2024
Design of soluble HIV-1 envelope trimers free of covalent gp120-gp41 bonds with prevalent native-like conformation
Zhang P, Gorman J, Tsybovsky Y, Lu M, Liu Q, Gopan V, Singh M, Lin Y, Miao H, Seo Y, Kwon A, Olia A, Chuang G, Geng H, Lai Y, Zhou T, Mascola J, Mothes W, Kwong P, Lusso P. Design of soluble HIV-1 envelope trimers free of covalent gp120-gp41 bonds with prevalent native-like conformation. Cell Reports 2024, 43: 114518. PMID: 39028623, PMCID: PMC11459465, DOI: 10.1016/j.celrep.2024.114518.Peer-Reviewed Original Research
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 ResearchConceptsVirus 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 Research
2015
Crystal structure, conformational fixation and entry-related interactions of mature ligand-free HIV-1 Env
Do Kwon Y, Pancera M, Acharya P, Georgiev I, Crooks E, Gorman J, Joyce M, Guttman M, Ma X, Narpala S, Soto C, Terry D, Yang Y, Zhou T, Ahlsen G, Bailer R, Chambers M, Chuang G, Doria-Rose N, Druz A, Hallen M, Harned A, Kirys T, Louder M, O'Dell S, Ofek G, Osawa K, Prabhakaran M, Sastry M, Stewart-Jones G, Stuckey J, Thomas P, Tittley T, Williams C, Zhang B, Zhao H, Zhou Z, Donald B, Lee L, Zolla-Pazner S, Baxa U, Schön A, Freire E, Shapiro L, Lee K, Arthos J, Munro J, Blanchard S, Mothes W, Binley J, McDermott A, Mascola J, Kwong P. Crystal structure, conformational fixation and entry-related interactions of mature ligand-free HIV-1 Env. Nature Structural & Molecular Biology 2015, 22: 522-531. PMID: 26098315, PMCID: PMC4706170, DOI: 10.1038/nsmb.3051.Peer-Reviewed Original Research
2000
Retroviral Entry Mediated by Receptor Priming and Low pH Triggering of an Envelope Glycoprotein
Mothes W, Boerger A, Narayan S, Cunningham J, Young J. Retroviral Entry Mediated by Receptor Priming and Low pH Triggering of an Envelope Glycoprotein. Cell 2000, 103: 679-689. PMID: 11106737, DOI: 10.1016/s0092-8674(00)00170-7.Peer-Reviewed Original Research