Courter JR, Smith AB, Kwong PD, Blanchard SC, Mothes W. Conformational dynamics of single HIV-1 envelope trimers on the surface of native virions. Science 2014, 346: 759-763. PMID: 25298114, PMCID: PMC4304640, DOI: 10.1126/science.1254426.Peer-Reviewed Original ResearchMeSH KeywordsAntibodies, NeutralizingCD4 AntigensFluorescence Resonance Energy TransferHIV Envelope Protein gp120HIV-1HumansImmune EvasionLigandsModels, ChemicalMolecular ImagingProtein MultimerizationProtein Structure, TertiaryVirion