@article{mbs:/content/journal/jgv/10.1099/vir.0.82165-0, author = "Asenjo, Ana and Calvo, Enrique and Villanueva, Nieves", title = "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", journal= "Journal of General Virology", year = "2006", volume = "87", number = "12", pages = "3637-3642", doi = "https://doi.org/10.1099/vir.0.82165-0", url = "https://www.microbiologyresearch.org/content/journal/jgv/10.1099/vir.0.82165-0", publisher = "Microbiology Society", issn = "1465-2099", type = "Journal Article", abstract = "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.", }