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J Gen Virol 87 (2006), 3637-3642; DOI 10.1099/vir.0.82165-0

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© 2006 Society for General Microbiology

Short Communication

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

Ana Asenjo1, Enrique Calvo2 and Nieves Villanueva1

1 Centro Nacional de Microbiología, Instituto de Salud Carlos III, Crta Majadahonda-Pozuelo km 2, Majadahonda, 28220 Madrid, Spain
2 Unidad de Proteómica, Centro Nacional de Investigaciones Cardiovasculares (CNIC), Melchor Fernández de Almagro 3, 28029 Madrid, Spain

Correspondence
Nieves Villanueva
nvilla{at}isciii.es

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.




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T.-L. Tran, N. Castagne, V. Dubosclard, S. Noinville, E. Koch, M. Moudjou, C. Henry, J. Bernard, R. P. Yeo, and J.-F. Eleouet
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[Abstract] [Full Text] [PDF]




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