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dc.contributor.authorLaajala, Mira
dc.contributor.authorHankaniemi, Minna M.
dc.contributor.authorMäättä, Juha A. E.
dc.contributor.authorHytönen, Vesa P.
dc.contributor.authorLaitinen, Olli H.
dc.contributor.authorMarjomäki, Varpu
dc.date.accessioned2020-01-03T07:51:46Z
dc.date.available2020-01-03T07:51:46Z
dc.date.issued2019
dc.identifier.citationLaajala, Mira; Hankaniemi, Minna M.; Määttä, Juha A. E.; Hytönen, Vesa P.; Laitinen, Olli H.; Marjomäki, Varpu (2019). Host Cell Calpains Can Cleave Structural Proteins from the Enterovirus Polyprotein. Viruses, 11 (12), 1106. DOI: 10.3390/v11121106
dc.identifier.otherCONVID_33942856
dc.identifier.urihttps://jyx.jyu.fi/handle/123456789/67074
dc.description.abstractEnteroviruses are small RNA viruses that cause diseases with various symptoms ranging from mild to severe. Enterovirus proteins are translated as a single polyprotein, which is cleaved by viral proteases to release capsid and nonstructural proteins. Here, we show that also cellular calpains have a potential role in the processing of the enteroviral polyprotein. Using purified calpains 1 and 2 in an in vitro assay, we show that addition of calpains leads to an increase in the release of VP1 and VP3 capsid proteins from P1 of enterovirus B species, detected by western blotting. This was prevented with a calpain inhibitor and was dependent on optimal calcium concentration, especially for calpain 2. In addition, calpain cleavage at the VP3-VP1 interface was supported by a competition assay using a peptide containing the VP3-VP1 cleavage site. Moreover, a mass spectrometry analysis showed that calpains can cleave this same peptide at the VP3-VP1 interface, the cutting site being two amino acids aside from 3C’s cutting site. Furthermore, we show that calpains cannot cleave between P1 and 2A. In conclusion, we show that cellular proteases, calpains, can cleave structural proteins from enterovirus polyprotein in vitro. Whether they assist polyprotein processing in infected cells remains to be shown.en
dc.format.mimetypeapplication/pdf
dc.languageeng
dc.publisherMDPI
dc.relation.ispartofseriesViruses
dc.rightsCC BY 4.0
dc.subject.otherenterovirus
dc.subject.othercalpain
dc.subject.otherproteolytic processing
dc.subject.otherRNA virus
dc.subject.otherpolyprotein
dc.titleHost Cell Calpains Can Cleave Structural Proteins from the Enterovirus Polyprotein
dc.typearticle
dc.identifier.urnURN:NBN:fi:jyu-202001031008
dc.contributor.laitosBio- ja ympäristötieteiden laitosfi
dc.contributor.laitosDepartment of Biological and Environmental Scienceen
dc.type.urihttp://purl.org/eprint/type/JournalArticle
dc.description.reviewstatuspeerReviewed
dc.relation.issn1999-4915
dc.relation.numberinseries12
dc.relation.volume11
dc.type.versionpublishedVersion
dc.rights.copyright© 2019 by the authors
dc.rights.accesslevelopenAccessfi
dc.subject.ysoproteiinit
dc.subject.ysoentsyymit
dc.subject.ysoenterovirukset
dc.subject.ysovirukset
dc.subject.ysoinfektiot
dc.format.contentfulltext
jyx.subject.urihttp://www.yso.fi/onto/yso/p4332
jyx.subject.urihttp://www.yso.fi/onto/yso/p4769
jyx.subject.urihttp://www.yso.fi/onto/yso/p20689
jyx.subject.urihttp://www.yso.fi/onto/yso/p1123
jyx.subject.urihttp://www.yso.fi/onto/yso/p7316
dc.rights.urlhttps://creativecommons.org/licenses/by/4.0/
dc.relation.doi10.3390/v11121106
jyx.fundinginformationThis research was funded by Jane and Aatos Erkko foundation and Academy of Finland, grant number 1309455.


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