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In rabies virus (RABV), the phosphoprotein (P-protein) isoform P3 localizes to nucleoli and inhibits rRNA biogenesis, whereas P1 lacks nucleolar targeting, even when forced into the nucleus. Here, we show that nucleolar targeting is an isoform- and phylogroup-specific property of lyssavirus P-proteins. Isoforms P3\u2013P5 accumulate in nucleoli, whereas P1 and P2 are excluded. Comparative analyses revealed that P3 nucleolar targeting is conserved in phylogroup I but absent in phylogroup II lyssaviruses. Co-immunoprecipitation assays identified conserved interactions with nucleolin and nucleophosmin (NPM1) but divergent binding to Treacle and nucleolar and coiled-body phosphoprotein 1 (NOLC1). These findings define nucleolar targeting as a gain-of-function of truncated P isoforms, demonstrate its conservation across phylogroup I lyssaviruses and suggest broader engagement with membraneless compartments, highlighting potential therapeutic vulnerabilities.<\/jats:p>","DOI":"10.1099\/jgv.0.002214","type":"journal-article","created":{"date-parts":[[2026,1,16]],"date-time":"2026-01-16T16:17:36Z","timestamp":1768580256000},"source":"Crossref","is-referenced-by-count":0,"title":["Nucleolar targeting of lyssavirus P-protein is isoform- and phylogroup-specific"],"prefix":"10.1099","volume":"107","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-4516-3906","authenticated-orcid":false,"given":"Gregory W.","family":"Moseley","sequence":"first","affiliation":[{"name":"Department of Microbiology, Biomedicine Discovery Institute, Monash University, Clayton, VIC, 3800, 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