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Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2019,10,8]]},"abstract":"<jats:p>Cedar virus (CedV) is a bat-borne henipavirus related to Nipah virus (NiV) and Hendra virus (HeV), zoonotic agents of fatal human disease. CedV receptor-binding protein (G) shares only \u223c30% sequence identity with those of NiV and HeV, although they can all use ephrin-B2 as an entry receptor. We demonstrate that CedV also enters cells through additional B- and A-class ephrins (ephrin-B1, ephrin-A2, and ephrin-A5) and report the crystal structure of the CedV G ectodomain alone and in complex with ephrin-B1 or ephrin-B2. The CedV G receptor-binding site is structurally distinct from other henipaviruses, underlying its capability to accommodate additional ephrin receptors. We also show that CedV can enter cells through mouse ephrin-A1 but not human ephrin-A1, which differ by 1 residue in the key contact region. This is evidence of species specific ephrin receptor usage by a henipavirus, and implicates additional ephrin receptors in potential zoonotic transmission.<\/jats:p>","DOI":"10.1073\/pnas.1911773116","type":"journal-article","created":{"date-parts":[[2019,9,23]],"date-time":"2019-09-23T20:35:24Z","timestamp":1569270924000},"page":"20707-20715","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":73,"title":["Structural and functional analyses reveal promiscuous and species specific use of ephrin receptors by Cedar virus"],"prefix":"10.1073","volume":"116","author":[{"given":"Eric D.","family":"Laing","sequence":"first","affiliation":[{"name":"Department of Microbiology and Immunology, Uniformed Services University of the Health Sciences, Bethesda, MD 20814;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Chanakha K.","family":"Navaratnarajah","sequence":"additional","affiliation":[{"name":"Department of Molecular Medicine, Mayo Clinic, Rochester, MN 55905;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sofia","family":"Cheliout Da Silva","sequence":"additional","affiliation":[{"name":"Department of Microbiology and Immunology, Uniformed Services University of the Health Sciences, Bethesda, MD 20814;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Stephanie R.","family":"Petzing","sequence":"additional","affiliation":[{"name":"Department of Microbiology and Immunology, Uniformed Services University of the Health Sciences, Bethesda, MD 20814;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yan","family":"Xu","sequence":"additional","affiliation":[{"name":"Structural Biology Program, Memorial Sloan Kettering Cancer Center, New York, NY 10065;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Spencer L.","family":"Sterling","sequence":"additional","affiliation":[{"name":"Department of Microbiology and Immunology, Uniformed Services University of the Health Sciences, Bethesda, MD 20814;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Glenn A.","family":"Marsh","sequence":"additional","affiliation":[{"name":"Commonwealth Scientific and Industrial Research Organization Australian Animal Health Laboratory, Geelong, VIC 3219, Australia;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2752-0535","authenticated-orcid":false,"given":"Lin-Fa","family":"Wang","sequence":"additional","affiliation":[{"name":"Programme in Emerging Infectious Diseases, Duke-National University of Singapore Medical School, Singapore 169857"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Moushimi","family":"Amaya","sequence":"additional","affiliation":[{"name":"Department of Microbiology and Immunology, Uniformed Services University of the Health Sciences, Bethesda, MD 20814;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Dimitar B.","family":"Nikolov","sequence":"additional","affiliation":[{"name":"Structural Biology Program, Memorial Sloan Kettering Cancer Center, New York, NY 10065;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6881-2548","authenticated-orcid":false,"given":"Roberto","family":"Cattaneo","sequence":"additional","affiliation":[{"name":"Department of Molecular Medicine, Mayo Clinic, Rochester, MN 55905;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-5382-0510","authenticated-orcid":false,"given":"Christopher C.","family":"Broder","sequence":"additional","affiliation":[{"name":"Department of Microbiology and Immunology, Uniformed Services University of the Health Sciences, Bethesda, MD 20814;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-5412-6942","authenticated-orcid":false,"given":"Kai","family":"Xu","sequence":"additional","affiliation":[{"name":"Structural Biology Program, Memorial Sloan Kettering Cancer Center, New York, NY 10065;"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"341","published-online":{"date-parts":[[2019,9,23]]},"reference":[{"key":"e_1_3_4_1_2","first-page":"153","article-title":"Animal challenge models of henipavirus infection and pathogenesis","volume":"359","author":"Geisbert T. 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Virology 382, 125\u2013131 (2008).","journal-title":"Virology"},{"key":"e_1_3_4_55_2","doi-asserted-by":"crossref","first-page":"457","DOI":"10.1128\/MMBR.00004-08","article-title":"Cross-species virus transmission and the emergence of new epidemic diseases","volume":"72","author":"Parrish C. R.","year":"2008","unstructured":"C. R. Parrish ., Cross-species virus transmission and the emergence of new epidemic diseases. Microbiol. Mol. Biol. Rev. 72, 457\u2013470 (2008).","journal-title":"Microbiol. Mol. Biol. Rev."},{"key":"e_1_3_4_56_2","doi-asserted-by":"crossref","first-page":"11429","DOI":"10.1128\/JVI.78.20.11429-11433.2004","article-title":"Efficient replication of severe acute respiratory syndrome coronavirus in mouse cells is limited by murine angiotensin-converting enzyme 2","volume":"78","author":"Li W.","year":"2004","unstructured":"W. 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Cell Rep. 24, 1730\u20131737 (2018).","journal-title":"Cell Rep."},{"key":"e_1_3_4_61_2","doi-asserted-by":"crossref","first-page":"50","DOI":"10.1016\/j.brainres.2008.09.100","article-title":"Regional and cellular distribution of ephrin-B1 in adult mouse brain","volume":"1247","author":"Migani P.","year":"2009","unstructured":"P. Migani, C. Bartlett, S. Dunlop, L. Beazley, J. Rodger, Regional and cellular distribution of ephrin-B1 in adult mouse brain. Brain Res. 1247, 50\u201361 (2009).","journal-title":"Brain Res."},{"key":"e_1_3_4_62_2","doi-asserted-by":"crossref","first-page":"734","DOI":"10.1002\/cne.21001","article-title":"Distribution of EphB receptors and ephrin-B1 in the developing vertebrate spinal cord","volume":"497","author":"Jevince A. R.","year":"2006","unstructured":"A. R. Jevince, S. R. Kadison, A. J. Pittman, C.-B. Chien, Z. Kaprielian, Distribution of EphB receptors and ephrin-B1 in the developing vertebrate spinal cord. J. Comp. Neurol. 497, 734\u2013750 (2006).","journal-title":"J. Comp. Neurol."},{"key":"e_1_3_4_63_2","doi-asserted-by":"crossref","first-page":"541","DOI":"10.1086\/519689","article-title":"Measles virus vaccine attenuation: Suboptimal infection of lymphatic tissue and tropism alteration","volume":"196","author":"Condack C.","year":"2007","unstructured":"C. Condack, J. C. Grivel, P. Devaux, L. Margolis, R. Cattaneo, Measles virus vaccine attenuation: Suboptimal infection of lymphatic tissue and tropism alteration. J. Infect. Dis. 196, 541\u2013549 (2007).","journal-title":"J. Infect. Dis."},{"key":"e_1_3_4_64_2","doi-asserted-by":"crossref","first-page":"16","DOI":"10.1016\/j.coviro.2014.01.004","article-title":"Structural basis of efficient contagion: Measles variations on a theme by parainfluenza viruses","volume":"5","author":"Mateo M.","year":"2014","unstructured":"M. Mateo, C. K. Navaratnarajah, R. 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Virol. 90, 6326\u20136343 (2016).","journal-title":"J. Virol."},{"key":"e_1_3_4_67_2","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1007\/978-1-59745-554-1_2","article-title":"Preparation of recombinant viral glycoproteins for novel and therapeutic antibody discovery","volume":"525","author":"Chan Y. P.","year":"2009","unstructured":"Y. P. Chan, L. Yan, Y. R. Feng, C. C. Broder, Preparation of recombinant viral glycoproteins for novel and therapeutic antibody discovery. Methods Mol. Biol. 525, 31\u201358, xiii (2009).","journal-title":"Methods Mol. Biol."},{"key":"e_1_3_4_68_2","doi-asserted-by":"crossref","first-page":"357","DOI":"10.1016\/j.virol.2007.11.011","article-title":"Functional studies of host-specific ephrin-B ligands as Henipavirus receptors","volume":"372","author":"Bossart K. N.","year":"2008","unstructured":"K. N. Bossart ., Functional studies of host-specific ephrin-B ligands as Henipavirus receptors. 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Nussbaum ., Functional and structural interactions between measles virus hemagglutinin and CD46. J. Virol. 69, 3341\u20133349 (1995).","journal-title":"J. Virol."},{"key":"e_1_3_4_74_2","first-page":"309","article-title":"Viral glycoprotein-mediated cell fusion assays using vaccinia virus vectors","volume":"269","author":"Bossart K. N.","year":"2004","unstructured":"K. N. Bossart, C. C. Broder, Viral glycoprotein-mediated cell fusion assays using vaccinia virus vectors. Methods Mol. Biol. 269, 309\u2013332 (2004).","journal-title":"Methods Mol. Biol."},{"key":"e_1_3_4_75_2","doi-asserted-by":"crossref","first-page":"68","DOI":"10.1128\/JVI.02253-15","article-title":"A structurally unresolved head segment of defined length favors proper measles virus hemagglutinin tetramerization and efficient membrane fusion triggering","volume":"90","author":"Navaratnarajah C. K.","year":"2015","unstructured":"C. K. Navaratnarajah, Q. Rosemarie, R. Cattaneo, A structurally unresolved head segment of defined length favors proper measles virus hemagglutinin tetramerization and efficient membrane fusion triggering. J. Virol. 90, 68\u201375 (2015).","journal-title":"J. Virol."},{"key":"e_1_3_4_76_2","first-page":"307","volume-title":"Methods in Enzymology","author":"Otwinowski Z.","year":"1997","unstructured":"Z. Otwinowski, W. Minor, \u201cProcessing of X-ray Diffraction Data Collected in Oscillation Mode\u201d in Methods in Enzymology, C. W. Carter Jr, R. M. Sweet, Eds. (Academic Press, New York, 1997), pp. 307\u2013326."},{"key":"e_1_3_4_77_2","doi-asserted-by":"crossref","first-page":"32","DOI":"10.1107\/S0907444906045975","article-title":"Solving structures of protein complexes by molecular replacement with Phaser","volume":"63","author":"McCoy A. J.","year":"2007","unstructured":"A. J. McCoy, Solving structures of protein complexes by molecular replacement with Phaser. Acta Crystallogr. D. Biol. Crystallogr. 63, 32\u201341 (2007).","journal-title":"Acta Crystallogr. D. Biol. Crystallogr."},{"key":"e_1_3_4_78_2","doi-asserted-by":"crossref","first-page":"2126","DOI":"10.1107\/S0907444904019158","article-title":"Coot: Model-building tools for molecular graphics","volume":"60","author":"Emsley P.","year":"2004","unstructured":"P. Emsley, K. Cowtan, Coot: Model-building tools for molecular graphics. Acta Crystallogr. D. Biol. Crystallogr. 60, 2126\u20132132 (2004).","journal-title":"Acta Crystallogr. D. Biol. Crystallogr."},{"key":"e_1_3_4_79_2","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1107\/S0907444909052925","article-title":"PHENIX: A comprehensive Python-based system for macromolecular structure solution","volume":"66","author":"Adams P. D.","year":"2010","unstructured":"P. D. Adams ., PHENIX: A comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr. D. Biol. 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