Crystal structure of the essential transcription antiterminator M2-1 protein of human respiratory syncytial virus and implications of its phosphorylation
Tanner SJ., Ariza A., Richard C-A., Kyle HF., Dods RL., Blondot M-L., Wu W., Trincão J., Trinh CH., Hiscox JA., Carroll MW., Silman NJ., Eléouët J-F., Edwards TA., Barr JN.
SignificanceHuman respiratory syncytial virus (HRSV) is the leading cause of lower respiratory tract illness in young children; however, no vaccine exists and current immunoprophylaxis regimes are both expensive and incompletely protective. We report the crystal structure of the HRSV M2-1 transcription factor that is essential for virus gene expression and thus growth. This structure reveals how M2-1 forms an extremely stable tetramer and has allowed us to pinpoint the location of critical regions that regulate M2-1 activity, providing insight into its function. This structure may represent a potent target for new antiviral compounds.