Biochemical characterization of the respiratory syncytial virus P-P and P-N protein complexes and localization of the P protein oligomerization domain.

@article{Castagn2004BiochemicalCO,
  title={Biochemical characterization of the respiratory syncytial virus P-P and P-N protein complexes and localization of the P protein oligomerization domain.},
  author={Nathalie Castagn{\'e} and Alexandra Barbier and Julie L. Bernard and Human Rezaei and J. Y. Huet and C{\'e}line Henry and Bruno Da Costa and Jean-François El{\'e}ou{\"e}t},
  journal={The Journal of general virology},
  year={2004},
  volume={85 Pt 6},
  pages={1643-53}
}
The RNA-dependent RNA polymerase complex of respiratory syncytial virus (RSV) is composed of the large polymerase (L), the phosphoprotein (P), the nucleocapsid protein (N) and the co-factors M2-1 and M2-2. The P protein plays a central role within the replicase-transcriptase machinery, forming homo-oligomers and complexes with N and L. In order to study P-P and N-P complexes, and the role of P phosphorylation in these interactions, the human RSV P and N proteins were expressed in E. coli as His… CONTINUE READING