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Originally published as JGV in Press, 10.1099/vir.0.010660-0 on March 18, 2009 J Gen Virol 90 (2009), 1730-1733; DOI 10.1099/vir.0.010660-0

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Short Communication

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. Webster2,3 and Nikolai V. Kaverin1

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, 262 Danny Thomas Place, Memphis, TN 38105 3678, USA
3 Department of Pathology, University of Tennessee, Memphis, TN 38105, USA

Correspondence
Nikolai V. Kaverin
labphysvir{at}mail.ru

The locations of amino acid positions relevant to antigenic variation in the nucleoprotein (NP) of influenza virus are not conclusively known. We analysed 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 analysed by performing ELISA with monoclonal antibodies. Four amino acid residues were found to determine four different antibody-binding sites. When mapped in a 3D 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.

A supplementary table showing the primers used in this study is available with the online version of this paper.






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