{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,9]],"date-time":"2026-09-09T15:21:27Z","timestamp":1788967287331,"version":"build-2803163510"},"reference-count":67,"publisher":"American Association for the Advancement of Science (AAAS)","issue":"23","content-domain":{"domain":["www.science.org"],"crossmark-restriction":true},"short-container-title":["Sci. Adv."],"published-print":{"date-parts":[[2025,6,6]]},"abstract":"<jats:p>\n                    Viral infections are on the rise and drugs targeting viral proteins are needed. Viroporins constitute a growing group of virus-encoded transmembrane oligomeric proteins that allow passage of small molecules across the membrane. Despite sparsity in viroporin structures, recent work has revealed diversity in both the number of transmembrane helices and oligomeric states. Here, we provide evidence that the small hydrophobic protein (SH) from mumps virus is a pentameric viroporin. From extensive biophysical data, a HADDOCK model of full-length SH shows its intracellular C-terminal region to form an extended structure crucial to stabilization of the pentamer. Heterologous expression of wild-type SH and variants in\n                    <jats:italic toggle=\"yes\">Xenopus laevis<\/jats:italic>\n                    oocytes reveals the viroporin as a chloride channel, with transport facilitated by conserved hydroxyl-carrying residues lining the pore. The channel function of SH is inhibited by the small-molecule BIT225, highlighting the potential for antiviral targeting through SH.\n                  <\/jats:p>","DOI":"10.1126\/sciadv.ads3071","type":"journal-article","created":{"date-parts":[[2025,6,6]],"date-time":"2025-06-06T13:58:24Z","timestamp":1749218304000},"update-policy":"https:\/\/doi.org\/10.34133\/aaas_crossmark","source":"Crossref","is-referenced-by-count":7,"title":["The SH protein of mumps virus is a druggable pentameric viroporin"],"prefix":"10.1126","volume":"11","author":[{"ORCID":"https:\/\/orcid.org\/0009-0002-4200-4707","authenticated-orcid":true,"given":"Kira","family":"Devantier","sequence":"first","affiliation":[{"name":"Laboratory for Molecular and Translational Pharmacology, Department of Biomedical Sciences, University of Copenhagen, Copenhagen, Denmark."},{"name":"Structural Biology and NMR Laboratory (SBiNLab), The Linderstr\u00f8m-Lang Centre for Protein Science and Integrative Structural Biology at University of Copenhagen (ISBUC), Department of Biology, University of Copenhagen, Copenhagen, Denmark."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Trine L.","family":"Toft-Bertelsen","sequence":"additional","affiliation":[{"name":"Department of Neuroscience, Faculty of Health and Medical Sciences, University of Copenhagen, Copenhagen, Denmark."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5459-9608","authenticated-orcid":true,"given":"Andreas","family":"Prestel","sequence":"additional","affiliation":[{"name":"Structural Biology and NMR Laboratory (SBiNLab), The Linderstr\u00f8m-Lang Centre for Protein Science and Integrative Structural Biology at University of Copenhagen (ISBUC), Department of Biology, University of Copenhagen, Copenhagen, Denmark."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5463-2324","authenticated-orcid":true,"given":"Viktoria M. 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