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Published online ahead of print on 18 March 2009 as doi:10.1099/vir.0.010660-0
Journal of General Virology 2009;90:1730.

A more recent version of this article appeared on July 1, 2009 J Gen Virol (2009), DOI 10.1099/vir.0.010660-0
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Location of antigenic sites recognized by monoclonal antibodies in the influenza A virus nucleoprotein molecule

Natalia L Varich1, Konstantin S Kochergin-Nikitsky1, Evgeny V Usachev1, Olga V Usacheva1, Alexei G Prilipov1, Robert G Webster2 and Nikolai V Kaverin1,3

1 D. I. Ivanovsky Institute of Virology, Gamaleya Str. 16, 123098 Moscow, Russia;
2 Division of Virology, Department of Infectious Diseases, St. Jude Children's Research Hospital

3 E-mail: labphysvir{at}mail.ru

The locations of amino acid positions relevant to antigenic variation in the nucleoprotein (NP) of the influenza virus are not conclusively known. We analyzed the antigenic structure of influenza A virus NP by introducing site-specific mutations at amino acid positions presumed to be relevant for the differentiation of strain differences by anti-NP monoclonal antibodies. Mutant proteins were expressed in a prokaryotic system and analyzed by performing enzyme-linked immunosorbent assay with monoclonal antibodies. Four amino acid residues were found to determine four different antibody-binding sites. When mapped in a three-dimensional x-ray model of NP, the four antigenically relevant amino acid positions were found to be located in separate physical sites of the NP molecule.

Received 29 January 2009; accepted 18 March 2009.




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