{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,4]],"date-time":"2026-08-04T12:47:54Z","timestamp":1785847674488,"version":"3.56.0"},"reference-count":60,"publisher":"American Chemical Society (ACS)","issue":"15","license":[{"start":{"date-parts":[[2026,7,22]],"date-time":"2026-07-22T00:00:00Z","timestamp":1784678400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100007165","name":"University of Missouri","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100007165","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000015","name":"U.S. Department of Energy","doi-asserted-by":"publisher","award":["KP1607011"],"award-info":[{"award-number":["KP1607011"]}],"id":[{"id":"10.13039\/100000015","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["1S10OD026703"],"award-info":[{"award-number":["1S10OD026703"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000057","name":"National Institute of General Medical Sciences","doi-asserted-by":"publisher","award":["P30GM133893"],"award-info":[{"award-number":["P30GM133893"]}],"id":[{"id":"10.13039\/100000057","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2026,8,4]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Fusion of the host membrane and viral envelope by class I viral fusion proteins is driven by the assembly of a postfusion six-helix bundle formed through antiparallel interactions between N-terminal (HR1) and C-terminal (HR2) heptad-repeat regions. Although mutations in these regions of the measles virus (MeV) fusion (F) glycoprotein are known to promote neuropathogenic and hyperfusogenic phenotypes, their effects on postfusion core stability have not been systematically examined. Here, we combine peptide biophysics and X-ray crystallography to interrogate how mutations within the HR2 domain, present in native neuropathogenic MeV isolates (e.g., L454W and N462K) and laboratory-generated hyperfusogenic variants (e.g., L454M and T461A), influence postfusion 6HB assembly. Circular dichroism (CD) spectroscopy reveals that, with few exceptions, these mutations decrease postfusion core stability, despite their association with enhanced fusion activity. We also report the first crystal structure of the wild-type MeV postfusion core as well as structures of six hyperfusogenic variants, enabling high-resolution comparison of the molecular basis of destabilization. Structural analysis shows that these effects arise from localized perturbations to steric packing, hydrogen bonding networks, and helix-stabilizing interactions within HR2, while the overall 6HB architecture remains conserved. Together, these results indicate that hyperfusogenic mutations are not associated with stabilization of the postfusion state and are instead consistent with models in which hyperfusogenicity arises from a reduction in the energetic barrier to fusion, potentially through effects on prefusion stability or triggering efficiency. These findings establish key sequence-structure\u2013stability relationships governing coiled-coil assembly and provide a framework for the design of HR1- and HR2-based fusion inhibitors.<\/jats:p>","DOI":"10.1021\/acs.biochem.6c00182","type":"journal-article","created":{"date-parts":[[2026,7,22]],"date-time":"2026-07-22T17:31:10Z","timestamp":1784741470000},"page":"2350-2358","source":"Crossref","is-referenced-by-count":0,"title":["Hyperfusogenic\nMutations Destabilize the Postfusion\nSix-Helix Bundle of the Measles Virus Fusion Glycoprotein"],"prefix":"10.1021","volume":"65","author":[{"given":"Nisansala","family":"Vithanage","sequence":"first","affiliation":[{"name":"University of Missouri , , , ,","place":["Columbia, Missouri, United States, 65211"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-7054-4204","authenticated-orcid":true,"given":"Victor K.","family":"Outlaw","sequence":"additional","affiliation":[{"name":"University of Missouri , , , ,","place":["Columbia, Missouri, United States, 65211"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"316","published-online":{"date-parts":[[2026,7,22]]},"reference":[{"key":"2026080408072767400_cit1","doi-asserted-by":"publisher","first-page":"231","DOI":"10.1016\/S0065-3527(05)64007-9","article-title":"Mechanism\nof Membrane Fusion by Viral Envelope Proteins","volume":"64","author":"Harrison","year":"2005","journal-title":"Adv. Virus Res."},{"issue":"3","key":"2026080408072767400_cit2","doi-asserted-by":"publisher","first-page":"189","DOI":"10.1080\/10409230802058320","article-title":"Structures\nand Mechanisms of Viral Membrane Fusion Proteins: Multiple Variations\non a Common Theme","volume":"43","author":"White","year":"2008","journal-title":"Crit. Rev. Biochem. Mol.\nBiol."},{"issue":"1","key":"2026080408072767400_cit3","doi-asserted-by":"publisher","first-page":"777","DOI":"10.1146\/annurev.biochem.70.1.777","article-title":"Mechanisms of Viral\nMembrane Fusion and Its Inhibition","volume":"70","author":"Eckert","year":"2001","journal-title":"Annu. Rev.\nBiochem."},{"issue":"4","key":"2026080408072767400_cit4","doi-asserted-by":"publisher","first-page":"613","DOI":"10.3390\/v4040613","article-title":"Paramyxovirus Fusion\nand Entry: Multiple Paths to a\nCommon End","volume":"4","author":"Chang","year":"2012","journal-title":"Viruses"},{"key":"2026080408072767400_cit5","doi-asserted-by":"publisher","first-page":"24","DOI":"10.1016\/j.coviro.2014.01.005","article-title":"Activation of Paramyxovirus Membrane Fusion and Virus\nEntry","volume":"5","author":"Jardetzky","year":"2014","journal-title":"Curr. Opin. Virol."},{"issue":"26","key":"2026080408072767400_cit6","doi-asserted-by":"publisher","first-page":"9288","DOI":"10.1073\/pnas.0503989102","article-title":"Structure\nof the Uncleaved Ectodomain of the Paramyxovirus (HPIV3) Fusion Protein","volume":"102","author":"Yin","year":"2005","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"issue":"3","key":"2026080408072767400_cit7","doi-asserted-by":"publisher","first-page":"142","DOI":"10.1007\/s40588-016-0040-8","article-title":"Paramyxovirus\nGlycoproteins\nand the Membrane Fusion Process","volume":"3","author":"Aguilar","year":"2016","journal-title":"Curr. Clin.\nMicrobiol. Rep."},{"key":"2026080408072767400_cit8","doi-asserted-by":"publisher","first-page":"309","DOI":"10.1016\/S1097-2765(00)80458-X","article-title":"Structural\nbasis for paramyxovirus-mediated membrane fusion","volume":"3","author":"Baker","year":"1999","journal-title":"Mol. Cell"},{"key":"2026080408072767400_cit9","doi-asserted-by":"publisher","first-page":"413","DOI":"10.1083\/jcb.151.2.413","article-title":"Evidence\nthat the transition of HIV-1\ngp41 into a six-helix bundle, not the bundle configuration, induces\nmembrane fusion","volume":"151","author":"Melikyan","year":"2000","journal-title":"J. Cell Biol."},{"issue":"4","key":"2026080408072767400_cit10","doi-asserted-by":"publisher","first-page":"112","DOI":"10.3390\/v8040112","article-title":"Measles Virus\nFusion\nProtein: Structure, Function and Inhibition","volume":"8","author":"Plattet","year":"2016","journal-title":"Viruses"},{"issue":"44","key":"2026080408072767400_cit11","doi-asserted-by":"publisher","first-page":"E3018","DOI":"10.1073\/pnas.1210925109","article-title":"Triggering the Measles\nVirus Membrane Fusion Machinery","volume":"109","author":"Brindley","year":"2012","journal-title":"Proc. Natl.\nAcad. Sci. U.S.A."},{"key":"2026080408072767400_cit12","doi-asserted-by":"publisher","first-page":"59","DOI":"10.1007\/978-3-540-70523-9_4","article-title":"Measles Virus Glycoprotein Complex\nAssembly, Receptor Attachment, and Cell Entry","volume":"329","author":"Navaratnarajah","year":"2009","journal-title":"Curr. Top. Microbiol. Immunol."},{"key":"2026080408072767400_cit13","doi-asserted-by":"publisher","first-page":"893","DOI":"10.1038\/35022579","article-title":"SLAM (CDw150) is a cellular receptor\nfor measles virus","volume":"406","author":"Tatsuo","year":"2000","journal-title":"Nature"},{"issue":"11","key":"2026080408072767400_cit14","doi-asserted-by":"publisher","DOI":"10.1371\/journal.ppat.0030178","article-title":"Predominant\nInfection of CD150+ Lymphocytes and Dendritic Cells during Measles\nVirus Infection of Macaques","volume":"3","author":"de Swart","year":"2007","journal-title":"PLoS Pathog."},{"key":"2026080408072767400_cit15","doi-asserted-by":"publisher","first-page":"530","DOI":"10.1038\/nature10639","article-title":"Adherens junction protein nectin-4\nis the epithelial receptor for measles virus","volume":"480","author":"Mu\u0308hlebach","year":"2011","journal-title":"Nature"},{"key":"2026080408072767400_cit16","doi-asserted-by":"publisher","DOI":"10.1371\/journal.ppat.1002240","article-title":"Tumor cell\nmarker PVRL4 (nectin 4)\nis an epithelial cell receptor for measles virus","volume":"7","author":"Noyce","year":"2011","journal-title":"PLoS Pathog."},{"issue":"15","key":"2026080408072767400_cit17","doi-asserted-by":"publisher","first-page":"6808","DOI":"10.1128\/JVI.00266-16","article-title":"Cell-To-Cell\nContact and Nectin-4 Govern Spread of Measles Virus from Primary Human\nMyeloid Cells to Primary Human Airway Epithelial Cells","volume":"90","author":"Singh","year":"2016","journal-title":"J. Virol."},{"issue":"5","key":"2026080408072767400_cit18","doi-asserted-by":"publisher","first-page":"897","DOI":"10.1016\/S0006-291X(02)02761-4","article-title":"The Fusion\nProtein Core of Measles Virus Forms Stable Coiled-Coil Trimer","volume":"299","author":"Zhu","year":"2002","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"2026080408072767400_cit19","doi-asserted-by":"publisher","first-page":"2186","DOI":"10.1073\/pnas.93.5.2186","article-title":"Peptides from\nconserved regions of\nparamyxovirus fusion (F) proteins are potent inhibitors of viral fusion","volume":"93","author":"Lambert","year":"1996","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2026080408072767400_cit20","doi-asserted-by":"publisher","first-page":"107","DOI":"10.1099\/0022-1317-78-1-107","article-title":"Inhibition of measles virus infection and fusion with\npeptides corresponding to the leucine zipper region of the fusion\nprotein","volume":"78","author":"Wild","year":"1997","journal-title":"J. Gen. Virol."},{"key":"2026080408072767400_cit21","doi-asserted-by":"publisher","first-page":"13785","DOI":"10.1128\/JVI.02436-13","article-title":"Fatal measles virus\ninfection prevented\nby brain-penetrant fusion inhibitors","volume":"87","author":"Welsch","year":"2013","journal-title":"J. Virol."},{"key":"2026080408072767400_cit22","doi-asserted-by":"publisher","first-page":"1143","DOI":"10.1128\/JVI.02417-14","article-title":"Prevention of measles virus infection\nby intranasal\ndelivery of fusion inhibitor peptides","volume":"89","author":"Mathieu","year":"2015","journal-title":"J. Virol."},{"key":"2026080408072767400_cit23","doi-asserted-by":"publisher","DOI":"10.1128\/jvi.01554-16","article-title":"In Vivo Efficacy of\nMeasles Virus Fusion Protein-Derived\nPeptides Is Modulated by the Properties of Self-Assembly and Membrane\nResidence","volume":"91","author":"Figueira","year":"2017","journal-title":"J. Virol."},{"key":"2026080408072767400_cit24","doi-asserted-by":"publisher","first-page":"12794","DOI":"10.1021\/acsnano.1c02057","article-title":"Inhibition\nof Measles Viral Fusion Is Enhanced by Targeting Multiple Domains\nof the Fusion Protein","volume":"15","author":"Bovier","year":"2021","journal-title":"ACS Nano"},{"issue":"8","key":"2026080408072767400_cit25","doi-asserted-by":"publisher","DOI":"10.1128\/jvi.01862-18","article-title":"Measles Virus\nBearing Measles Inclusion Body Encephalitis-Derived Fusion Protein\nIs Pathogenic after Infection via the Respiratory Route","volume":"93","author":"Mathieu","year":"2019","journal-title":"J. Virol."},{"issue":"3","key":"2026080408072767400_cit26","doi-asserted-by":"publisher","DOI":"10.1128\/mbio.00799-21","article-title":"Molecular Features\nof the Measles Virus Viral Fusion Complex That Favor Infection and\nSpread in the Brain","volume":"12","author":"Mathieu","year":"2021","journal-title":"mBio"},{"issue":"4","key":"2026080408072767400_cit27","doi-asserted-by":"publisher","first-page":"605","DOI":"10.3390\/v13040605","article-title":"Mutated Measles Virus Matrix and Fusion Protein Influence\nViral Titer in Vitro and Neuro-Invasion in Lewis Rat Brain Slice Cultures","volume":"13","author":"Busch","year":"2021","journal-title":"Viruses"},{"issue":"1","key":"2026080408072767400_cit28","doi-asserted-by":"publisher","DOI":"10.1128\/mbio.02528-14","article-title":"Measles Fusion\nMachinery Is Dysregulated\nin Neuropathogenic Variants","volume":"6","author":"Jurgens","year":"2015","journal-title":"mBio"},{"issue":"18","key":"2026080408072767400_cit29","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.2026027118","article-title":"Fitness Selection of\nHyperfusogenic\nMeasles Virus F Proteins Associated with Neuropathogenic Phenotypes","volume":"118","author":"Ikegame","year":"2021","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"issue":"21","key":"2026080408072767400_cit30","doi-asserted-by":"publisher","first-page":"11189","DOI":"10.1128\/jvi.01075-10","article-title":"The F Gene of the Osaka-2 Strain\nof Measles Virus Derived from a\nCase of Subacute Sclerosing Panencephalitis Is a Major Determinant\nof Neurovirulence","volume":"84","author":"Ayata","year":"2010","journal-title":"J. Virol."},{"issue":"5","key":"2026080408072767400_cit31","doi-asserted-by":"publisher","first-page":"2648","DOI":"10.1128\/JVI.02632-12","article-title":"Mutant Fusion Proteins with Enhanced\nFusion Activity\nPromote Measles Virus Spread in Human Neuronal Cells and Brains of\nSuckling Hamsters","volume":"87","author":"Watanabe","year":"2013","journal-title":"J. Virol."},{"issue":"2","key":"2026080408072767400_cit32","doi-asserted-by":"publisher","first-page":"164","DOI":"10.1016\/j.tim.2018.08.010","article-title":"New Insights\ninto Measles Virus Brain Infections","volume":"27","author":"Watanabe","year":"2019","journal-title":"Trends\nMicrobiol."},{"issue":"11","key":"2026080408072767400_cit33","doi-asserted-by":"publisher","first-page":"1017","DOI":"10.3390\/v11111017","article-title":"Measles Encephalitis:\nTowards New\nTherapeutics","volume":"11","author":"Ferren","year":"2019","journal-title":"Viruses"},{"issue":"4","key":"2026080408072767400_cit34","doi-asserted-by":"publisher","DOI":"10.1126\/sciadv.adf3731","article-title":"Collective Fusion Activity Determines\nNeurotropism of an En Bloc Transmitted Enveloped Virus","volume":"9","author":"Shirogane","year":"2023","journal-title":"Sci. Adv."},{"issue":"1","key":"2026080408072767400_cit35","doi-asserted-by":"publisher","DOI":"10.1128\/jvi.01750-24","article-title":"The Measles Virus Matrix\nF50S Mutation from a Lethal Case of Subacute Sclerosing Panencephalitis\nPromotes Receptor-Independent Neuronal Spread","volume":"99","author":"Yousaf","year":"2024","journal-title":"J. Virol."},{"issue":"12","key":"2026080408072767400_cit36","doi-asserted-by":"publisher","DOI":"10.1371\/journal.ppat.1011817","article-title":"Brain Tropism\nAcquisition: The Spatial Dynamics and Evolution of a Measles Virus\nCollective Infectious Unit That Drove Lethal Subacute Sclerosing Panencephalitis","volume":"19","author":"Yousaf","year":"2023","journal-title":"PLoS Pathog."},{"issue":"5","key":"2026080408072767400_cit37","doi-asserted-by":"publisher","first-page":"2710","DOI":"10.1128\/JVI.03346-14","article-title":"Measles Virus Mutants Possessing\nthe Fusion Protein\nwith Enhanced Fusion Activity Spread Effectively in Neuronal Cells,\nbut Not in Other Cells, without Causing Strong Cytopathology","volume":"89","author":"Watanabe","year":"2014","journal-title":"J. Virol."},{"issue":"7","key":"2026080408072767400_cit38","doi-asserted-by":"publisher","first-page":"1627","DOI":"10.1021\/acschembio.5c00208","article-title":"SARS-CoV-2 Omicron Variant Spike Glycoprotein Mutation\nQ954H Enhances Fusion Core Stability","volume":"20","author":"Vithanage","year":"2025","journal-title":"ACS Chem.\nBiol."},{"issue":"26","key":"2026080408072767400_cit39","doi-asserted-by":"publisher","first-page":"9288","DOI":"10.1073\/pnas.0503989102","article-title":"Structure\nof the uncleaved ectodomain of the paramyxovirus (hPIV3) fusion protein","volume":"102","author":"Yin","year":"2005","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"issue":"19","key":"2026080408072767400_cit40","doi-asserted-by":"publisher","first-page":"4538","DOI":"10.1111\/j.1742-4658.2006.05459.x","article-title":"Crystal Structures\nof Nipah and Hendra Virus Fusion Core Proteins","volume":"273","author":"Lou","year":"2006","journal-title":"FEBS J."},{"key":"2026080408072767400_cit41","doi-asserted-by":"publisher","first-page":"12648","DOI":"10.1021\/jacs.9b04615","article-title":"Dual Inhibition of Human Parainfluenza Type 3 and Respiratory\nSyncytial Virus Infectivity with a Single Agent","volume":"141","author":"Outlaw","year":"2019","journal-title":"J. Am. Chem. Soc."},{"issue":"5","key":"2026080408072767400_cit42","doi-asserted-by":"publisher","first-page":"2140","DOI":"10.1021\/jacs.9b11548","article-title":"Structure-Guided Improvement\nof a Dual HPIV3\/RSV Fusion\nInhibitor","volume":"142","author":"Outlaw","year":"2020","journal-title":"J. Am. Chem. Soc."},{"key":"2026080408072767400_cit57","doi-asserted-by":"publisher","first-page":"125","DOI":"10.1107\/S0907444909047337","article-title":"Integration,\nscaling, space-group assignment and post-refinement","volume":"66","author":"Kabsch","year":"2010","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"2026080408072767400_cit58","doi-asserted-by":"publisher","first-page":"293","DOI":"10.1107\/S0907444911007773","article-title":"Data processing and\nanalysis with the autoPROC toolbox.","volume":"D67","author":"Vonrhein","year":"2011","journal-title":"Acta Cryst."},{"issue":"2","key":"2026080408072767400_cit59","doi-asserted-by":"publisher","first-page":"213","DOI":"10.1107\/S0907444909052925","article-title":"PHENIX: a Comprehensive Python-Based\nSystem for Macromolecular Structure Solution","volume":"66","author":"Adams","year":"2010","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"2026080408072767400_cit60","doi-asserted-by":"publisher","first-page":"2126","DOI":"10.1107\/S0907444904019158","article-title":"Coot: Model-Building\nTools for Molecular Graphics","volume":"60","author":"Emsley","year":"2004","journal-title":"Acta Crystallogr.\nD Biol. Crystallogr."},{"key":"2026080408072767400_cit43","doi-asserted-by":"publisher","first-page":"38","DOI":"10.1002\/(SICI)1097-0134(1998)33:2+&lt;38::AID-PROT6&gt;3.0.CO;2-S","article-title":"Conformational mapping\nof a viral\nfusion peptide in structure-promoting solvents using circular dichroism\nand electrospray mass spectrometry","volume":"33","author":"Waring","year":"1998","journal-title":"Proteins:\nStruct., Funct., Bioinf."},{"key":"2026080408072767400_cit44","doi-asserted-by":"publisher","first-page":"96","DOI":"10.1016\/s0005-2736(01)00443-6","article-title":"Conformational\nmapping of the N-terminal peptide of HIV-1 gp41 in membrane environments\nusing 13C-enhanced Fourier transform infrared spectroscopy","volume":"1559","author":"Gordon","year":"2002","journal-title":"Biochim. Biophys. Acta - Biomembr."},{"key":"2026080408072767400_cit45","doi-asserted-by":"publisher","first-page":"344","DOI":"10.1016\/j.bbamem.2009.10.018","article-title":"Structural\ncharacterization\nof the transmembrane proximal region of the hepatitis C virus E1 glycoprotein","volume":"1798","author":"Spadaccini","year":"2010","journal-title":"Biochim. Biophys. Acta Gen. Subj."},{"issue":"6368","key":"2026080408072767400_cit46","doi-asserted-by":"publisher","first-page":"453","DOI":"10.1038\/356453a0","article-title":"Effect\nof Alanine\nversus Glycine in Alpha-Helices on Protein Stability","volume":"356","author":"Serrano","year":"1992","journal-title":"Nature"},{"key":"2026080408072767400_cit47","doi-asserted-by":"publisher","first-page":"413","DOI":"10.1083\/jcb.151.2.413","article-title":"Evidence that the transition of HIV-1\ngp41 into a six-helix bundle, not the bundle configuration, induces\nmembrane fusion","volume":"151","author":"Melikyan","year":"2000","journal-title":"J. Cell Biol."},{"key":"2026080408072767400_cit48","doi-asserted-by":"publisher","first-page":"5633","DOI":"10.1021\/bi010085w","article-title":"Thermodynamics of peptide inhibitor\nbinding to HIV-1\ngp41","volume":"40","author":"Cole","year":"2001","journal-title":"Biochemistry"},{"key":"2026080408072767400_cit49","doi-asserted-by":"publisher","first-page":"86","DOI":"10.1186\/preaccept-1715264856128511","article-title":"Resistance to N-peptide fusion inhibitors\ncorrelates with thermodynamic stability of the gp41 six-helix bundle\nbut not HIV entry kinetics","volume":"11","author":"De Feo","year":"2014","journal-title":"Retrovirology"},{"key":"2026080408072767400_cit50","doi-asserted-by":"publisher","first-page":"18207","DOI":"10.1073\/pnas.1413592112","article-title":"Single-chain protein mimetics of\nthe N-terminal heptad-repeat\nregion of gp41 with potential as anti-HIV-1 drugs","volume":"111","author":"Crespillo","year":"2014","journal-title":"Proc. Natl. Acad. Sci. U. S. 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