Abstract:
:Abstract Influenza virus nucleoprotein (NP) binds to the viral genome RNA and forms the internal ribonucleoprotein complex of the virus particle. Avian and human influenza virus NP have characteristic differences at several amino acid positions. It is not known whether any of these differences can be recognized by antibodies. In the present study five monoclonal antibodies (MAbs) were produced against NP of A/Duck/Novosibirsk/56/05 (H5N1) influenza virus. Two MAbs discerned human and avian influenza strains on ELISA testing. The NP expressed in a prokaryotic system was used for the analysis of site-specific mutants carrying amino acid substitutions in the relevant positions. Amino acid residues in positions 100 and 101 were shown to be recognized by the MAbs. The residue in position 100 is host-specific, and its recognition by the MAb 2E6 may be useful for the differentiation of human and avian viruses. The data are discussed in view of the effects of amino acid substitutions in influenza virus NP affecting both host range and antibody-binding specificity.
journal_name
Viral Immunoljournal_title
Viral immunologyauthors
Varich NL,Sadykova GK,Prilipov AG,Kochergin-Nikitsky KS,Kushch AA,Masalova OV,Klimova RR,Gitelman AK,Kaverin NVdoi
10.1089/vim.2010.0088subject
Has Abstractpub_date
2011-04-01 00:00:00pages
101-7issue
2eissn
0882-8245issn
1557-8976journal_volume
24pub_type
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