{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,19]],"date-time":"2026-09-19T12:36:01Z","timestamp":1789821361520,"version":"4.0.1"},"reference-count":43,"publisher":"American Society for Microbiology","issue":"21","license":[{"start":{"date-parts":[[2015,11,1]],"date-time":"2015-11-01T00:00:00Z","timestamp":1446336000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["J Virol"],"published-print":{"date-parts":[[2015,11]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            The mumps virus (MuV) genome encodes a phosphoprotein (P) that is important for viral RNA synthesis. P forms the viral RNA-dependent RNA polymerase with the large protein (L). P also interacts with the viral nucleoprotein (NP) and self-associates to form a homotetramer. The P protein consists of three domains, the N-terminal domain (P\n            <jats:sub>N<\/jats:sub>\n            ), the oligomerization domain (P\n            <jats:sub>O<\/jats:sub>\n            ), and the C-terminal domain (P\n            <jats:sub>C<\/jats:sub>\n            ). While P\n            <jats:sub>N<\/jats:sub>\n            is known to relax the NP-bound RNA genome, the roles of P\n            <jats:sub>O<\/jats:sub>\n            and P\n            <jats:sub>C<\/jats:sub>\n            are not clear. In this study, we investigated the roles of P\n            <jats:sub>O<\/jats:sub>\n            and P\n            <jats:sub>C<\/jats:sub>\n            in viral RNA synthesis using mutational analysis and a minigenome system. We found that P\n            <jats:sub>N<\/jats:sub>\n            and P\n            <jats:sub>C<\/jats:sub>\n            functions can be\n            <jats:italic>trans<\/jats:italic>\n            -complemented. However, this complementation requires P\n            <jats:sub>O<\/jats:sub>\n            , indicating that P\n            <jats:sub>O<\/jats:sub>\n            is essential for P function. Using this\n            <jats:italic>trans<\/jats:italic>\n            -complementation system, we found that P forms parallel dimers (P\n            <jats:sub>N<\/jats:sub>\n            to P\n            <jats:sub>N<\/jats:sub>\n            and P\n            <jats:sub>C<\/jats:sub>\n            to P\n            <jats:sub>C<\/jats:sub>\n            ). Furthermore, we found that residues R231, K238, K253, and K260 in P\n            <jats:sub>O<\/jats:sub>\n            are critical for P's functions. We identified P\n            <jats:sub>C<\/jats:sub>\n            to be the domain that interacts with L. These results provide structure-function insights into the role of MuV P.\n          <\/jats:p>\n          <jats:p>\n            <jats:bold>IMPORTANCE<\/jats:bold>\n            MuV, a paramyxovirus, is an important human pathogen. The P protein of MuV is critical for viral RNA synthesis. In this work, we established a novel minigenome system that allows the domains of P to be complemented in\n            <jats:italic>trans<\/jats:italic>\n            . Using this system, we confirmed that MuV P forms parallel dimers. An understanding of viral RNA synthesis will allow the design of better vaccines and the development of antivirals.\n          <\/jats:p>","DOI":"10.1128\/jvi.01719-15","type":"journal-article","created":{"date-parts":[[2015,8,27]],"date-time":"2015-08-27T02:09:53Z","timestamp":1440641393000},"page":"11002-11010","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":17,"title":["Oligomerization of Mumps Virus Phosphoprotein"],"prefix":"10.1128","volume":"89","author":[{"given":"Adrian","family":"Pickar","sequence":"first","affiliation":[{"name":"Department of Infectious Diseases, College of Veterinary Medicine, University of Georgia, Athens, Georgia, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Andrew","family":"Elson","sequence":"additional","affiliation":[{"name":"Department of Infectious Diseases, College of Veterinary Medicine, University of Georgia, Athens, Georgia, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yang","family":"Yang","sequence":"additional","affiliation":[{"name":"Department of Infectious Diseases, College of Veterinary Medicine, University of Georgia, Athens, Georgia, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Pei","family":"Xu","sequence":"additional","affiliation":[{"name":"Department of Infectious Diseases, College of Veterinary Medicine, University of Georgia, Athens, Georgia, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ming","family":"Luo","sequence":"additional","affiliation":[{"name":"Department of Chemistry, Georgia State University, Atlanta, Georgia, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Biao","family":"He","sequence":"additional","affiliation":[{"name":"Department of Infectious Diseases, College of Veterinary Medicine, University of Georgia, Athens, Georgia, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","first-page":"1381","volume-title":"Fields virology","author":"Carbone KM","year":"2001","unstructured":"Carbone KM, Wolinsky JS. 2001. 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