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protein). Although P protein is known to undergo phosphorylation by cellular kinases, the location and functions of the phosphorylation sites remains poorly defined. Here, we report the identification by mass-spectrometry (MS) of residues of P protein that are modified by phosphorylation in mammalian cells, including several novel sites. Analysis of P protein with phospho-mimetic and phospho-inhibitory mutations of three novel residues\/clusters that were commonly identified by MS (Ser48, Ser183\/187, Ser217\/219\/220) indicate that phosphorylation at each of these sites does not have a major influence on nuclear trafficking or antagonistic functions toward IFN signalling pathways. However, phosphorylation of Ser48 in the N-terminus of P protein impaired function in transcription\/replication and in the formation of replication structures that contain complexes of P and N proteins, suggestive of altered interactions of these proteins. The crystal structure of P protein containing the S48E phospho-mimetic mutation indicates that Ser48 phosphorylation facilitates the binding of residues 41\u201352 of P protein into the RNA-binding groove of non-RNA-bound N protein (N0), primarily through the formation of a salt bridge with Arg434 of N protein. These data indicate that Ser48 modification regulates the cycling of P-N0 chaperone complexes that deliver N protein to RNA to enable transcription\/replication, such that enhanced interaction due to S48E phospho-mimetic mutation reduces N protein delivery to the RNA, inhibiting subsequent transcription\/replication processes. These data are, to our knowledge, the first to implicate phosphorylation of RABV P protein in conserved replication functions of the P gene.<\/jats:p>","DOI":"10.3390\/v17081075","type":"journal-article","created":{"date-parts":[[2025,8,4]],"date-time":"2025-08-04T09:41:17Z","timestamp":1754300477000},"page":"1075","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":2,"title":["The Replication Function of Rabies Virus P Protein Is Regulated by a Novel Phosphorylation Site in the N-Terminal N Protein-Binding Region"],"prefix":"10.3390","volume":"17","author":[{"given":"Ericka","family":"Tudhope","sequence":"first","affiliation":[{"name":"Department of Microbiology, Biomedicine Discovery Institute, Monash University, Clayton, VIC 3800, Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2098-2462","authenticated-orcid":false,"given":"Camilla M.","family":"Donnelly","sequence":"additional","affiliation":[{"name":"Gulbali Institute, Charles Sturt University, Wagga Wagga, NSW 2678, Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-4220-3597","authenticated-orcid":false,"given":"Ashish","family":"Sethi","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Pharmacology, University of Melbourne, Parkville, VIC 3057, Australia"},{"name":"Australian Nuclear Science Technology Organisation, The Australian Synchrotron, 800 Blackburn Rd, Clayton, VIC 3168, Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-5571-6733","authenticated-orcid":false,"given":"Cassandra","family":"David","sequence":"additional","affiliation":[{"name":"Department of Microbiology, Biomedicine Discovery Institute, Monash University, Clayton, VIC 3800, Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nicholas","family":"Williamson","sequence":"additional","affiliation":[{"name":"The Bio21 Molecular Science and Biotechnology Institute, The University of Melbourne, Parkville, VIC 3057, Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-7925-7180","authenticated-orcid":false,"given":"Murray","family":"Stewart","sequence":"additional","affiliation":[{"name":"MRC Laboratory of Molecular Biology, Francis Crick Ave., Cambridge Biomedical Campus, Cambridge CB2 0QH, UK"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jade K.","family":"Forwood","sequence":"additional","affiliation":[{"name":"Gulbali Institute, Charles Sturt University, Wagga Wagga, NSW 2678, Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0323-449X","authenticated-orcid":false,"given":"Paul R.","family":"Gooley","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Pharmacology, University of Melbourne, Parkville, VIC 3057, Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-4516-3906","authenticated-orcid":false,"given":"Gregory W.","family":"Moseley","sequence":"additional","affiliation":[{"name":"Department of Microbiology, Biomedicine Discovery Institute, Monash University, Clayton, VIC 3800, Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2025,8,1]]},"reference":[{"key":"ref_1","unstructured":"WHO (2025, July 01). 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