Murray, J. and Loney, C. and Murphy, L. B. and Graham, S. and Yeo, R. P. (2001) 'Characterization of monoclonal antibodies raised against recombinant respiratory syncytial virus nucleocapsid (N) protein : identification of a region in the carboxy terminus of N involved in the interaction with P protein.', Virology., 289 (2). pp. 252-261.
To investigate structure and biological properties of the nucleocapsid (N) protein of respiratory syncytial virus (RSV), we have generated a panel of 16 monoclonal antibodies, raised against recombinant N protein, and epitope mapped seven of these to three antigenic sites (Site I aa 16–30; Site II aa 341–350; Site III aa 351–365). Characterization by immunofluorescence and by immunoprecipitation assay demonstrated that a monoclonal antibody to antigenic site I can detect N protein complexed with phospho (P) protein. Antibodies to antigenic sites II and III, which are adjacent to each other near the carboxyl terminus of the N protein, have distinct properties. A site III monoclonal antibody detected N protein in cytoplasmic inclusion bodies and in the cytosol, but not when N was complexed to P protein, while the site II antibody reacted with N protein in the nucleocapsid fraction but did not detect cytosolic N protein. Further investigation into the reactivities of the antibodies after binding of P to N in vitro demonstrated that antigenic sites II and III were blocked by the interaction, indicating an involvement for the carboxy domain of N in the N–P interaction. This was confirmed by the ability of peptides from the carboxy terminus of N to inhibit the N–P interaction in vitro.
|Keywords:||RSV, Nucleocapsid, N–P interaction, Monoclonal antibodies, Peptides, P binding.|
|Full text:||Full text not available from this repository.|
|Publisher Web site:||http://dx.doi.org/10.1006/viro.2001.1150|
|Record Created:||15 May 2007|
|Last Modified:||08 Apr 2009 16:31|
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