Basse Vincent, Wang Yao, Rodrigues-Machado Carine, Henry Céline, Richard Charles-Adrien, Leyrat Cédric, Galloux Marie
Unité de Virologie et Immunologie Moléculaires (VIM), Université Paris-Saclay, INRAE, Jouy-en-Josas, France.
Institut de Génomique Fonctionnelle, Université de Montpellier, CNRS, INSERM, Montpellier, France.
J Biol Chem. 2025 Mar;301(3):108256. doi: 10.1016/j.jbc.2025.108256. Epub 2025 Feb 3.
The negative-sense RNA genome of respiratory syncytial virus (RSV) is encapsidated by the viral nucleoprotein N, forming a left-handed helical nucleocapsid which serves as template for the viral polymerase. Specific oligomerization of N along the viral genome necessitates a switch of conformation of N, from the neosynthesized monomeric and RNA-free N protein, named N, to N-RNA oligomers. Although the binding of the N-terminal part of RSV phosphoprotein P plays the role of chaperone to impair RNA binding to N, N-P interaction alone is not sufficient to prevent N oligomerization. Here, we explored the potential role of post translational modifications that could participate in the stability of N. Among the post translational modifications specifically identified on recombinant monomeric N, we validated the presence of a phosphorylation site on residue Y88 of N which modulates N oligomerization. Our results suggest that RSV N oligomerization depends on the regulation by post translational modifications.
呼吸道合胞病毒（RSV）的负链RNA基因组由病毒核蛋白N包裹，形成左手螺旋核衣壳，作为病毒聚合酶的模板。N沿病毒基因组的特异性寡聚化需要N的构象转换，从新合成的单体且无RNA的N蛋白（称为N0）转变为N-RNA寡聚体。尽管RSV磷蛋白P的N端部分的结合起到分子伴侣的作用，削弱RNA与N的结合，但单独的N-P相互作用不足以防止N寡聚化。在这里，我们探索了可能参与N稳定性的翻译后修饰的潜在作用。在重组单体N上特异性鉴定出的翻译后修饰中，我们验证了N的Y88残基上存在一个磷酸化位点，该位点调节N寡聚化。我们的结果表明，RSV N寡聚化取决于翻译后修饰的调控。
