The bulk of the phosphorylation of human respiratory syncytial virus phosphoprotein is not essential but modulates viral RNA transcription and replication.
The ability of variants of the human respiratory syncytial virus (HRSV) phosphoprotein (P protein) to support RNA transcription and replication has been studied by using HRSV-based subgenomic replicons. The serine residues normally phosphorylated in P during HRSV infection have been replaced by other residues. The results indicate that the bulk of phosphorylation of P (98%) is not essential for viral RNA transcription or replication but that phosphorylation can modulate these processes.
Villanueva
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N
Centro Nacional de Microbiologia, Instituto de Salud Carlos III, Carretera Majadahonda-Pozuelo Km2, Majadahonda, Madrid 28220, Spain. nvilla@isciii.es
Hardy
R
R
Asenjo
A
A
Yu
Q
Q
Wertz
G
G
D015707:HN Protein; D006801:Humans; D010750:Phosphoproteins / Q000378:metabolism*; D010766:Phosphorylation; D012333:RNA, Messenger / Q000235:genetics / Q000378:metabolism*; D012367:RNA, Viral / Q000235:genetics / Q000378:metabolism*; D012093:Replicon; D012136:Respiratory Syncytial Viruses / Q000235:genetics / Q000378:metabolism*; D014158:Transcription, Genetic; D014759:Viral Envelope Proteins; D014764:Viral Proteins / Q000378:metabolism*; D014779:Virus Replication
D015707:HN Protein; D010750:Phosphoproteins; D012333:RNA, Messenger; D012367:RNA, Viral; D014759:Viral Envelope Proteins; D014764:Viral Proteins; C116204:attachment protein G