{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,7]],"date-time":"2026-10-07T13:34:20Z","timestamp":1791380060156,"version":"4.3.3"},"reference-count":58,"publisher":"National Academy of Sciences","issue":"42","license":[{"start":{"date-parts":[[2024,10,10]],"date-time":"2024-10-10T00:00:00Z","timestamp":1728518400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0\/"}],"funder":[{"DOI":"10.13039\/100000060","name":"HHS | NIH | National Institute of Allergy and Infectious Diseases","doi-asserted-by":"publisher","award":["NIH 1U19AI171292-01"],"award-info":[{"award-number":["NIH 1U19AI171292-01"]}],"id":[{"id":"10.13039\/100000060","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000054","name":"HHS | NIH | National Cancer Institute","doi-asserted-by":"publisher","award":["2P30CA016086-45"],"award-info":[{"award-number":["2P30CA016086-45"]}],"id":[{"id":"10.13039\/100000054","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2024,10,15]]},"abstract":"<jats:p>\n                    Chikungunya virus (CHIKV) is a mosquito-borne alphavirus that has been responsible for numerous large-scale outbreaks in the last twenty years. Currently, there are no FDA-approved therapeutics for any alphavirus infection. CHIKV nonstructural protein 2 (nsP2), which contains a cysteine protease domain, is essential for viral replication, making it an attractive target for a drug discovery campaign. Here, we optimized a CHIKV nsP2 protease (nsP2pro) biochemical assay for the screening of a 6,120-compound cysteine-directed covalent fragment library. Using a 50% inhibition threshold, we identified 153 hits (2.5% hit rate). In dose\u2013response follow-up, RA-0002034, a covalent fragment that contains a vinyl sulfone warhead, inhibited CHIKV nsP2pro with an IC\n                    <jats:sub>50<\/jats:sub>\n                    of 58 \u00b1 17 nM, and further analysis with time-dependent inhibition studies yielded a k\n                    <jats:sub>inact<\/jats:sub>\n                    \u2009\/K\n                    <jats:sub>I<\/jats:sub>\n                    of 6.4 \u00d7 10\n                    <jats:sup>3<\/jats:sup>\n                    M\n                    <jats:sup>\u22121<\/jats:sup>\n                    s\n                    <jats:sup>\u22121<\/jats:sup>\n                    . LC-MS\/MS analysis determined that RA-0002034 covalently modified the catalytic cysteine in a site-specific manner. Additionally, RA-0002034 showed no significant off-target reactivity in proteomic experiments or against a panel of cysteine proteases. In addition to the potent biochemical inhibition of CHIKV nsP2pro activity and exceptional selectivity, RA-0002034 was tested in cellular models of alphavirus infection and effectively inhibited viral replication of both CHIKV and related alphaviruses. This study highlights the identification and characterization of the chemical probe RA-0002034 as a promising hit compound from covalent fragment-based screening for development toward a CHIKV or pan-alphavirus therapeutic.\n                  <\/jats:p>","DOI":"10.1073\/pnas.2409166121","type":"journal-article","created":{"date-parts":[[2024,10,10]],"date-time":"2024-10-10T11:54:56Z","timestamp":1728561296000},"update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":37,"title":["Identification of a cell-active chikungunya virus nsP2 protease inhibitor using a covalent fragment-based screening approach"],"prefix":"10.1073","volume":"121","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-5306-0790","authenticated-orcid":false,"given":"Eric M.","family":"Merten","sequence":"first","affiliation":[{"name":"Eshelman School of Pharmacy, Center for Integrative Chemical Biology and Drug Discovery, Division of Chemical Biology and Medicinal Chemistry, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4713-2241","authenticated-orcid":false,"given":"John D.","family":"Sears","sequence":"additional","affiliation":[{"name":"Department of Microbiology and Immunology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8682-9260","authenticated-orcid":false,"given":"Tina M.","family":"Leisner","sequence":"additional","affiliation":[{"name":"Eshelman School of Pharmacy, Center for Integrative Chemical Biology and Drug Discovery, Division of Chemical Biology and Medicinal Chemistry, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"P. Brian","family":"Hardy","sequence":"additional","affiliation":[{"name":"Eshelman School of Pharmacy, Center for Integrative Chemical Biology and Drug Discovery, Division of Chemical Biology and Medicinal Chemistry, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9359-6074","authenticated-orcid":false,"given":"Anirban","family":"Ghoshal","sequence":"additional","affiliation":[{"name":"Structural Genomics Consortium, Division of Chemical Biology and Medicinal Chemistry, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8684-8755","authenticated-orcid":false,"given":"Mohammad Anwar","family":"Hossain","sequence":"additional","affiliation":[{"name":"Structural Genomics Consortium, Division of Chemical Biology and Medicinal Chemistry, University of North Carolina at 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