%0 Journal Article %A Asenjo, Ana %A Calvo, Enrique %A Villanueva, Nieves %T Phosphorylation of human respiratory syncytial virus P protein at threonine 108 controls its interaction with the M2-1 protein in the viral RNA polymerase complex %D 2006 %J Journal of General Virology, %V 87 %N 12 %P 3637-3642 %@ 1465-2099 %R https://doi.org/10.1099/vir.0.82165-0 %I Microbiology Society, %X The human respiratory syncytial virus (HRSV) P protein is phosphorylated, with different turnover rates, at several serine (S) and threonine (T) residues. The role of phosphothreonines in viral RNA synthesis was studied by using P protein substitution variants and the HRSV-based minigenome pM/SH. By using liquid chromatography coupled to ion-trap mass spectrometry, it was found that P protein T108 was phosphorylated by addition of a high-turnover phosphate group. This phosphorylation occurs in P protein expressed transiently and during HRSV infection. The results suggest that phosphorylation at P protein T108 affects M2-1 transcriptional activities, because this modification prevents interaction between the P and M2-1 proteins. Therefore, P protein phosphorylation–dephosphorylation at T108 could distinguish the role of the P protein in viral transcription and replication. %U https://www.microbiologyresearch.org/content/journal/jgv/10.1099/vir.0.82165-0