Phosphorylation of the human respiratory syncytial virus N protein provokes a decrease in viral RNA synthesis.
When HEp-2 cells are infected by human respiratory syncytial virus (HRSV) its N protein becomes phosphorylated at tyrosine (Y) Y38, in a strictly regulated way. To determine how this phosphorylation affects nucleocapsid (NC) template activity during viral RNA synthesis, N protein variants were analysed in which Y38 and nearby Y residues were substituted by phenylalanine (F; Y23F, Y38F and Y69F) or aspartic acid (D; Y23D and Y38D). While the capacity of these proteins to form the NC and to interact with the P protein was maintained, their NC template activity was altered affecting distinctly viral transcription and replication of HRSV based minigenomes. Thus, Y38 phosphorylation of the HRSV N protein modulates NC template activity probably by altering the interactions of the monomeric components of the NC.
Centro Nacional de Microbiología (CNM), Instituto de Salud Carlos III (ISCIII), Crta. Majadahonda-Pozuelo km 2, Majadahonda, Madrid 28220, Spain.
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Asenjo
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Cuesta
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Vivo
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Villanueva
D019943:Amino Acid Substitution; D056945:Hep G2 Cells; D006801:Humans; D016297:Mutagenesis, Site-Directed; D050505:Mutant Proteins / Q000235:genetics / Q000378:metabolism; D019590:Nucleocapsid Proteins / Q000235:genetics / Q000378:metabolism*; D010766:Phosphorylation; D012367:RNA, Viral / Q000096:biosynthesis*; D018113:Respiratory Syncytial Virus, Human / Q000254:growth & development*; D014779:Virus Replication
D050505:Mutant Proteins; D019590:Nucleocapsid Proteins; D012367:RNA, Viral