Abstract
The neuraminidase (NA) in viral surface is one of the main subtype-specific antigen of influenza type A viruses. Neuraminidase is an enzyme to break the bonds between hemagglutinin (HA) and sialic acid to release newly formed viruses from infected cells. In this study, the H3N2 subtype virus NA genes were sequenced and NA proteins were screened for B-cell epitopes and assessed based on immunoinformatics. Based on this results, four peptides DR6, EY7, VG8 and RE8 (covering amino acid residues 151–156, 368–374, 398–405 and 428–435, respectively) of the NA protein were synthesized artificially. These peptides were used to immunize New Zealand rabbits subcutaneously to raise antisera. Experimental results showed that these four peptides were capable of eliciting antibodies against H3N2 viruses in a specific and sensitive feature, detected in vitro by enzyme-linked immunosorbent assay. Moreover, hemadsorption anti-releasing effects took place in three three-antisera-mixtures at a dilution of 1:40. Alignment using NA gene database showed that amino acid residues in these four epitope peptides were substituted at specific sites in all the NAs sequenced in this study. It was suggested that these NA epitope peptides might be used in combination with HA proteins as vaccine antigens.
Article PDF
Similar content being viewed by others
References
Yen H L, Webster R G. Pandemic influenza as a current threat. Curr Top Microbiol Immunol, 2009, 333: 3–24
Baek Y H, Park J H, Song Y J, et al. Molecular characterization and phylogenetic analysis of H3N2 human influenza A viruses in Cheongju, South Korea. J Microbiol, 2009, 47: 91–100
Huang P, Deng F. Influenza. Guangzhou: Guangdong Technological Press, 2004. 89–91
Huang I C, Li W, Sui J, et al. Influenza A virus neuraminidase limits viral superinfection. J Virol, 2008, 82: 4834–4843
Huang P, Xu Y, Ni H, et al. Linear B-cell epitope mapping of neuraminidases of the H1N1 viruses based on immunoinformatics. Vaccine, 2011, 29: 1278–1282
Huang P, Yu S Y, Ke C W. Stepwise prediction and statistical screening: The B-cell epitopes on neuraminidase of human avian H5N1 virus. Chin Sci Bull, 2008, 53: 3642–3647
Tomar N, De R K. Immunoinformatics: An integrated scenario. Immunology, 2010, 31: 153–168
Xu X L, Sun J, Liu Q, et al. Evaluation of spatial epitope computational tools based on experimentally-confirmed dataset for protein antigens. Chin Sci Bull, 2010, 55: 2169–2174
Bordoli L, Schwede T. Automated protein structure modeling with SWISS-MODEL Workspace and the Protein Model Portal. Methods Mol Biol, 2012, 857: 107–136
Krieger E, Koraimann G, Vriend G. Increasing the precision of comparative models with YASARA NOVA: A self-parametrizing force field. Proteins, 2002, 47: 393–402
Yuan X, Qua Z, Wu X, et al. Molecular modeling and epitopes mapping of human adenovirus type 3 hexon protein. Vaccine, 2009, 27: 5103–5110
Liang L, Huang P, Wen M, et al. Epitope peptides of influenza H3N2 neuraminidase gene designed by immunoinformatics. Acta Bioch Bioph Sin, 2012, 44: 113–118
Huang P, Xu Y S, Zhong J, et al. Characterization of epitope peptides of neuraminidases of the 2009 A H1N1 viruses designed by immunoinformatics. Prog Biochem Biophys, 2011, 38: 929–9
Yen H L, Hoffmann E, Taylor G, et al. Importance of neuraminidase active site residues to the neuraminidase inhibitor resistance of influenza viruses. J Virol, 2006, 80: 8787–8795
Author information
Authors and Affiliations
Corresponding author
Additional information
This article is published with open access at Springerlink.com
Rights and permissions
This article is published under an open access license. Please check the 'Copyright Information' section either on this page or in the PDF for details of this license and what re-use is permitted. If your intended use exceeds what is permitted by the license or if you are unable to locate the licence and re-use information, please contact the Rights and Permissions team.
About this article
Cite this article
Zhong, J., Huang, P., Wen, M. et al. Antigenic epitope peptides of influenza H3N2 virus neuraminidase gene based on experiments. Chin. Sci. Bull. 57, 2908–2913 (2012). https://doi.org/10.1007/s11434-012-5266-0
Received:
Accepted:
Published:
Issue Date:
DOI: https://doi.org/10.1007/s11434-012-5266-0