C-terminal phosphorylation of human respiratory syncytial virus P protein occurs mainly at serine residue 232.
To determine which human respiratory syncytial virus (HRSV) P protein serine residues are modified by cellular protein kinase(s), several mutated versions of P protein were expressed in the absence of other viral proteins. Mutations at serines 232 or 232 and 237 drastically reduced the extent of phosphorylation P protein in vivo. Serine 232 is the main site of modification and is also essential for in vitro phosphorylation by casein kinase II. Additional in vivo phosphorylation was also detected in the region containing serines 116, 117 and 119.
Servicio de Viroloía, Centro Nacional de Microbiología, Virología e Inmunología Sanitarias, Instituto de Salud Carlos III, Madrid, Spain.
M P
MP
Sánchez-Seco
J
J
Navarro
R
R
Martínez
N
N
Villanueva
D000595:Amino Acid Sequence; D001483:Base Sequence; D015707:HN Protein; D008969:Molecular Sequence Data; D009154:Mutation; D010766:Phosphorylation; D018113:Respiratory Syncytial Virus, Human / Q000737:chemistry*; D012694:Serine / Q000378:metabolism; D014759:Viral Envelope Proteins; D014764:Viral Proteins / Q000378:metabolism*
D015707:HN Protein; D014759:Viral Envelope Proteins; D014764:Viral Proteins; C116204:attachment protein G; D012694:Serine