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J Gen Virol. 2006 Dec;87(Pt 12):3637-42.

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.

Author information

1
Centro Nacional de MicrobiologĂ­a, Instituto de Salud Carlos III, Crta Majadahonda-Pozuelo km 2, Majadahonda, 28220 Madrid, Spain.

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.

PMID:
17098979
DOI:
10.1099/vir.0.82165-0
[Indexed for MEDLINE]

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