{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,25]],"date-time":"2026-02-25T08:18:10Z","timestamp":1772007490511,"version":"3.50.1"},"reference-count":77,"publisher":"MDPI AG","issue":"11","license":[{"start":{"date-parts":[[2024,11,4]],"date-time":"2024-11-04T00:00:00Z","timestamp":1730678400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"French ANR","award":["ANR-07-001-01(ANRAGE)"],"award-info":[{"award-number":["ANR-07-001-01(ANRAGE)"]}]},{"name":"postdoctoral fellowships from Joseph Fourier University","award":["ANR-07-001-01(ANRAGE)"],"award-info":[{"award-number":["ANR-07-001-01(ANRAGE)"]}]},{"name":"ANR program","award":["ANR-07-001-01(ANRAGE)"],"award-info":[{"award-number":["ANR-07-001-01(ANRAGE)"]}]},{"name":"French Minist\u00e8re de l\u2019Education Nationale, de la Recherche et de la Technologie","award":["ANR-07-001-01(ANRAGE)"],"award-info":[{"award-number":["ANR-07-001-01(ANRAGE)"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Viruses"],"abstract":"<jats:p>The dynamic interplay between a multimeric phosphoprotein (P) and polymeric nucleoprotein (N) in complex with the viral RNA is at the heart of the functioning of the RNA-synthesizing machine of negative-sense RNA viruses of the order Mononegavirales. P multimerization and N phosphorylation are often cited as key factors in regulating these interactions, but a detailed understanding of the molecular mechanisms is not yet available. Working with recombinant rabies virus (RABV) N and P proteins and using mainly surface plasmon resonance, we measured the binding interactions of full-length P dimers and of two monomeric fragments of either circular or linear N-RNA complexes, and we analyzed the equilibrium binding isotherms using different models. We found that RABV P binds with nanomolar affinity to both circular and linear N-RNA complexes and that the dimerization of P protein enhances the binding affinity by 15\u201330-fold as compared to the monomeric fragments, but less than expected for a bivalent ligand, in which the binding domains are connected by a flexible linker. We also showed that the phosphorylation of N at Ser389 creates high-affinity sites on the polymeric N-RNA complex that enhance the binding affinity of P by a factor of about 360.<\/jats:p>","DOI":"10.3390\/v16111735","type":"journal-article","created":{"date-parts":[[2024,11,4]],"date-time":"2024-11-04T09:52:54Z","timestamp":1730713974000},"page":"1735","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":4,"title":["Dimerization of Rabies Virus Phosphoprotein and Phosphorylation of Its Nucleoprotein Enhance Their Binding Affinity"],"prefix":"10.3390","volume":"16","author":[{"suffix":"Jr.","given":"Euripedes de Almeida","family":"Ribeiro","sequence":"first","affiliation":[{"name":"Institut de Biologie Structurale, Universit\u00e9 Grenoble Alpes, CEA, CNRS, 38000 Grenoble, France"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0189-0562","authenticated-orcid":false,"given":"C\u00e9dric","family":"Leyrat","sequence":"additional","affiliation":[{"name":"Institut de Biologie Structurale, Universit\u00e9 Grenoble Alpes, CEA, CNRS, 38000 Grenoble, France"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9865-2864","authenticated-orcid":false,"given":"Francine C. A.","family":"G\u00e9rard","sequence":"additional","affiliation":[{"name":"Institut de Biologie Structurale, Universit\u00e9 Grenoble Alpes, CEA, CNRS, 38000 Grenoble, France"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8677-2110","authenticated-orcid":false,"given":"Marc","family":"Jamin","sequence":"additional","affiliation":[{"name":"Institut de Biologie Structurale, Universit\u00e9 Grenoble Alpes, CEA, CNRS, 38000 Grenoble, France"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"1968","published-online":{"date-parts":[[2024,11,4]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","unstructured":"Tarantola, A. (2017). Four Thousand Years of Concepts Relating to Rabies in Animals and Humans, Its Prevention and Its Cure. Trop. Med. Infect. Dis., 2.","DOI":"10.3390\/tropicalmed2020005"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"409","DOI":"10.20506\/rst.37.2.2811","article-title":"Rabies control in Europe: An overview of past, current and future strategies","volume":"37","author":"Muller","year":"2018","journal-title":"Rev. Sci. Tech."},{"key":"ref_3","first-page":"421","article-title":"Rabies control in North America\u2014Past, present and future","volume":"37","year":"2018","journal-title":"Rev. Sci. Tech."},{"key":"ref_4","doi-asserted-by":"crossref","unstructured":"Hampson, K., Coudeville, L., Lembo, T., Sambo, M., Kieffer, A., Attlan, M., Barrat, J., Blanton, J.D., Briggs, D.J., and Cleaveland, S. (2015). Estimating the global burden of endemic canine rabies. PLoS Negl. Trop. Dis., 9.","DOI":"10.1371\/journal.pntd.0003786"},{"key":"ref_5","unstructured":"(2024, July 15). WHO Rabies\u2014Fact Sheet. Available online: https:\/\/www.who.int\/news-room\/fact-sheets\/detail\/rabies."},{"key":"ref_6","first-page":"360","article-title":"Re-evaluating the burden of rabies in Africa and Asia","volume":"83","author":"Knobel","year":"2005","journal-title":"Bull. World Health Organ."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"481","DOI":"10.2217\/17460794.3.5.481","article-title":"Concepts in the pathogenesis of rabies","volume":"3","author":"Dietzschold","year":"2008","journal-title":"Future Virol."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"51","DOI":"10.1038\/nrmicro2260","article-title":"The cell biology of rabies virus: Using stealth to reach the brain","volume":"8","author":"Schnell","year":"2010","journal-title":"Nat. Rev. Microbiol."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"17091","DOI":"10.1038\/nrdp.2017.91","article-title":"Rabies","volume":"3","author":"Fooks","year":"2017","journal-title":"Nat. Rev. Dis. Primers"},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"241","DOI":"10.1038\/nrmicro.2018.11","article-title":"The spread and evolution of rabies virus: Conquering new frontiers","volume":"16","author":"Fisher","year":"2018","journal-title":"Nat. Rev. Microbiol."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"210","DOI":"10.1016\/j.molmed.2004.03.003","article-title":"Vesicular stomatitis virus: Re-inventing the bullet","volume":"10","author":"Litchy","year":"2004","journal-title":"Trends Mol. Med."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"275","DOI":"10.1007\/s10540-007-9054-z","article-title":"Reviewing Chandipura: A Vesiculovirus in Human Epidemics","volume":"27","author":"Basak","year":"2007","journal-title":"Biosci. Rep."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"264","DOI":"10.1016\/S0966-842X(03)00120-3","article-title":"Plant and animal rhabdovirus host range: A bug\u2019s view","volume":"11","author":"Hogenhout","year":"2003","journal-title":"Trends Microbiol."},{"key":"ref_14","first-page":"2321","article-title":"The order Mononegavirales","volume":"142","author":"Pringle","year":"1997","journal-title":"Arch. Virol."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"3023","DOI":"10.1007\/s00705-020-04731-2","article-title":"2020 taxonomic update for phylum Negarnaviricota (Riboviria: Orthornavirae), including the large orders Bunyavirales and Mononegavirales","volume":"165","author":"Kuhn","year":"2020","journal-title":"Arch. Virol."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"360","DOI":"10.1126\/science.1125280","article-title":"Crystal structure of the rabies virus nucleoprotein-RNA complex","volume":"313","author":"Albertini","year":"2006","journal-title":"Science"},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"e01508-16","DOI":"10.1128\/JVI.01508-16","article-title":"An In Vitro RNA Synthesis Assay for Rabies Virus Defines Ribonucleoprotein Interactions Critical for Polymerase Activity","volume":"91","author":"Morin","year":"2017","journal-title":"J. Virol."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"978","DOI":"10.1016\/j.jmb.2009.03.061","article-title":"Modular organization of rabies virus phosphoprotein","volume":"388","author":"Ribeiro","year":"2009","journal-title":"J. Mol. Biol."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"707","DOI":"10.1128\/jvi.69.2.707-712.1995","article-title":"Translation initiation at alternate in-frame AUG codons in the rabies virus phosphoprotein mRNA Is mediated by a ribosomal leaky scanning mechanism","volume":"69","author":"Chenik","year":"1995","journal-title":"J. Virol."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"4959","DOI":"10.1016\/j.jmb.2019.10.011","article-title":"The LC8-RavP ensemble Structure Evinces A Role for LC8 in Regulating Lyssavirus Polymerase Functionality","volume":"431","author":"Jespersen","year":"2019","journal-title":"J. Mol. Biol."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"111949","DOI":"10.1016\/j.celrep.2022.111949","article-title":"Rabies virus P protein binds to TBK1 and interferes with the formation of innate immunity-related liquid condensates","volume":"42","author":"Scrima","year":"2023","journal-title":"Cell Rep."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"1089","DOI":"10.1292\/jvms.16-0092","article-title":"The importance of immune evasion in the pathogenesis of rabies virus","volume":"78","author":"Ito","year":"2016","journal-title":"J. Vet. Med. Sci."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"14411","DOI":"10.1128\/JVI.79.22.14411-14420.2005","article-title":"Rabies virus P protein interacts with STAT1 and inhibits interferon signal transduction pathways","volume":"79","author":"Vidy","year":"2005","journal-title":"J. Virol."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"10328","DOI":"10.1021\/bi7007799","article-title":"Unphosphorylated Rhabdoviridae phosphoproteins form elongated dimers in solution","volume":"46","author":"Ribeiro","year":"2007","journal-title":"Biochemistry"},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"3707","DOI":"10.1128\/JVI.02557-09","article-title":"Structure of the dimerization domain of the rabies virus phosphoprotein","volume":"84","author":"Ivanov","year":"2010","journal-title":"J. Virol."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"819","DOI":"10.1016\/j.jmb.2004.08.071","article-title":"Structure and function of the C-terminal domain of the polymerase cofactor of rabies virus","volume":"343","author":"Mavrakis","year":"2004","journal-title":"J. Mol. Biol."},{"key":"ref_27","doi-asserted-by":"crossref","unstructured":"G\u00e9rard, F.C.A., Bourhis, J.M., Mas, C., Branchard, A., Vu, D.D., Varhoshkova, S., Leyrat, C., and Jamin, M. (2022). Structure and Dynamics of the Unassembled Nucleoprotein of Rabies Virus in Complex with Its Phosphoprotein Chaperone Module. Viruses, 14.","DOI":"10.3390\/v14122813"},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"406","DOI":"10.1006\/viro.2002.1748","article-title":"Isolation and characterisation of the rabies virus N degrees-P complex produced in insect cells","volume":"305","author":"Mavrakis","year":"2003","journal-title":"Virology"},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"2683","DOI":"10.1099\/0022-1317-70-10-2683","article-title":"Vesicular Stomatitis Virus RNA Replication: A Role for the NS Protein","volume":"70","author":"Howard","year":"1989","journal-title":"J. Gen. Virol."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"2658","DOI":"10.1128\/jvi.62.8.2658-2664.1988","article-title":"Complex Formation with Vesicular Stomatitis Virus Phosphoprotein NS prevents Binding of Nucleocapsid Protein N to Nonspecific RNA","volume":"62","author":"Masters","year":"1988","journal-title":"J. Virol."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"422","DOI":"10.1016\/j.virol.2006.01.030","article-title":"Rabies virus chaperone: Identification of the phosphoprotein peptide that keeps nucleoprotein soluble and free from non-specific RNA","volume":"349","author":"Mavrakis","year":"2006","journal-title":"Virology"},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"2099","DOI":"10.1073\/pnas.1918809117","article-title":"Structure of a rabies virus polymerase complex from electron cryo-microscopy","volume":"117","author":"Horwitz","year":"2020","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"558","DOI":"10.1016\/j.jmb.2009.09.042","article-title":"Binding of rabies virus polymerase cofactor to recombinant circular nucleoprotein-RNA complexes","volume":"394","author":"Ribeiro","year":"2009","journal-title":"J. Mol. Biol."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"e00111-22","DOI":"10.1128\/jvi.00111-22","article-title":"Molecular Basis of Functional Effects of Phosphorylation of the C-Terminal Domain of the Rabies Virus P Protein","volume":"96","author":"Zhan","year":"2022","journal-title":"J. Virol."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"58","DOI":"10.1038\/s41467-017-00102-9","article-title":"Negri bodies are viral factories with properties of liquid organelles","volume":"8","author":"Nikolic","year":"2017","journal-title":"Nat. Commun."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"7948","DOI":"10.1128\/JVI.00554-09","article-title":"Functional Characterization of Negri Bodies (NBs) in Rabies Virus-Infected Cells: Evidence that NBs Are Sites of Viral Transcription and Replication","volume":"83","author":"Lahaye","year":"2009","journal-title":"J. Virol."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"2808","DOI":"10.1128\/JVI.80.6.2808-2814.2006","article-title":"Crystal structure of the oligomerization domain of the phosphoprotein of vesicular stomatitis virus","volume":"80","author":"Ding","year":"2006","journal-title":"J. Virol."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"2470","DOI":"10.1016\/j.bpj.2020.04.010","article-title":"Structural Description of the Nipah Virus Phosphoprotein and Its Interaction with STAT1","volume":"118","author":"Jensen","year":"2020","journal-title":"Biophys. J."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"99","DOI":"10.1006\/viro.1999.0066","article-title":"On the domain structure and the polymerization state of the sendai virus P protein","volume":"266","author":"Tarbouriech","year":"2000","journal-title":"Virology"},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"e01085-16","DOI":"10.1128\/JVI.01085-16","article-title":"Crystal Structure of the Marburg Virus VP35 Oligomerization Domain","volume":"91","author":"Bruhn","year":"2017","journal-title":"J. Virol."},{"key":"ref_41","doi-asserted-by":"crossref","unstructured":"Leyrat, C., Renner, M., Harlos, K., and Grimes, J.M. (2013). Solution and crystallographic structures of the central region of the phosphoprotein from human metapneumovirus. PLoS ONE, 8.","DOI":"10.1371\/journal.pone.0080371"},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"130","DOI":"10.1006\/viro.1996.0359","article-title":"Reexamination of the Sendai virus P protein domains required for RNA synthesis: A possible supplemental role for the P protein","volume":"221","author":"Curran","year":"1996","journal-title":"Virology"},{"key":"ref_43","doi-asserted-by":"crossref","unstructured":"Bourhis, J.M., Yabukarski, F., Communie, G., Schneider, R., Volchkova, V.A., Freneat, M., Gerard, F.C., Ducournau, C., Mas, C., and Tarbouriech, N. (2022). Structural Dynamics of the C-terminal X Domain of Nipah and Hendra Viruses Controls the Attachment to the C-terminal Tail of the Nucleocapsid Protein. J. Mol. Biol., 434.","DOI":"10.1016\/j.jmb.2022.167551"},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"246","DOI":"10.1016\/0042-6822(73)90413-3","article-title":"Phosphoproteins, structural components of rhabdoviruses","volume":"52","author":"Sokol","year":"1973","journal-title":"Virology"},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"1661","DOI":"10.1128\/JVI.73.2.1661-1664.1999","article-title":"Phosphorylation of rabies virus nucleoprotein regulates viral RNA transcription and replication by modulating leader RNA encapsidation","volume":"73","author":"Yang","year":"1999","journal-title":"J. Virol."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"4153","DOI":"10.1128\/JVI.76.9.4153-4161.2002","article-title":"Both viral transcription and replication are reduced when the rabies virus nucleoprotein is not phosphorylated","volume":"76","author":"Wu","year":"2002","journal-title":"J. Virol."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"486","DOI":"10.1016\/0042-6822(90)90346-S","article-title":"Expression, characterization, and purification of a phosphorylated rabies nucleoprotein synthesized in insect cells by baculovirus vectors","volume":"178","author":"Harris","year":"1990","journal-title":"Virology"},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1016\/0168-1702(87)90023-2","article-title":"Localization and immunological characterization of antigenic domains of the rabies virus internal N and NS proteins","volume":"8","author":"Dietzschold","year":"1987","journal-title":"Virus Res."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"333","DOI":"10.1016\/S0006-291X(03)00594-1","article-title":"Rabies virus nucleoprotein is phosphorylated by cellular casein kinase II","volume":"304","author":"Wu","year":"2003","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"395","DOI":"10.1006\/viro.1999.9962","article-title":"Nucleocapsid formation and\/or subsequent conformational change of rabies virus nucleoprotein (N) is a prerequisite step for acquiring the phosphatase-sensitive epitope of monoclonal antibody 5-2-26","volume":"263","author":"Kawai","year":"1999","journal-title":"Virology"},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"399","DOI":"10.1111\/j.1348-0421.2004.tb03529.x","article-title":"Association of rabies virus nominal phosphoprotein (P) with viral nucleocapsid (NC) is enhanced by phosphorylation of the viral nucleoprotein (N)","volume":"48","author":"Toriumi","year":"2004","journal-title":"Microbiol. Immunol."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"182","DOI":"10.1016\/j.jmb.2012.07.003","article-title":"Ensemble structure of the modular and flexible full-length vesicular stomatitis virus phosphoprotein","volume":"423","author":"Leyrat","year":"2012","journal-title":"J. Mol. Biol."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"1948","DOI":"10.1021\/bi00859a010","article-title":"Spectroscopic determination of tryptophan and tyrosine in proteins","volume":"6","author":"Edelhoch","year":"1967","journal-title":"Biochemistry"},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"129","DOI":"10.1016\/j.jsb.2006.10.011","article-title":"Isolation and crystallization of a unique size category of recombinant Rabies virus Nucleoprotein-RNA rings","volume":"158","author":"Albertini","year":"2007","journal-title":"J. Struct. Biol."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"4046","DOI":"10.1073\/pnas.78.7.4046","article-title":"On the attribution and additivity of binding energies","volume":"78","author":"Jencks","year":"1991","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"469","DOI":"10.1016\/0022-2836(74)90031-X","article-title":"Theoretical aspects of DNA-Protein Interactions: Co-operative and non-co-operative binding of large ligands to a one-dimensional homogeneous lattice","volume":"86","author":"McGhee","year":"1974","journal-title":"J. Mol. Biol."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"367","DOI":"10.1006\/jmbi.1994.0091","article-title":"High-affinity Antigen Binding by Chelating Recombinant Antibodies (CRAbs)","volume":"246","author":"Neri","year":"1995","journal-title":"J. Mol. Biol."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"341","DOI":"10.1016\/0019-2791(72)90097-3","article-title":"The influence of polyvalency on the binding properties of antibodies","volume":"9","author":"Crothers","year":"1972","journal-title":"Immunochemistry"},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1101\/gad.10.1.27","article-title":"Oct-1 POU domain-DNA interactions: Cooperative binding of isolated subdomams and effects of covalent linkage","volume":"10","author":"Klemm","year":"1996","journal-title":"Genes Dev."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"6763","DOI":"10.1021\/jp011355n","article-title":"Loops in Proteins Can Be Modeled as Worm-Like Chains","volume":"105","author":"Zhou","year":"2001","journal-title":"J. Phys. Chem. B"},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/S0022-2836(03)00372-3","article-title":"Quantitative Account of the Enhanced Affinity of Two Linked scFvs Specific for Different Epitopes on the Same Antigen","volume":"329","author":"Zhou","year":"2003","journal-title":"J. Mol. Biol."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"9613","DOI":"10.1128\/JVI.75.20.9613-9622.2001","article-title":"Functional interaction map of lyssavirus phosphoprotein: Identification of the minimal transcription domains","volume":"75","author":"Jacob","year":"2001","journal-title":"J. Virol."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"e01789-19","DOI":"10.1128\/JVI.01789-19","article-title":"Vesicular Stomatitis Virus Phosphoprotein Dimerization Domain Is Dispensable for Virus Growth","volume":"94","author":"Jamin","year":"2020","journal-title":"J. Virol."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"e00115-20","DOI":"10.1128\/JVI.00115-20","article-title":"Oligomerization of the Vesicular Stomatitis Virus Phosphoprotein Is Dispensable for mRNA Synthesis but Facilitates RNA Replication","volume":"94","author":"Bloyet","year":"2020","journal-title":"J. Virol."},{"key":"ref_65","doi-asserted-by":"crossref","unstructured":"Nevers, Q., Scrima, N., Glon, D., Le Bars, R., Decombe, A., Garnier, N., Ouldali, M., Lagaudriere-Gesbert, C., Blondel, D., and Albertini, A. (2022). Properties of rabies virus phosphoprotein and nucleoprotein biocondensates formed in vitro and in cellulo. PLoS Pathog., 18.","DOI":"10.1371\/journal.ppat.1011022"},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"598","DOI":"10.1128\/jvi.54.2.598-607.1985","article-title":"Mass and molecular composition of vesicular stomatitis virus: A scanning transmission electron microscopy analysis","volume":"54","author":"Thomas","year":"1985","journal-title":"J. Virol."},{"key":"ref_67","doi-asserted-by":"crossref","unstructured":"Zaccai, N., Serdyuk, I.N., and Zaccai, G. (2017). Methods in Molecular Biophysics\u2014Structure, Dynamics, Function for Biology and Medicine, Cambridge University Press. [2nd ed.].","DOI":"10.1017\/9781107297227"},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"7199","DOI":"10.1128\/JVI.73.9.7199-7209.1999","article-title":"Transcript initiation and 5\u2019-end modifications are separable events during vesicular stomatitis virus transcription","volume":"73","author":"Stillman","year":"1999","journal-title":"J. Virol."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"1320","DOI":"10.1038\/emboj.2011.483","article-title":"Mechanism of RNA synthesis initiation by the vesicular stomatitis virus polymerase","volume":"31","author":"Morin","year":"2012","journal-title":"Embo J."},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"463","DOI":"10.1016\/j.virol.2003.10.031","article-title":"Viral RNA polymerase scanning and the gymnastics of Sendai virus RNA synthesis","volume":"318","author":"Kolakofsky","year":"2004","journal-title":"Virology"},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"337","DOI":"10.1016\/S0167-4781(02)00462-1","article-title":"Transcriptional control of the RNA-dependent RNA polymerase of vesicular stomatitis virus","volume":"1577","author":"Barr","year":"2002","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"2895","DOI":"10.1099\/0022-1317-82-12-2895","article-title":"Sendai virus genome synthesis and assembly are coupled: A possible mechanism to promote viral RNA polymerase processivity","volume":"82","author":"Gubbay","year":"2001","journal-title":"J. Gen. Virol."},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"6900","DOI":"10.1128\/JVI.79.11.6900-6908.2005","article-title":"Dynamics of viral RNA synthesis during measles virus infection","volume":"79","author":"Plumet","year":"2005","journal-title":"J. Virol."},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1007\/s12250-019-00157-6","article-title":"Proteomic Profiling of Purified Rabies Virus Particles","volume":"35","author":"Zhang","year":"2020","journal-title":"Virol. Sin."},{"key":"ref_75","doi-asserted-by":"crossref","unstructured":"Richard, C.A., Rincheval, V., Lassoued, S., Fix, J., Cardone, C., Esneau, C., Nekhai, S., Galloux, M., Rameix-Welti, M.A., and Sizun, C. (2018). RSV hijacks cellular protein phosphatase 1 to regulate M2-1 phosphorylation and viral transcription. PLoS Pathog., 14.","DOI":"10.1371\/journal.ppat.1006920"},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"2133","DOI":"10.1099\/vir.0.032342-0","article-title":"Determination of a phosphorylation site in Nipah virus nucleoprotein and its involvement in virus transcription","volume":"92","author":"Huang","year":"2011","journal-title":"J. Gen. Virol."},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"136","DOI":"10.1016\/j.molcel.2017.11.034","article-title":"The Ebola Virus Nucleoprotein Recruits the Host PP2A-B56 Phosphatase to Activate Transcriptional Support Activity of VP30","volume":"69","author":"Kruse","year":"2018","journal-title":"Mol. 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