{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,5]],"date-time":"2026-10-05T18:09:29Z","timestamp":1791223769208,"version":"4.1.0"},"reference-count":44,"publisher":"American Society for Microbiology","issue":"13","license":[{"start":{"date-parts":[[2013,7,1]],"date-time":"2013-07-01T00:00:00Z","timestamp":1372636800000},"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":[[2013,7]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            The phosphoprotein (P) is virally encoded by the\n            <jats:named-content content-type=\"genus-species\">Rhabdoviridae<\/jats:named-content>\n            and\n            <jats:named-content content-type=\"genus-species\">Paramyxoviridae<\/jats:named-content>\n            in the order\n            <jats:named-content content-type=\"genus-species\">Mononegavirales<\/jats:named-content>\n            . P is a self-associated oligomer and forms complexes with the large viral polymerase protein (L), the nucleocapsid protein (N), and the assembled nucleocapsid. P from different viruses has shown structural diversities even though their essential functions are the same. We systematically mapped the domains in mumps virus (MuV) P and investigated their interactions with nucleocapsid-like particles (NLPs). Similar to other P proteins, MuV P contains N-terminal, central, and C-terminal domains with flexible linkers between neighboring domains. By pulldown assays, we discovered that in addition to the previously proposed nucleocapsid binding domain (residues 343 to 391), the N-terminal region of MuV P (residues 1 to 194) could also bind NLPs. Further analysis of binding kinetics was conducted using surface plasmon resonance. This is the first observation that both the N- and C-terminal regions of a negative-strand RNA virus P are involved in binding the nucleocapsid. In addition, we defined the oligomerization domain (P\n            <jats:sub>OD<\/jats:sub>\n            ) of MuV P as residues 213 to 277 and determined its crystal structure. The tetrameric MuV P\n            <jats:sub>OD<\/jats:sub>\n            is formed by one pair of long parallel \u03b1-helices with another pair in opposite orientation. Unlike the parallel orientation of each \u03b1-helix in the tetramer of Sendai virus P\n            <jats:sub>OD<\/jats:sub>\n            , this represents a novel orientation of a P\n            <jats:sub>OD<\/jats:sub>\n            where both the N- and the C-terminal domains are at either end of the tetramer. This is consistent with the observation that both the N- and the C-terminal domains are involved in binding the nucleocapsid.\n          <\/jats:p>","DOI":"10.1128\/jvi.00653-13","type":"journal-article","created":{"date-parts":[[2013,5,2]],"date-time":"2013-05-02T08:36:26Z","timestamp":1367483786000},"page":"7558-7568","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":69,"title":["Structural and Functional Characterization of the Mumps Virus Phosphoprotein"],"prefix":"10.1128","volume":"87","author":[{"given":"Robert","family":"Cox","sequence":"first","affiliation":[{"name":"Department of Microbiology, University of Alabama at Birmingham, Birmingham, Alabama, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Todd J.","family":"Green","sequence":"additional","affiliation":[{"name":"Department of Microbiology, University of Alabama at Birmingham, Birmingham, Alabama, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sangeetha","family":"Purushotham","sequence":"additional","affiliation":[{"name":"Department of Vision Sciences, University of Alabama at Birmingham, Birmingham, Alabama, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Champion","family":"Deivanayagam","sequence":"additional","affiliation":[{"name":"Department of Vision Sciences, University of Alabama at Birmingham, Birmingham, Alabama, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gregory J.","family":"Bedwell","sequence":"additional","affiliation":[{"name":"Department of Microbiology, University of Alabama at Birmingham, Birmingham, Alabama, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Peter E.","family":"Prevelige","sequence":"additional","affiliation":[{"name":"Department of Microbiology, University of Alabama at Birmingham, Birmingham, Alabama, 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