@article{mbs:/content/journal/jgv/10.1099/vir.0.19370-0, author = "Stokes, H. L. and Easton, A. J. and Marriott, A. C.", title = "Chimeric pneumovirus nucleocapsid (N) proteins allow identification of amino acids essential for the function of the respiratory syncytial virus N protein", journal= "Journal of General Virology", year = "2003", volume = "84", number = "10", pages = "2679-2683", doi = "https://doi.org/10.1099/vir.0.19370-0", url = "https://www.microbiologyresearch.org/content/journal/jgv/10.1099/vir.0.19370-0", publisher = "Microbiology Society", issn = "1465-2099", type = "Journal Article", abstract = "The nucleocapsid (N) protein of the pneumovirus respiratory syncytial virus (RSV) is a major structural protein which encapsidates the RNA genome and is essential for replication and transcription of the RSV genome. The N protein of the related virus pneumonia virus of mice (PVM) is functionally unable to replace the RSV N protein in a minigenome replication assay. Using chimeric proteins, in which the immediate C-terminal part of the RSV N protein was replaced with the equivalent region of the PVM N protein, it was shown that six amino acid residues near the C terminus of the N protein (between residues 352–369) are essential for its function in replication and for the ability of the N protein to bind to the viral phosphoprotein, P.", }