{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,1]],"date-time":"2026-10-01T12:19:01Z","timestamp":1790857141148,"version":"4.1.0"},"reference-count":50,"publisher":"American Society for Microbiology","issue":"11","license":[{"start":{"date-parts":[[2009,6,1]],"date-time":"2009-06-01T00:00:00Z","timestamp":1243814400000},"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":[[2009,6]]},"abstract":"<jats:title>ABSTRACT<\/jats:title><jats:p>The internal hydrophobic sequence within the flaviviral capsid protein (protein C) plays an important role in the assembly of infectious virions. Here, this sequence was analyzed in a West Nile virus lineage I isolate (crow V76\/1). An infectious cDNA clone was constructed and used to introduce deletions into the internal hydrophobic domain which comprises helix \u03b12 and part of the loop intervening helices \u03b12 and \u03b13. In total, nine capsid deletion mutants (4 to 14 amino acids long) were constructed and tested for virus viability. Some of the short deletions did not significantly affect growth in cell culture, whereas larger deletions removing almost the entire hydrophobic region significantly impaired viral growth. Efficient growth of the majority of mutants could, however, be restored by the acquisition of second-site mutations. In most cases, these resuscitating mutations were point mutations within protein C changing individual amino acids into more hydrophobic residues, reminiscent of what had been observed previously for another flavivirus, tick-borne encephalitis virus. However, we also identified viable spontaneous pseudorevertants with more than one-third of the capsid protein removed, i.e., 36 or 37 of a total of 105 residues, including all of helix \u03b13 and a hydrophilic segment connecting \u03b13 and \u03b14. These large deletions are predicted to induce formation of large, predominantly hydrophobic fusion helices which may substitute for the loss of the internal hydrophobic domain, underlining the unrivaled structural and functional flexibility of protein C.<\/jats:p>","DOI":"10.1128\/jvi.02653-08","type":"journal-article","created":{"date-parts":[[2009,3,19]],"date-time":"2009-03-19T01:09:14Z","timestamp":1237424954000},"page":"5581-5591","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":35,"title":["Helices \u03b12 and \u03b13 of West Nile Virus Capsid Protein Are Dispensable for Assembly of Infectious Virions"],"prefix":"10.1128","volume":"83","author":[{"given":"Petra","family":"Schlick","sequence":"first","affiliation":[{"name":"Intercell AG, Campus Vienna Biocenter, Vienna, Austria"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Christian","family":"Taucher","sequence":"additional","affiliation":[{"name":"Clinical Institute of Virology, Medical University of Vienna, Vienna, Austria"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Beate","family":"Schittl","sequence":"additional","affiliation":[{"name":"Intercell AG, Campus Vienna Biocenter, Vienna, Austria"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Janina L.","family":"Tran","sequence":"additional","affiliation":[{"name":"Intercell AG, Campus Vienna Biocenter, Vienna, Austria"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Regina M.","family":"Kofler","sequence":"additional","affiliation":[{"name":"Clinical Institute of Virology, Medical University of Vienna, Vienna, Austria"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Wolfgang","family":"Schueler","sequence":"additional","affiliation":[{"name":"Intercell AG, Campus Vienna Biocenter, Vienna, Austria"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Alexander","family":"von Gabain","sequence":"additional","affiliation":[{"name":"Intercell AG, Campus Vienna Biocenter, Vienna, Austria"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Andreas","family":"Meinke","sequence":"additional","affiliation":[{"name":"Intercell AG, Campus Vienna Biocenter, Vienna, Austria"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Christian W.","family":"Mandl","sequence":"additional","affiliation":[{"name":"Clinical Institute of Virology, Medical University of Vienna, Vienna, Austria"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"publisher","DOI":"10.1128\/jvi.69.9.5816-5820.1995"},{"key":"e_1_3_2_3_2","doi-asserted-by":"crossref","first-page":"120","DOI":"10.1002\/0470058005.ch9","volume":"277","year":"2006","unstructured":"Alvarez, D. 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