{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,20]],"date-time":"2026-10-20T10:03:21Z","timestamp":1792490601052,"version":"4.5.0"},"reference-count":62,"publisher":"Springer Science and Business Media LLC","issue":"1","license":[{"start":{"date-parts":[[2018,1,24]],"date-time":"2018-01-24T00:00:00Z","timestamp":1516752000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0"},{"start":{"date-parts":[[2018,1,24]],"date-time":"2018-01-24T00:00:00Z","timestamp":1516752000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0"}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Nat Commun"],"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Entry of enveloped viruses relies on insertion of hydrophobic residues of the viral fusion protein into the host cell membrane. However, the intermediate conformations during fusion remain unknown. Here, we address the fusion mechanism of Rift Valley fever virus. We determine the crystal structure of the\u00a0Gn glycoprotein and fit it with the Gc fusion protein into cryo-electron microscopy reconstructions of the virion. Our analysis reveals how the Gn shields the hydrophobic fusion loops of the Gc, preventing premature fusion. Electron cryotomography of virions interacting with membranes under acidic conditions reveals how the fusogenic Gc is activated upon removal of the Gn shield. Repositioning of the Gn allows extension of Gc and insertion of fusion loops in the outer leaflet of the target membrane. These data show early structural transitions that enveloped viruses undergo during host cell entry and indicate that analogous shielding mechanisms are utilized across diverse virus families.<\/jats:p>","DOI":"10.1038\/s41467-017-02789-2","type":"journal-article","created":{"date-parts":[[2018,1,18]],"date-time":"2018-01-18T07:21:33Z","timestamp":1516260093000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":111,"title":["Shielding and activation of a viral membrane fusion protein"],"prefix":"10.1038","volume":"9","author":[{"given":"Steinar","family":"Halldorsson","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9353-0355","authenticated-orcid":false,"given":"Sai","family":"Li","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mengqiu","family":"Li","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Karl","family":"Harlos","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8066-8785","authenticated-orcid":false,"given":"Thomas A.","family":"Bowden","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0348-7323","authenticated-orcid":false,"given":"Juha T.","family":"Huiskonen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2018,1,24]]},"reference":[{"key":"2789_CR1","doi-asserted-by":"publisher","first-page":"690","DOI":"10.1038\/nsmb.1456","volume":"15","author":"SC Harrison","year":"2008","unstructured":"Harrison, S. C. Viral membrane fusion. Nat. Struct. Mol. Biol. 15, 690\u2013698 (2008).","journal-title":"Nat. Struct. Mol. Biol."},{"key":"2789_CR2","doi-asserted-by":"publisher","first-page":"3762","DOI":"10.1128\/JVI.02483-08","volume":"83","author":"JT Huiskonen","year":"2009","unstructured":"Huiskonen, J. T., Overby, A. K., Weber, F. & Gr\u00fcnewald, K. Electron cryo-microscopy and single-particle averaging of Rift Valley fever virus: evidence for GN-GC glycoprotein heterodimers. J. Virol. 83, 3762\u20133769 (2009).","journal-title":"J. Virol."},{"key":"2789_CR3","doi-asserted-by":"publisher","first-page":"10341","DOI":"10.1128\/JVI.01191-08","volume":"82","author":"AN Freiberg","year":"2008","unstructured":"Freiberg, A. N., Sherman, M. B., Morais, M. C., Holbrook, M. R. & Watowich, S. J. Three-dimensional organization of Rift Valley fever virus revealed by cryoelectron tomography. J. Virol. 82, 10341\u201310348 (2008).","journal-title":"J. Virol."},{"key":"2789_CR4","doi-asserted-by":"publisher","first-page":"11","DOI":"10.1016\/j.virol.2009.02.038","volume":"387","author":"MB Sherman","year":"2009","unstructured":"Sherman, M. B., Freiberg, A. N., Holbrook, M. R. & Watowich, S. J. Single-particle cryo-electron microscopy of Rift Valley fever virus. Virology 387, 11\u201315 (2009).","journal-title":"Virology"},{"key":"2789_CR5","doi-asserted-by":"crossref","unstructured":"Phoenix, I. et al. N-glycans on the Rift Valley fever virus envelope glycoproteins Gn and Gc redundantly support viral infection via DC-SIGN. Viruses 8, 149 (2016).","DOI":"10.3390\/v8050149"},{"key":"2789_CR6","doi-asserted-by":"publisher","first-page":"75","DOI":"10.1016\/j.chom.2011.06.007","volume":"10","author":"PY Lozach","year":"2011","unstructured":"Lozach, P.-Y. et al. DC-SIGN as a receptor for phleboviruses. Cell Host Microbe 10, 75\u201388 (2011).","journal-title":"Cell Host Microbe"},{"key":"2789_CR7","doi-asserted-by":"publisher","first-page":"10244","DOI":"10.1128\/JVI.01662-14","volume":"88","author":"M Crispin","year":"2014","unstructured":"Crispin, M. et al. Uukuniemi Phlebovirus assembly and secretion leave a functional imprint on the virion glycome. J. Virol. 88, 10244\u201310251 (2014).","journal-title":"J. Virol."},{"key":"2789_CR8","doi-asserted-by":"publisher","first-page":"12954","DOI":"10.1128\/JVI.02242-12","volume":"86","author":"B Harmon","year":"2012","unstructured":"Harmon, B. et al. Rift Valley fever virus strain MP-12 enters mammalian host cells via caveola-mediated endocytosis. J. Virol. 86, 12954\u201312970 (2012).","journal-title":"J. Virol."},{"key":"2789_CR9","doi-asserted-by":"publisher","first-page":"488","DOI":"10.1016\/j.chom.2010.05.007","volume":"7","author":"PY Lozach","year":"2010","unstructured":"Lozach, P.-Y. et al. Entry of bunyaviruses into mammalian cells. Cell. Host. Microbe 7, 488\u2013499 (2010).","journal-title":"Cell. Host. Microbe"},{"key":"2789_CR10","doi-asserted-by":"publisher","first-page":"34","DOI":"10.1016\/j.coviro.2014.01.009","volume":"5C","author":"Y Modis","year":"2014","unstructured":"Modis, Y. Relating structure to evolution in class II viral membrane fusion proteins. Curr. Opin. Virol. 5C, 34\u201341 (2014).","journal-title":"Curr. Opin. Virol."},{"key":"2789_CR11","doi-asserted-by":"publisher","first-page":"1696","DOI":"10.1073\/pnas.1217780110","volume":"110","author":"M Dessau","year":"2013","unstructured":"Dessau, M. & Modis, Y. Crystal structure of glycoprotein C from Rift Valley fever virus. Proc. Natl Acad. Sci. USA 110, 1696\u20131701 (2013).","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"2789_CR12","doi-asserted-by":"publisher","first-page":"7154","DOI":"10.1073\/pnas.1603827113","volume":"113","author":"S Halldorsson","year":"2016","unstructured":"Halldorsson, S. et al. Structure of a phleboviral envelope glycoprotein reveals a consolidated model of membrane fusion. Proc. Natl Acad. Sci. USA 113, 7154\u20137159 (2016).","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"2789_CR13","doi-asserted-by":"publisher","first-page":"6412","DOI":"10.1074\/jbc.M115.691113","volume":"291","author":"D Bitto","year":"2016","unstructured":"Bitto, D., Halldorsson, S., Caputo, A. & Huiskonen, J. T. Low pH and anionic lipid-dependent fusion of uukuniemi phlebovirus to liposomes. J. Biol. Chem. 291, 6412\u20136422 (2016).","journal-title":"J. Biol. Chem."},{"key":"2789_CR14","doi-asserted-by":"publisher","first-page":"2375","DOI":"10.1073\/pnas.0708738105","volume":"105","author":"AK Overby","year":"2008","unstructured":"Overby, A. K., Pettersson, R. F., Gr\u00fcnewald, K. & Huiskonen, J. T. Insights into bunyavirus architecture from electron cryotomography of Uukuniemi virus. Proc. Natl Acad. Sci. USA 105, 2375\u20132379 (2008).","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"2789_CR15","doi-asserted-by":"publisher","first-page":"959","DOI":"10.1016\/j.celrep.2016.03.082","volume":"15","author":"S Li","year":"2016","unstructured":"Li, S. et al. A molecular-level account of the antigenic hantaviral surface. Cell Rep. 15, 959\u2013967 (2016).","journal-title":"Cell Rep."},{"key":"2789_CR16","doi-asserted-by":"publisher","first-page":"e00378","DOI":"10.1128\/JVI.00378-17","volume":"91","author":"I Rissanen","year":"2017","unstructured":"Rissanen, I. et al. Structural transitions of the conserved and metastable hantaviral glycoprotein envelope. J. Virol. 91, e00378\u201317 (2017).","journal-title":"J. Virol."},{"key":"2789_CR17","doi-asserted-by":"publisher","first-page":"709","DOI":"10.1038\/nature09555","volume":"468","author":"JE Voss","year":"2010","unstructured":"Voss, J. E. et al. Glycoprotein organization of Chikungunya virus particles revealed by X-ray crystallography. Nature 468, 709\u2013712 (2010).","journal-title":"Nature"},{"key":"2789_CR18","doi-asserted-by":"publisher","DOI":"10.1038\/ncomms9843","volume":"6","author":"SL Ilca","year":"2015","unstructured":"Ilca, S. L. et al. Localized reconstruction of subunits from electron cryomicroscopy images of macromolecular complexes. Nat. Commun. 6, 8843 (2015).","journal-title":"Nat. Commun."},{"key":"2789_CR19","doi-asserted-by":"publisher","first-page":"174","DOI":"10.1016\/j.ymeth.2009.04.005","volume":"49","author":"LG Trabuco","year":"2009","unstructured":"Trabuco, L. G., Villa, E., Schreiner, E., Harrison, C. B. & Schulten, K. Molecular dynamics flexible fitting: a practical guide to combine cryo-electron microscopy and X-ray crystallography. Methods 49, 174\u2013180 (2009).","journal-title":"Methods"},{"key":"2789_CR20","doi-asserted-by":"publisher","first-page":"257","DOI":"10.1083\/jcb.112.2.257","volume":"112","author":"R Persson","year":"1991","unstructured":"Persson, R. & Pettersson, R. F. Formation and intracellular transport of a heterodimeric viral spike protein complex. J. Cell. Biol. 112, 257\u2013266 (1991).","journal-title":"J. Cell. Biol."},{"key":"2789_CR21","doi-asserted-by":"publisher","first-page":"49","DOI":"10.1016\/0168-1702(95)00006-C","volume":"36","author":"L Melin","year":"1995","unstructured":"Melin, L. et al. The membrane glycoprotein G1 of Uukuniemi virus contains a signal for localization to the Golgi complex. Virus Res. 36, 49\u201366 (1995).","journal-title":"Virus Res."},{"key":"2789_CR22","doi-asserted-by":"publisher","first-page":"1702","DOI":"10.1021\/pr401162k","volume":"13","author":"M Crispin","year":"2014","unstructured":"Crispin, M. et al. Structural plasticity of the Semliki Forest virus glycome upon interspecies transmission. J. Proteome Res. 13, 1702\u20131712 (2014).","journal-title":"J. Proteome Res."},{"key":"2789_CR23","doi-asserted-by":"publisher","first-page":"6208","DOI":"10.1128\/JVI.00317-10","volume":"84","author":"TA Bowden","year":"2010","unstructured":"Bowden, T. A., Crispin, M., Harvey, D. J., Jones, E. Y. & Stuart, D. I. Dimeric architecture of the Hendra virus attachment glycoprotein: evidence for a conserved mode of assembly. J. Virol. 84, 6208\u20136217 (2010).","journal-title":"J. Virol."},{"key":"2789_CR24","doi-asserted-by":"publisher","first-page":"137","DOI":"10.1016\/S0092-8674(01)00303-8","volume":"105","author":"J Lescar","year":"2001","unstructured":"Lescar, J. et al. The fusion glycoprotein shell of Semliki Forest virus: an icosahedral assembly primed for fusogenic activation at endosomal pH. Cell 105, 137\u2013148 (2001).","journal-title":"Cell"},{"key":"2789_CR25","doi-asserted-by":"publisher","first-page":"705","DOI":"10.1038\/nature09546","volume":"468","author":"L Li","year":"2010","unstructured":"Li, L., Jose, J., Xiang, Y., Kuhn, R. J. & Rossmann, M. G. Structural changes of envelope proteins during alphavirus fusion. Nature 468, 705\u2013708 (2010).","journal-title":"Nature"},{"key":"2789_CR26","doi-asserted-by":"publisher","first-page":"467","DOI":"10.1126\/science.aaf5316","volume":"352","author":"D Sirohi","year":"2016","unstructured":"Sirohi, D. et al. The 3.8 \u00c5 resolution cryo-EM structure of Zika virus. Science 352, 467\u2013470 (2016).","journal-title":"Science"},{"key":"2789_CR27","doi-asserted-by":"publisher","first-page":"717","DOI":"10.1016\/S0092-8674(02)00660-8","volume":"108","author":"RJ Kuhn","year":"2002","unstructured":"Kuhn, R. J. et al. Structure of dengue virus: implications for flavivirus organization, maturation, and fusion. Cell 108, 717\u2013725 (2002).","journal-title":"Cell"},{"key":"2789_CR28","doi-asserted-by":"publisher","first-page":"320","DOI":"10.1038\/nature02239","volume":"427","author":"DL Gibbons","year":"2004","unstructured":"Gibbons, D. L. et al. Conformational change and protein-protein interactions of the fusion protein of Semliki Forest virus. Nature 427, 320\u2013325 (2004).","journal-title":"Nature"},{"key":"2789_CR29","doi-asserted-by":"publisher","first-page":"13642","DOI":"10.1128\/JVI.01973-12","volume":"86","author":"SM de Boer","year":"2012","unstructured":"de Boer, S. M. et al. Acid-activated structural reorganization of the Rift Valley fever virus Gc fusion protein. J. Virol. 86, 13642\u201313652 (2012).","journal-title":"J. Virol."},{"key":"2789_CR30","doi-asserted-by":"publisher","first-page":"13362","DOI":"10.1073\/pnas.1301911110","volume":"110","author":"S Cao","year":"2013","unstructured":"Cao, S. & Zhang, W. Characterization of an early-stage fusion intermediate of Sindbis virus using cryoelectron microscopy. Proc. Natl. Acad. Sci. USA. 110, 13362\u201313367 (2013).","journal-title":"Proc. Natl. Acad. Sci. USA."},{"key":"2789_CR31","doi-asserted-by":"publisher","first-page":"E7564","DOI":"10.1073\/pnas.1705176114","volume":"114","author":"Y Wu","year":"2017","unstructured":"Wu, Y. et al. Structures of phlebovirus glycoprotein Gn and identification of a neutralizing antibody epitope. Proc. Natl. Acad. Sci. USA. 114, E7564\u2013E7573 (2017).","journal-title":"Proc. Natl. Acad. Sci. USA."},{"key":"2789_CR32","doi-asserted-by":"publisher","first-page":"389","DOI":"10.1016\/j.str.2005.01.007","volume":"13","author":"F Fabiola","year":"2005","unstructured":"Fabiola, F. & Chapman, M. S. Fitting of high-resolution structures into electron microscopy reconstruction images. Structure 13, 389\u2013400 (2005).","journal-title":"Structure"},{"key":"2789_CR33","doi-asserted-by":"publisher","first-page":"1243","DOI":"10.1107\/S0907444906029799","volume":"62","author":"AR Aricescu","year":"2006","unstructured":"Aricescu, A. R., Lu, W. & Jones, E. Y. A time- and cost-efficient system for high-level protein production in mammalian cells. Acta Crystallogr. D. Biol. Crystallogr. 62, 1243\u20131250 (2006).","journal-title":"Acta Crystallogr. D. Biol. Crystallogr."},{"key":"2789_CR34","doi-asserted-by":"publisher","first-page":"651","DOI":"10.1107\/S0907444905007808","volume":"61","author":"TS Walter","year":"2005","unstructured":"Walter, T. S. et al. A procedure for setting up high-throughput nanolitre crystallization experiments. Crystallization workflow for initial screening, automated storage, imaging and optimization. Acta Crystallogr. D Biol. Crystallogr. 61, 651\u2013657 (2005).","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"2789_CR35","doi-asserted-by":"publisher","first-page":"1260","DOI":"10.1107\/S0907444913015308","volume":"69","author":"G Winter","year":"2013","unstructured":"Winter, G., Lobley, C. M. C. & Prince, S. M. Decision making in xia2. Acta Crystallogr. D Biol. Crystallogr. 69, 1260\u20131273 (2013).","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"2789_CR36","first-page":"215","volume":"364","author":"C Vonrhein","year":"2007","unstructured":"Vonrhein, C., Blanc, E., Roversi, P. & Bricogne, G. Automated structure solution with autoSHARP. Methods Mol. Biol. 364, 215\u2013230 (2007).","journal-title":"Methods Mol. Biol."},{"key":"2789_CR37","doi-asserted-by":"publisher","first-page":"1002","DOI":"10.1107\/S0907444906022116","volume":"62","author":"K Cowtan","year":"2006","unstructured":"Cowtan, K. The Buccaneer software for automated model building. 1. Tracing protein chains. Acta Crystallogr. D Biol. Crystallogr. 62, 1002\u20131011 (2006).","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"2789_CR38","doi-asserted-by":"publisher","first-page":"213","DOI":"10.1107\/S0907444909052925","volume":"66","author":"PD Adams","year":"2010","unstructured":"Adams, P. D. et al. PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr. D Biol. Crystallogr. 66, 213\u2013221 (2010).","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"2789_CR39","doi-asserted-by":"publisher","first-page":"486","DOI":"10.1107\/S0907444910007493","volume":"66","author":"P Emsley","year":"2010","unstructured":"Emsley, P., Lohkamp, B., Scott, W. G. & Cowtan, K. Features and development of Coot. Acta Crystallogr. D Biol. Crystallogr. 66, 486\u2013501 (2010).","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"2789_CR40","doi-asserted-by":"publisher","first-page":"12","DOI":"10.1107\/S0907444909042073","volume":"66","author":"VB Chen","year":"2010","unstructured":"Chen, V. B. et al. MolProbity: all-atom structure validation for macromolecular crystallography. Acta Crystallogr. D Biol. Crystallogr. 66, 12\u201321 (2010).","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"2789_CR41","doi-asserted-by":"publisher","first-page":"405","DOI":"10.4269\/ajtmh.1995.53.405","volume":"53","author":"R Muller","year":"1995","unstructured":"Muller, R. et al. Characterization of clone 13, a naturally attenuated avirulent isolate of Rift Valley fever virus, which is altered in the small segment. Am. J. Trop. Med. Hyg. 53, 405\u2013411 (1995).","journal-title":"Am. J. Trop. Med. Hyg."},{"key":"2789_CR42","doi-asserted-by":"publisher","first-page":"584","DOI":"10.1038\/nmeth.2472","volume":"10","author":"X Li","year":"2013","unstructured":"Li, X. et al. Electron counting and beam-induced motion correction enable near-atomic-resolution single-particle cryo-EM. Nat. Methods 10, 584\u2013590 (2013).","journal-title":"Nat. Methods"},{"key":"2789_CR43","doi-asserted-by":"publisher","first-page":"334","DOI":"10.1016\/S1047-8477(03)00069-8","volume":"142","author":"JA Mindell","year":"2003","unstructured":"Mindell, J. A. & Grigorieff, N. Accurate determination of local defocus and specimen tilt in electron microscopy. J. Struct. Biol. 142, 334\u2013347 (2003).","journal-title":"J. Struct. Biol."},{"key":"2789_CR44","doi-asserted-by":"publisher","first-page":"519","DOI":"10.1016\/j.jsb.2012.09.006","volume":"180","author":"SH Scheres","year":"2012","unstructured":"Scheres, S. H. W. RELION: implementation of a Bayesian approach to cryo-EM structure determination. J. Struct. Biol. 180, 519\u2013530 (2012).","journal-title":"J. Struct. Biol."},{"key":"2789_CR45","doi-asserted-by":"publisher","first-page":"e11182","DOI":"10.7554\/eLife.11182","volume":"4","author":"X-C Bai","year":"2015","unstructured":"Bai, X.-C., Rajendra, E., Yang, G., Shi, Y. & Scheres, S. H. Sampling the conformational space of the catalytic subunit of human \u03b3-secretase. Elife 4, e11182 (2015).","journal-title":"Elife"},{"key":"2789_CR46","doi-asserted-by":"publisher","DOI":"10.1038\/ncomms14814","volume":"8","author":"Z Sun","year":"2017","unstructured":"Sun, Z. et al. Double-stranded RNA virus outer shell assembly by bona fide domain-swapping. Nat. Commun. 8, 14814 (2017).","journal-title":"Nat. Commun."},{"key":"2789_CR47","doi-asserted-by":"publisher","first-page":"1605","DOI":"10.1002\/jcc.20084","volume":"25","author":"EF Pettersen","year":"2004","unstructured":"Pettersen, E. F. et al. UCSF Chimera--a visualization system for exploratory research and analysis. J. Comput. Chem. 25, 1605\u20131612 (2004).","journal-title":"J. Comput. Chem."},{"key":"2789_CR48","doi-asserted-by":"publisher","DOI":"10.1038\/nmeth.4193","author":"SQ Zheng","year":"2017","unstructured":"Zheng, S. Q. et al. MotionCor2: anisotropic correction of beam-induced motion for improved cryo-electron microscopy. Nat. Methods. https:\/\/doi.org\/10.1038\/nmeth.4193 (2017).","journal-title":"Nat. Methods"},{"key":"2789_CR49","doi-asserted-by":"publisher","first-page":"506","DOI":"10.1126\/science.aaf9620","volume":"353","author":"FK Schur","year":"2016","unstructured":"Schur, F. K. et al. An atomic model of HIV-1 capsid-SP1 reveals structures regulating assembly and maturation. Science 353, 506\u2013508 (2016).","journal-title":"Science"},{"key":"2789_CR50","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1016\/j.jsb.2015.11.003","volume":"193","author":"K Zhang","year":"2016","unstructured":"Zhang, K. Gctf: real-time CTF determination and correction. J. Struct. Biol. 193, 1\u201312 (2016).","journal-title":"J. Struct. Biol."},{"key":"2789_CR51","doi-asserted-by":"publisher","first-page":"71","DOI":"10.1006\/jsbi.1996.0013","volume":"116","author":"JR Kremer","year":"1996","unstructured":"Kremer, J. R., Mastronarde, D. N. & McIntosh, J. R. Computer visualization of three-dimensional image data using IMOD. J. Struct. Biol. 116, 71\u201376 (1996).","journal-title":"J. Struct. Biol."},{"key":"2789_CR52","doi-asserted-by":"publisher","DOI":"10.1016\/j.jsb.2016.06.005","author":"D Castano-Diez","year":"2016","unstructured":"Castano-Diez, D., Kudryashev, M. & Stahlberg, H. Dynamo catalogue: geometrical tools and data management for particle picking in subtomogram averaging of cryo-electron tomograms. J. Struct. Biol. https:\/\/doi.org\/10.1016\/j.jsb.2016.06.005 (2016).","journal-title":"J. Struct. Biol."},{"key":"2789_CR53","doi-asserted-by":"publisher","first-page":"e1005418","DOI":"10.1371\/journal.ppat.1005418","volume":"12","author":"S Li","year":"2016","unstructured":"Li, S. et al. Acidic pH-induced conformations and LAMP1 binding of the lassa virus glycoprotein spike. PLoS Pathog. 12, e1005418 (2016).","journal-title":"PLoS Pathog."},{"key":"2789_CR54","doi-asserted-by":"publisher","first-page":"139","DOI":"10.1016\/j.jsb.2011.12.017","volume":"178","author":"D Castano-Diez","year":"2012","unstructured":"Castano-Diez, D., Kudryashev, M., Arheit, M. & Stahlberg, H. Dynamo: a flexible, user-friendly development tool for subtomogram averaging of cryo-EM data in high-performance computing environments. J. Struct. Biol. 178, 139\u2013151 (2012).","journal-title":"J. Struct. Biol."},{"key":"2789_CR55","doi-asserted-by":"publisher","first-page":"1781","DOI":"10.1002\/jcc.20289","volume":"26","author":"JC Phillips","year":"2005","unstructured":"Phillips, J. C. et al. Scalable molecular dynamics with NAMD. J. Comput. Chem. 26, 1781\u20131802 (2005).","journal-title":"J. Comput. Chem."},{"key":"2789_CR56","doi-asserted-by":"publisher","first-page":"3586","DOI":"10.1021\/jp973084f","volume":"102","author":"AD MacKerell","year":"1998","unstructured":"MacKerell, A. D. et al. All-atom empirical potential for molecular modeling and dynamics studies of proteins. J. Phys. Chem. B. 102, 3586\u20133616 (1998).","journal-title":"J. Phys. Chem. B."},{"key":"2789_CR57","doi-asserted-by":"publisher","first-page":"1400","DOI":"10.1002\/jcc.20065","volume":"25","author":"AD Mackerell Jr.","year":"2004","unstructured":"Mackerell, A. D. Jr. Feig, M. & Brooks, C. L. 3rd. Extending the treatment of backbone energetics in protein force fields: limitations of gas-phase quantum mechanics in reproducing protein conformational distributions in molecular dynamics simulations. J. Comput. Chem. 25, 1400\u20131415 (2004).","journal-title":"J. Comput. Chem."},{"key":"2789_CR58","doi-asserted-by":"publisher","first-page":"643","DOI":"10.1038\/nature12162","volume":"497","author":"G Zhao","year":"2013","unstructured":"Zhao, G. et al. Mature HIV-1 capsid structure by cryo-electron microscopy and all-atom molecular dynamics. Nature 497, 643\u2013646 (2013).","journal-title":"Nature"},{"key":"2789_CR59","doi-asserted-by":"publisher","first-page":"4613","DOI":"10.1063\/1.470648","volume":"103","author":"SE Feller","year":"1995","unstructured":"Feller, S. E., Zhang, Y. H., Pastor, R. W. & Brooks, B. R. Constant-pressure molecular-dynamics simulation - the Langevin Piston method. J. Chem. Phys. 103, 4613\u20134621 (1995).","journal-title":"J. Chem. Phys."},{"key":"2789_CR60","doi-asserted-by":"publisher","first-page":"10089","DOI":"10.1063\/1.464397","volume":"98","author":"T Darden","year":"1993","unstructured":"Darden, T., York, D. & Pedersen, L. Particle mesh Ewald - an N.Log(N) method for Ewald sums in large systems. J. Chem. Phys. 98, 10089\u201310092 (1993).","journal-title":"J. Chem. Phys."},{"key":"2789_CR61","doi-asserted-by":"publisher","first-page":"83","DOI":"10.1016\/bs.aivir.2017.02.002","volume":"98","author":"P Guardado-Calvo","year":"2017","unstructured":"Guardado-Calvo, P. & Rey, F. A. The envelope proteins of the Bunyavirales. Adv. Virus Res. 98, 83\u2013118 (2017).","journal-title":"Adv. Virus Res."},{"key":"2789_CR62","doi-asserted-by":"publisher","first-page":"W252","DOI":"10.1093\/nar\/gku340","volume":"42","author":"M Biasini","year":"2014","unstructured":"Biasini, M. et al. SWISS-MODEL: modelling protein tertiary and quaternary structure using evolutionary information. Nucleic Acids Res. 42, W252\u2013W258 (2014).","journal-title":"Nucleic Acids Res."}],"container-title":["Nature Communications"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.nature.com\/articles\/s41467-017-02789-2","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.nature.com\/articles\/s41467-017-02789-2.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.nature.com\/articles\/s41467-017-02789-2.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,12,20]],"date-time":"2022-12-20T07:47:49Z","timestamp":1671522469000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.nature.com\/articles\/s41467-017-02789-2"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2018,1,24]]},"references-count":62,"journal-issue":{"issue":"1","published-online":{"date-parts":[[2018,12]]}},"alternative-id":["2789"],"URL":"https:\/\/doi.org\/10.1038\/s41467-017-02789-2","relation":{},"ISSN":["2041-1723"],"issn-type":[{"value":"2041-1723","type":"electronic"}],"subject":[],"published":{"date-parts":[[2018,1,24]]},"assertion":[{"value":"30 August 2017","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"28 December 2017","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"24 January 2018","order":3,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"The authors declare no competing financial interests.","order":1,"name":"Ethics","group":{"name":"EthicsHeading","label":"Competing interests"}}],"article-number":"349"}}