Centro Nacional de Microbiología (CNM), Instituto de Salud Carlos III (ISCIII), Crta. Majadahonda-Pozuelo km 2, Majadahonda, Madrid 28220, Spain.
Virus Res. 2012 Jan;163(1):396-400. doi: 10.1016/j.virusres.2011.10.004. Epub 2011 Oct 13.
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.
当 Hep-2 细胞感染人类呼吸道合胞病毒（HRSV）时，其 N 蛋白会在酪氨酸（Y）Y38 处发生严格调控的磷酸化。为了确定这种磷酸化如何影响病毒 RNA 合成过程中的核衣壳（NC）模板活性，分析了 N 蛋白的变体，其中 Y38 和附近的 Y 残基被苯丙氨酸（F；Y23F、Y38F 和 Y69F）或天冬氨酸（D；Y23D 和 Y38D）取代。虽然这些蛋白质形成 NC 和与 P 蛋白相互作用的能力得以维持，但它们的 NC 模板活性发生了改变，明显影响了基于 HRSV 小基因的 minigenomes 的病毒转录和复制。因此，HRSV N 蛋白的 Y38 磷酸化通过改变 NC 单体成分的相互作用来调节 NC 模板活性。
