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Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2017,8,29]]},"abstract":"<jats:title>Significance<\/jats:title>\n                  <jats:p>Coronaviruses such as Middle East respiratory syndrome coronavirus (MERS-CoV) cause severe respiratory distress with high fatality rates. The spike (S) glycoprotein is a determinant of host range and is the target of neutralizing antibodies and subunit vaccine development. We describe an engineering strategy for stabilization of soluble S proteins in the prefusion conformation, which results in greatly increased expression, conformational homogeneity, and elicitation of potent antibody responses. Cryo-EM structures of the stabilized MERS-CoV S protein in complex with a stem-directed neutralizing antibody provide a molecular basis for host-cell protease requirements and identify a site of immune pressure. We also defined four conformational states of the trimer wherein each receptor-binding domain is either packed together at the membrane-distal apex or rotated into a receptor-accessible conformation.<\/jats:p>","DOI":"10.1073\/pnas.1707304114","type":"journal-article","created":{"date-parts":[[2017,8,14]],"date-time":"2017-08-14T20:50:24Z","timestamp":1502743824000},"update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":1116,"title":["Immunogenicity and structures of a rationally designed prefusion MERS-CoV spike antigen"],"prefix":"10.1073","volume":"114","author":[{"given":"Jesper","family":"Pallesen","sequence":"first","affiliation":[{"name":"Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nianshuang","family":"Wang","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Cell 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