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dc.contributor.authorWillensky, Shmuelen
dc.contributor.authorBar-Rogovsky, Hagiten
dc.contributor.authorBignon, Eduardo Aen
dc.contributor.authorTischler, Nicole Den
dc.contributor.authorModis, Yorgo Evgeniosen
dc.contributor.authorDessau, Mosheen
dc.date.accessioned2017-08-16T09:22:15Z
dc.date.available2017-08-16T09:22:15Z
dc.date.issued2016-10-26en
dc.identifier.urihttps://www.repository.cam.ac.uk/handle/1810/266459
dc.description.abstractHantaviruses are important emerging human pathogens and are the causative agents of serious diseases in humans with high mortality rates. Like other members in the Bunyaviridae family their M segment encodes two glycoproteins, GN and GC, which are responsible for the early events of infection. Hantaviruses deliver their tripartite genome into the cytoplasm by fusion of the viral and endosomal membranes in response to the reduced pH of the endosome. Unlike phleboviruses (e.g. Rift valley fever virus), that have an icosahedral glycoprotein envelope, hantaviruses display a pleomorphic virion morphology as GN and GC assemble into spikes with apparent four-fold symmetry organized in a grid-like pattern on the viral membrane. Here we present the crystal structure of glycoprotein C (GC) from Puumala virus (PUUV), a representative member of the Hantavirus genus. The crystal structure shows GC as the membrane fusion effector of PUUV and it presents a class II membrane fusion protein fold. Furthermore, GC was crystallized in its post-fusion trimeric conformation that until now had been observed only in Flavi- and Togaviridae family members. The PUUV GC structure together with our functional data provides intriguing evolutionary and mechanistic insights into class II membrane fusion proteins and reveals new targets for membrane fusion inhibitors against these important pathogens.
dc.languageEnglishen
dc.language.isoenen
dc.rightsAttribution 4.0 Internationalen
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/en
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/en
dc.titleCrystal Structure of Glycoprotein C from a Hantavirus in the Post-fusion Conformationen
dc.typeArticle
dc.description.versionThis is the final version of the article. It first appeared from PLOS via https://doi.org/10.1371/journal.ppat.1005948en
prism.numbere1005948en
prism.publicationDate2016en
prism.publicationNamePLOS Pathogensen
prism.volume12en
dc.identifier.doi10.17863/CAM.10205
dcterms.dateAccepted2016-09-22en
rioxxterms.versionofrecord10.1371/journal.ppat.1005948en
rioxxterms.versionVoRen
rioxxterms.licenseref.urihttp://creativecommons.org/licenses/by/4.0/en
rioxxterms.licenseref.startdate2016-10-26en
dc.contributor.orcidModis, Yorgo Evgenios [0000-0002-6084-0429]
rioxxterms.typeJournal Article/Reviewen
pubs.funder-project-idWellcome Trust (101908/Z/13/Z)


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Attribution 4.0 International
Except where otherwise noted, this item's licence is described as Attribution 4.0 International