{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T14:35:25Z","timestamp":1791297325254,"version":"4.1.0"},"reference-count":46,"publisher":"American Society for Microbiology","issue":"23","license":[{"start":{"date-parts":[[2006,12,1]],"date-time":"2006-12-01T00:00:00Z","timestamp":1164931200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["J Virol"],"published-print":{"date-parts":[[2006,12]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>The envelope glycoprotein (E) of West Nile virus (WNV) undergoes a conformational rearrangement triggered by low pH that results in a class II fusion event required for viral entry. Herein we present the 3.0-A\u030a crystal structure of the ectodomain of WNV E, which reveals insights into the flavivirus life cycle. We found that WNV E adopts a three-domain architecture that is shared by the E proteins from dengue and tick-borne encephalitis viruses and forms a rod-shaped configuration similar to that observed in immature flavivirus particles. Interestingly, the single N-linked glycosylation site on WNV E is displaced by a novel \u03b1-helix, which could potentially alter lectin-mediated attachment. The localization of histidines within the hinge regions of E implicates these residues in pH-induced conformational transitions. Most strikingly, the WNV E ectodomain crystallized as a monomer, in contrast to other flavivirus E proteins, which have crystallized as antiparallel dimers. WNV E assembles in a crystalline lattice of perpendicular molecules, with the fusion loop of one E protein buried in a hydrophobic pocket at the DI-DIII interface of another. Dimeric E proteins pack their fusion loops into analogous pockets at the dimer interface. We speculate that E proteins could pivot around the fusion loop-pocket junction, allowing virion conformational transitions while minimizing fusion loop exposure.<\/jats:p>","DOI":"10.1128\/jvi.01125-06","type":"journal-article","created":{"date-parts":[[2006,11,13]],"date-time":"2006-11-13T19:03:38Z","timestamp":1163444618000},"page":"11467-11474","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":233,"title":["Crystal Structure of the West Nile Virus Envelope Glycoprotein"],"prefix":"10.1128","volume":"80","author":[{"given":"Grant E.","family":"Nybakken","sequence":"first","affiliation":[{"name":"Departments of Pathology and Immunology"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Christopher A.","family":"Nelson","sequence":"additional","affiliation":[{"name":"Departments of Pathology and Immunology"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Beverly 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