RT Journal Article SR Electronic(1) A1 Asenjo, Ana A1 Calvo, Enrique A1 Villanueva, NievesYR 2006 T1 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 JF Journal of General Virology, VO 87 IS 12 SP 3637 OP 3642 DO https://doi.org/10.1099/vir.0.82165-0 PB Microbiology Society, SN 1465-2099, AB 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., UL https://www.microbiologyresearch.org/content/journal/jgv/10.1099/vir.0.82165-0