Zaire Ebolavirus (EBOV) causes a severe feverish disease with high case fatality rates. Transcription of EBOV is dependent on the activity of the nucleocapsid protein VP30 which represents an essential viral transcription factor. Activity of VP30 is regulated via phosphorylation at six N-terminal serine residues. Recent data demonstrated that dynamic phosphorylation and dephosphorylation of serine residue 29 is essential for transcriptional support activity of VP30. To analyze the spatio/temporal dynamics of VP30 phosphorylation, we generated a peptide antibody recognizing specifically VP30 phosphorylated at serine 29. Using this antibody we could demonstrate that (i) the majority of VP30 molecules in EBOV-infected cells is dephosphorylated at the crucial position serine 29, (ii) both, VP30 phosphorylation and dephosphorylation take place in viral inclusion bodies that are induced by the nucleoprotein NP and (iii) NP influences the phosphorylation state of VP30.

扎伊尔埃博拉病毒（EBOV）导致严重的发烧性疾病，病死率很高。EBOV的转录取决于代表必需的病毒转录因子的核衣壳蛋白VP30的活性。VP30的活性通过六个N端丝氨酸残基的磷酸化。最新数据表明，丝氨酸残基29的动态磷酸化和去磷酸化对于VP30的转录支持活性至关重要。为了分析VP30磷酸化的时空动态，我们生成了一种肽抗体，专门识别在丝氨酸29处磷酸化的VP30。使用该抗体，我们可以证明（i）EBOV感染细胞中的大多数VP30分子在关键位置被去磷酸化丝氨酸29，（ii）VP30磷酸化和去磷酸化均发生在由核蛋白NP诱导的病毒包涵体中，并且（iii）NP影响VP30的磷酸化状态。