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Regulated but not constitutive human respiratory syncytial virus (HRSV) P protein phosphorylation is essential for oligomerization
Author(s) -
Asenjo Ana,
Villanueva Nieves
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)01171-6
Subject(s) - phosphoprotein , phosphorylation , serine , virus , protein phosphorylation , transfection , chemistry , biology , microbiology and biotechnology , virology , biochemistry , protein kinase a , gene
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.