Chimeric pneumovirus nucleocapsid (N) proteins allow identification of amino acids essential for the function of the respiratory syncytial virus N protein

• Published in: Journal of general virology Vol. 84; no. 10; pp. 2679 - 2683
• Main Authors: Stokes, H. L, Easton, A. J, Marriott, A. C
• Format: Journal Article
• Language: English
• Published: England Soc General Microbiol 01-10-2003
• Subjects: Amino Acid Sequence; Amino Acids - metabolism; AN protein; Animals; AP protein; Humans; Mice; Molecular Sequence Data; Murine pneumonia virus - metabolism; N protein; Nucleocapsid Proteins - chemistry; Nucleocapsid Proteins - genetics; Nucleocapsid Proteins - metabolism; P protein; Phosphoproteins - metabolism; Pneumonia virus of mice; Recombinant Fusion Proteins - metabolism; Respiratory syncytial virus; Respiratory Syncytial Viruses - metabolism; Viral Proteins - chemistry; Viral Proteins - genetics; Viral Proteins - metabolism
• ISSN: 0022-1317; 1465-2099
• DOI: 10.1099/vir.0.19370-0

University of Warwick, Department of Biological Sciences, Coventry CV4 7AL, UK
Correspondence Tony Marriott a.c.marriott{at}warwick.ac.uk
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.
Present address: Department of Pathology & Microbiology, School of Medical Sciences, University of Bristol, University Walk, Bristol BS8 1TD, UK.