{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T14:33:56Z","timestamp":1791297236021,"version":"4.1.0"},"reference-count":0,"publisher":"American Society for Microbiology","issue":"2","license":[{"start":{"date-parts":[[1995,2,1]],"date-time":"1995-02-01T00:00:00Z","timestamp":791596800000},"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":[[1995,2]]},"abstract":"<jats:p>The flavivirus envelope protein E undergoes irreversible conformational changes at a mildly acidic pH which are believed to be necessary for membrane fusion in endosomes. In this study we used a combination of chemical cross-linking and sedimentation analysis to show that the envelope proteins of the flavivirus tick-borne encephalitis virus also change their oligomeric structure when exposed to a mildly acidic environment. Under neutral or slightly alkaline conditions, protein E on the surface of native virions exists as a homodimer which can be isolated by solubilization with the nonionic detergent Triton X-100. Solubilization with the same detergent after pretreatment at an acidic pH, however, yielded homotrimers rather than homodimers, suggesting that exposure to an acidic pH had induced a simultaneous weakening of dimeric contacts and a strengthening of trimeric ones. The pH threshold for the dimer-to-trimer transition was found to be 6.5. Because the pH dependence of this transition parallels that of previously observed changes in the conformation and hydrophobicity of protein E and that of virus-induced membrane fusion, it appears likely that the mechanism of fusion with endosomal membranes involves a specific rearrangement of the proteins in the viral envelope. Immature virions in which protein E is associated with the uncleaved precursor (prM) of the membrane protein M did not undergo a low-pH-induced rearrangement. This is consistent with a protective role of protein prM for protein E during intracellular transport of immature virions through acidic compartments of the trans-Golgi network.<\/jats:p>","DOI":"10.1128\/jvi.69.2.695-700.1995","type":"journal-article","created":{"date-parts":[[2020,1,6]],"date-time":"2020-01-06T21:25:15Z","timestamp":1578345915000},"page":"695-700","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":253,"title":["Oligomeric rearrangement of tick-borne encephalitis virus envelope proteins induced by an acidic pH"],"prefix":"10.1128","volume":"69","author":[{"given":"S L","family":"Allison","sequence":"first","affiliation":[{"name":"Institute of Virology, University of Vienna, Austria."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"J","family":"Schalich","sequence":"additional","affiliation":[{"name":"Institute of Virology, University of Vienna, Austria."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"K","family":"Stiasny","sequence":"additional","affiliation":[{"name":"Institute of Virology, University of Vienna, Austria."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"C W","family":"Mandl","sequence":"additional","affiliation":[{"name":"Institute of Virology, University of Vienna, Austria."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"C","family":"Kunz","sequence":"additional","affiliation":[{"name":"Institute of Virology, University of Vienna, Austria."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"F X","family":"Heinz","sequence":"additional","affiliation":[{"name":"Institute of Virology, University of Vienna, Austria."}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","container-title":["Journal of Virology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/journals.asm.org\/doi\/pdf\/10.1128\/jvi.69.2.695-700.1995","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/journals.asm.org\/doi\/pdf\/10.1128\/jvi.69.2.695-700.1995","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,3,5]],"date-time":"2022-03-05T13:11:11Z","timestamp":1646485871000},"score":1,"resource":{"primary":{"URL":"https:\/\/journals.asm.org\/doi\/10.1128\/jvi.69.2.695-700.1995"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1995,2]]},"references-count":0,"journal-issue":{"issue":"2","published-print":{"date-parts":[[1995,2]]}},"alternative-id":["10.1128\/jvi.69.2.695-700.1995"],"URL":"https:\/\/doi.org\/10.1128\/jvi.69.2.695-700.1995","relation":{},"ISSN":["0022-538X","1098-5514"],"issn-type":[{"value":"0022-538X","type":"print"},{"value":"1098-5514","type":"electronic"}],"subject":[],"published":{"date-parts":[[1995,2]]},"assertion":[{"value":"1995-02-01","order":2,"name":"published","label":"Published","group":{"name":"publication_history","label":"Publication History"}}]}}