Regulated but not constitutive human respiratory syncytial virus (HRSV) P protein phosphorylation is essential for oligomerization

FEBS Letters

Villanueva, Nieves¹  Asenjo, Ana¹ 

[1] Centro Nacional de Microbiologia (C.N.M), Instituto de Salud Carlos III (ISCIII), Carretera Majadahonda-Pozuelo Km 2, Majadahonda, Madrid 28220, Spain

关键词: Human respiratory syncytial virus;    P protein;    Phosphorylation;    Oligomerization;   

DOI  :  10.1016/S0014-5793(00)01171-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Purified human respiratory syncytial virus (HRSV) P phosphoprotein from transfected HEp-2 cells is able to oligomerize forming tetramers. The bulk of constitutive P protein phosphorylation (99.8%) (serine residues 116, 117, 119, 232 and 237) can be removed without affecting protein oligomerization. However, dephosphorylated P protein, produced in bacteria, is unable to oligomerize. This difference can be explained by a transient P protein phosphorylation, detected in HEp-2 cells, that could be essential for P protein oligomerization.

【 授权许可】

Unknown