{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,23]],"date-time":"2026-09-23T12:34:04Z","timestamp":1790166844273,"version":"4.1.0"},"reference-count":57,"publisher":"MDPI AG","issue":"12","license":[{"start":{"date-parts":[[2019,11,28]],"date-time":"2019-11-28T00:00:00Z","timestamp":1574899200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100004012","name":"Jane and Aatos Erkko foundation","doi-asserted-by":"publisher","award":["-"],"award-info":[{"award-number":["-"]}],"id":[{"id":"10.13039\/501100004012","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100002341","name":"Academy of Finland","doi-asserted-by":"publisher","award":["1309455"],"award-info":[{"award-number":["1309455"]}],"id":[{"id":"10.13039\/501100002341","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Viruses"],"abstract":"<jats:p>Enteroviruses 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\u2019s 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.<\/jats:p>","DOI":"10.3390\/v11121106","type":"journal-article","created":{"date-parts":[[2019,11,28]],"date-time":"2019-11-28T10:54:10Z","timestamp":1574938450000},"page":"1106","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":9,"title":["Host Cell Calpains Can Cleave Structural Proteins from the Enterovirus Polyprotein"],"prefix":"10.3390","volume":"11","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-3981-280X","authenticated-orcid":false,"given":"Mira","family":"Laajala","sequence":"first","affiliation":[{"name":"Department of Biological and Environmental Science\/Nanoscience Center, University of Jyv\u00e4skyl\u00e4, Survontie 9C, FI-40500 Jyv\u00e4skyl\u00e4, Finland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Minna M.","family":"Hankaniemi","sequence":"additional","affiliation":[{"name":"Faculty of Medicine and Health Technology, Tampere University, FI-33014 Tampere, Finland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Juha A. E.","family":"M\u00e4\u00e4tt\u00e4","sequence":"additional","affiliation":[{"name":"Faculty of Medicine and Health Technology, Tampere University, FI-33014 Tampere, Finland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9357-1480","authenticated-orcid":false,"given":"Vesa P.","family":"Hyt\u00f6nen","sequence":"additional","affiliation":[{"name":"Faculty of Medicine and Health Technology, Tampere University, FI-33014 Tampere, Finland"},{"name":"Department of Clinical Chemistry, Fimlab Laboratories, Pirkanmaa Hospital District, FI-33520 Tampere, Finland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3751-9952","authenticated-orcid":false,"given":"Olli H.","family":"Laitinen","sequence":"additional","affiliation":[{"name":"Faculty of Medicine and Health Technology, Tampere University, FI-33014 Tampere, Finland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4592-5926","authenticated-orcid":false,"given":"Varpu","family":"Marjom\u00e4ki","sequence":"additional","affiliation":[{"name":"Department of Biological and Environmental Science\/Nanoscience Center, University of Jyv\u00e4skyl\u00e4, Survontie 9C, FI-40500 Jyv\u00e4skyl\u00e4, Finland"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2019,11,28]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"282","DOI":"10.1016\/j.meegid.2012.10.016","article-title":"Picornavirus and Enterovirus Diversity with Associated Human Diseases","volume":"14","author":"Tapparel","year":"2013","journal-title":"Infect. 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