{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,15]],"date-time":"2026-10-15T00:41:35Z","timestamp":1792024895997,"version":"4.4.0"},"update-to":[{"DOI":"10.1371\/journal.ppat.1009371","type":"new_version","label":"New version","source":"publisher","updated":{"date-parts":[[2021,3,5]],"date-time":"2021-03-05T00:00:00Z","timestamp":1614902400000}}],"reference-count":70,"publisher":"Public Library of Science (PLoS)","issue":"2","license":[{"start":{"date-parts":[[2021,2,23]],"date-time":"2021-02-23T00:00:00Z","timestamp":1614038400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100000060","name":"National Institute of Allergy and Infectious Diseases","doi-asserted-by":"publisher","award":["AI071002"],"award-info":[{"award-number":["AI071002"]}],"id":[{"id":"10.13039\/100000060","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000060","name":"National Institute of Allergy and Infectious Diseases","doi-asserted-by":"publisher","award":["AI153400"],"award-info":[{"award-number":["AI153400"]}],"id":[{"id":"10.13039\/100000060","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["www.plospathogens.org"],"crossmark-restriction":false},"short-container-title":["PLoS Pathog"],"abstract":"<jats:p>\n                    Morbilliviruses, such as measles virus (MeV) and canine distemper virus (CDV), are highly infectious members of the paramyxovirus family. MeV is responsible for major morbidity and mortality in non-vaccinated populations. ERDRP-0519, a pan-morbillivirus small molecule inhibitor for the treatment of measles, targets the morbillivirus RNA-dependent RNA-polymerase (RdRP) complex and displayed unparalleled oral efficacy against lethal infection of ferrets with CDV, an established surrogate model for human measles. Resistance profiling identified the L subunit of the RdRP, which harbors all enzymatic activity of the polymerase complex, as the molecular target of inhibition. Here, we examined binding characteristics, physical docking site, and the molecular mechanism of action of ERDRP-0519 through label-free biolayer interferometry, photoaffinity cross-linking, and\n                    <jats:italic>in vitro<\/jats:italic>\n                    RdRP assays using purified MeV RdRP complexes and synthetic templates. Results demonstrate that unlike all other mononegavirus small molecule inhibitors identified to date, ERDRP-0519 inhibits all phosphodiester bond formation in both\n                    <jats:italic>de novo<\/jats:italic>\n                    initiation of RNA synthesis at the promoter and RNA elongation by a committed polymerase complex. Photocrosslinking and resistance profiling-informed ligand docking revealed that this unprecedented mechanism of action of ERDRP-0519 is due to simultaneous engagement of the L protein polyribonucleotidyl transferase (PRNTase)-like domain and the flexible intrusion loop by the compound, pharmacologically locking the polymerase in pre-initiation conformation. This study informs selection of ERDRP-0519 as clinical candidate for measles therapy and identifies a previously unrecognized druggable site in mononegavirus L polymerase proteins that can silence all synthesis of viral RNA.\n                  <\/jats:p>","DOI":"10.1371\/journal.ppat.1009371","type":"journal-article","created":{"date-parts":[[2021,2,23]],"date-time":"2021-02-23T14:58:59Z","timestamp":1614092339000},"page":"e1009371","update-policy":"https:\/\/doi.org\/10.1371\/journal.ppat.corrections_policy","source":"Crossref","is-referenced-by-count":37,"title":["Therapeutic targeting of measles virus polymerase with ERDRP-0519 suppresses all RNA synthesis activity"],"prefix":"10.1371","volume":"17","author":[{"given":"Robert M.","family":"Cox","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-1660-1666","authenticated-orcid":true,"given":"Julien","family":"Sourimant","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mugunthan","family":"Govindarajan","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-5132-2833","authenticated-orcid":true,"given":"Michael G.","family":"Natchus","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2034-2107","authenticated-orcid":true,"given":"Richard K.","family":"Plemper","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"340","published-online":{"date-parts":[[2021,2,23]]},"reference":[{"issue":"4536","key":"ppat.1009371.ref001","doi-asserted-by":"crossref","first-page":"1053","DOI":"10.1126\/science.7063839","article-title":"Directly transmitted infections diseases: control by vaccination","volume":"215","author":"RM Anderson","year":"1982","journal-title":"Science"},{"issue":"3","key":"ppat.1009371.ref002","doi-asserted-by":"crossref","first-page":"365","DOI":"10.1017\/S002217240006160X","article-title":"Age-related changes in the rate of disease transmission: implications for the design of vaccination programmes","volume":"94","author":"RM Anderson","year":"1985","journal-title":"J Hyg (Lond)"},{"issue":"11","key":"ppat.1009371.ref003","doi-asserted-by":"crossref","first-page":"1149","DOI":"10.1001\/jama.2016.1353","article-title":"Association Between Vaccine Refusal and Vaccine-Preventable Diseases in the United States: A Review of Measles and Pertussis","volume":"315","author":"VK Phadke","year":"2016","journal-title":"JAMA"},{"issue":"5","key":"ppat.1009371.ref004","doi-asserted-by":"crossref","first-page":"494","DOI":"10.1001\/jamapediatrics.2015.0384","article-title":"Substandard vaccination compliance and the 2015 measles outbreak","volume":"169","author":"MS Majumder","year":"2015","journal-title":"JAMA Pediatr"},{"key":"ppat.1009371.ref005","article-title":"Regional Office for Europe","author":"World Health Organization","year":"2019","journal-title":"European Region loses ground in effort to eliminate measles"},{"issue":"7804","key":"ppat.1009371.ref006","doi-asserted-by":"crossref","first-page":"446","DOI":"10.1038\/d41586-020-01011-6","article-title":"Why measles deaths are surging\u2014and coronavirus could make it worse","volume":"580","author":"L. Roberts","year":"2020","journal-title":"Nature"},{"issue":"6501","key":"ppat.1009371.ref007","first-page":"261","article-title":"COVID-19 policies: Remember measles","volume":"369","author":"D Guha-Sapir","journal-title":"Science. 2020"},{"key":"ppat.1009371.ref008","article-title":"Routine childhood immunisation during the COVID-19 pandemic in Africa: a benefit-risk analysis of health benefits versus excess risk of SARS-CoV-2 infection","author":"K Abbas","year":"2020","journal-title":"Lancet Glob Health"},{"issue":"8","key":"ppat.1009371.ref009","first-page":"811","article-title":"Measles control\u2014can measles virus inhibitors make a difference?","volume":"10","author":"RK Plemper","year":"2009","journal-title":"Curr Opin Investig Drugs"},{"issue":"232","key":"ppat.1009371.ref010","doi-asserted-by":"crossref","first-page":"232ra52","DOI":"10.1126\/scitranslmed.3008517","article-title":"An orally available, small-molecule polymerase inhibitor shows efficacy against a lethal morbillivirus infection in a large animal model","volume":"6","author":"SA Krumm","year":"2014","journal-title":"Sci Transl Med."},{"issue":"9","key":"ppat.1009371.ref011","doi-asserted-by":"crossref","first-page":"4220","DOI":"10.1021\/jm201699w","article-title":"Non-nucleoside inhibitors of the measles virus RNA-dependent RNA polymerase: synthesis, structure-activity relationships, and pharmacokinetics","volume":"55","author":"JM Ndungu","year":"2012","journal-title":"J Med Chem"},{"issue":"9","key":"ppat.1009371.ref012","doi-asserted-by":"crossref","first-page":"3860","DOI":"10.1128\/AAC.00503-09","article-title":"Target analysis of the experimental measles therapeutic AS-136A","volume":"53","author":"JJ Yoon","year":"2009","journal-title":"Antimicrob Agents Chemother"},{"issue":"7","key":"ppat.1009371.ref013","doi-asserted-by":"crossref","first-page":"2293","DOI":"10.1128\/AAC.00289-07","article-title":"Nonnucleoside inhibitor of measles virus RNA-dependent RNA polymerase complex activity","volume":"51","author":"LK White","year":"2007","journal-title":"Antimicrob Agents Chemother"},{"issue":"23","key":"ppat.1009371.ref014","doi-asserted-by":"crossref","first-page":"12579","DOI":"10.1128\/JVI.77.23.12579-12591.2003","article-title":"A ferret model of canine distemper virus virulence and immunosuppression","volume":"77","author":"V von Messling","year":"2003","journal-title":"J Virol"},{"issue":"28","key":"ppat.1009371.ref015","doi-asserted-by":"crossref","first-page":"11713","DOI":"10.1073\/pnas.0903228106","article-title":"Structure of the vesicular stomatitis virus nucleocapsid in complex with the nucleocapsid-binding domain of the small polymerase cofactor, P","volume":"106","author":"TJ Green","year":"2009","journal-title":"Proc Natl Acad Sci U S A"},{"issue":"1","key":"ppat.1009371.ref016","doi-asserted-by":"crossref","first-page":"222","DOI":"10.1016\/0042-6822(88)90253-X","article-title":"The vesicular stomatitis virus L protein possesses the mRNA methyltransferase activities","volume":"163","author":"N Hercyk","year":"1988","journal-title":"Virology"},{"issue":"2","key":"ppat.1009371.ref017","doi-asserted-by":"crossref","first-page":"515","DOI":"10.1128\/JVI.52.2.515-521.1984","article-title":"Aberrant polyadenylation by a vesicular stomatitis virus mutant is due to an altered L protein","volume":"52","author":"DM Hunt","year":"1984","journal-title":"J Virol"},{"issue":"6","key":"ppat.1009371.ref018","doi-asserted-by":"crossref","first-page":"1325","DOI":"10.1128\/JVI.12.6.1325-1335.1973","article-title":"L protein requirement for in vitro RNA synthesis by vesicular stomatitis virus","volume":"12","author":"SU Emerson","year":"1973","journal-title":"J Virol"},{"issue":"2","key":"ppat.1009371.ref019","doi-asserted-by":"crossref","first-page":"572","DOI":"10.1073\/pnas.66.2.572","article-title":"Ribonucleic acid synthesis of vesicular stomatitis virus, II. 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