{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"institution":[{"name":"bioRxiv"}],"indexed":{"date-parts":[[2026,10,12]],"date-time":"2026-10-12T20:20:44Z","timestamp":1791836444997,"version":"4.3.4"},"posted":{"date-parts":[[2024,4,29]]},"group-title":"Biochemistry","reference-count":48,"publisher":"openRxiv","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"accepted":{"date-parts":[[2024,4,29]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                <jats:p>\n                  <jats:italic>Enteroviruses<\/jats:italic>\n                  are the causative agents of paediatric hand-foot-and-mouth disease, and a target for pandemic preparedness due to the risk of higher order complications in a large-scale outbreak. The 2A protease of these viruses is responsible for the self-cleavage of the poly protein, allowing for correct folding and assembly of capsid proteins in the final stages of viral replication. These 2A proteases are highly conserved between\n                  <jats:italic>Enterovirus<\/jats:italic>\n                  species, such as\n                  <jats:italic>Enterovirus A71 and Coxsackievirus A16<\/jats:italic>\n                  . Inhibition of the 2A protease deranges capsid folding and assembly, preventing formation of mature virions in host cells and making the protease a valuable target for antiviral activity. Herein, we describe a crystallographic fragment screening campaign that identified 75 fragments which bind to the 2A protease including 38 unique compounds shown to bind within the active site. These fragments reveal a path for the development of non-peptidomimetic inhibitors of the 2A protease with broad-spectrum anti-enteroviral activity.\n                <\/jats:p>","DOI":"10.1101\/2024.04.29.591684","type":"posted-content","created":{"date-parts":[[2024,4,30]],"date-time":"2024-04-30T00:10:19Z","timestamp":1714435819000},"source":"Crossref","is-referenced-by-count":6,"title":["Crystallographic Fragment Screen of Coxsackievirus A16 2A Protease identifies new opportunities for the development of broad-spectrum anti-enterovirals"],"prefix":"10.64898","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-4706-9916","authenticated-orcid":false,"given":"Ryan M.","family":"Lithgo","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-1845-6028","authenticated-orcid":false,"given":"Charles 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