New mutational trends in the HA protein of 2009 H1N1 pandemic influenza virus from May 2010 to February 2011
Wei Hu
.
DOI: 10.4236/ns.2011.35051   PDF    HTML     7,156 Downloads   11,689 Views   Citations

Abstract

As we enter the year of 2011, the 2009 H1N1 pandemic influenza virus is in the news again. At least 20 people have died of this virus in China since the beginning of 2011 and it is now the predominant flu strain in the country. Although this novel virus was quite stable during its run in the flu season of 2009-2010, a genetic variant of this virus was found in Singapore in early 2010, and then in Australia and New Zealand during their 2010 winter influenza season. Several critical mutations in the HA protein of this variant were uncovered in the strains collected from January 2010 to April 2010. Moreover, a structural homology model of HA from the A/Brisbane/10/2010(H1N1) strain was made based on the structure of A/California/04/2009 (H1N1). The purpose of this study was to investigate mutations in the HA protein of 2009 H1N1 from sequence data collected worldwide from May 2010 to February 2011. A fundamental problem in bioinformatics and biology is to find the similar gene sequences for a given gene sequence of interest. Here we proposed the inverse problem, i.e., finding the exemplars from a group of related gene sequences. With a clustering algorithm affinity propagation, six exemplars of the HA sequences were identified to represent six clusters. One of the clusters contained strain A/Brisbane/12/2010(H1N1) that only differed from A/Brisbane/10/2010 in the HA sequence at position 449. Based on the sequence identity of the six exemplars, nine mutations in HA were located that could be used to distinguish these six clusters. Finally, we discovered the change of correlation patterns for the HA and NA of 2009 H1N1 as a result of the HA receptor binding specificity switch, revealing the balanced interplay between these two surface proteins of the virus.

Share and Cite:

Hu, W. (2011) New mutational trends in the HA protein of 2009 H1N1 pandemic influenza virus from May 2010 to February 2011. Natural Science, 3, 379-387. doi: 10.4236/ns.2011.35051.

Conflicts of Interest

The authors declare no conflicts of interest.

References

[1] Mo, H.(2011) A/H1N1 now predominant flu strain in China. http://news.xinhuanet.com/english2010/china/ 2011-02/10/c_13726154.htm
[2] Barr, I.G., Cui, L., Komadina, N., Lee, R.T., Lin, R.T., Deng, Y., Caldwell, N., Shaw, R., Maurer-Stroh, S. (2010) A new pandemic influenza A(H1N1) genetic variant predominated in the winter 2010 influenza season in Australia. New Zealand and Singapore. Europe Surveillance, 15, 19692.
[3] Hu, W. (2009) Analysis of correlated mutations, stalk motifs, and phylogenetic relationship of the 2009 influenza a virus neuraminidase sequences. Journal of Biomedical Science and Engineering, 2, 550-558. doi:10.4236/jbise.2009.27080
[4] Hu, W. (2010) The interaction between the 2009 H1N1 Influenza a hemagglutinin and neuraminidase: mutations, comutations, and the na stalk motifs. Journal of Biomedical Science and Engineering, 3, 1-12.
[5] Hu, W. (2010) Novel host markers in the 2009 pandemic H1N1 Influenza a virus. Journal of Biomedical Science and Engineering, 3, 584-601. doi:10.4236/jbise.2010.36081
[6] Hu, W. (2010) Nucleotide host markers in the influenza a viruses. Journal of Biomedical Science and Engineering, 3, 684-699. doi:10.4236/jbise.2010.37093
[7] Hu, W. (2010) Identification of highly conserved domains in hemagglutinin associated with the receptor binding specificity of influenza viruses: 2009 H1N1, Avian H5N1, and Swine H1N2. Journal of Biomedical Science and Engineering, 3, 114-123. doi:10.4236/jbise.2010.32017
[8] Hu, W. (2010) Quantifying the effects of mutations on receptor binding specificity of influenza viruses. Journal of Biomedical Science and Engineering, 3, 227-240. doi:10.4236/jbise.2010.33031
[9] Hu, W. (2010) Subtle differences in receptor binding specificity and gene sequences of the 2009 pandemic H1N1 Influenza Virus. Advances in Bioscience and Biotechnology, 1, 305-314. doi:10.4236/abb.2010.14040
[10] Hu, W. (2010) Correlated mutations in the four influenza proteins essential for Viral RNA Synthesis, Host Adaptation, and Virulence: NP, PA, PB1, and PB2. Natural Science, 2, 1138-1147. doi:10.4236/ns.2010.210141
[11] Hu, W. (2010) Highly conserved domains in hemagglutinin of Influenza Viruses characterizing dual receptor binding. Natural Science, 2, 1005-1014. doi:10.4236/ns.2009.29123
[12] Hu, W. (2010) Host markers and correlated mutations in the overlapping genes of Influenza Viruses: M1, M2; NS1, NS2; and PB1, PB1-F2. Natural Science, 2, 1225-1246. doi:10.4236/ns.2010.211150
[13] Hu, W. (2011) Receptor binding specificity and origin of 2009 H1N1 Pandemic Influenza Virus. Natural Science, 3, 234-248. doi:10.4236/ns.2011.33030
[14] Maurer-Stroh, S., Lee, R.T., Eisenhaber, F., Cui, L., Phuah, S.P., Lin, R.T. (2010) A new common mutation in the hemagglutinin of the 2009 (H1N1) influenza a virus. PLoS Curr, 1, 1162.
[15] Brendan, J.F. and Delbert, D. (2007) Clustering by passing messages between data points. Science, 315, 972-976. doi:10.1126/science.1136800
[16] Inmar, E.G. and Brendan J.F. (2009) A binary variable model for affinity propagation. Neural Computation, 21(6), 1589-1600. doi:10.1162/neco.2009.05-08-785
[17] Childs, R.A., Palma, A.S., Wharton, S., et al. (2009) Receptor-binding specificity of pandemic influenza A (H1N1) 2009 virus determined by carbohydrate microarray. Nature Biotechnology, 27, 797-799. doi:10.1038/nbt0909-797
[18] Katoh, K., Kuma, K., Toh, H. and Miyata, T. (2005) MAFFT version 5: improvement in accuracy of multiple sequence alignment. Nucleic Acids Reseach, 33, 511-518.doi:10.1093/nar/gki198
[19] Inmar, E. G. and Brendan, J. F. (2009) A binary variable model for affinity propagation. Neural Computation, 21, 1589-1600. doi:10.1162/neco.2009.05-08-785
[20] Delbert, D., Brendan, J. F., Nebojsa, J., Vladimir, J., et al. (2008) Constructing treatment portfolios using affinity propagation. International Conference on Research in Computational Molecular Biology, Singapore, 30 March - 2 February 2008, 360-371.
[21] Delbert, D. and Brendan, J.F. (2007) Non-metric affinity propagation for unsupervised image categorization. International Conference on Computer Vision, Rio de Janeiro, 14-20 October 2007, 1-8.
[22] Nevena, L., Inmar, E.G., Parham, A. and Brendan, J.F. (2009) Facility Location for Subspace Segmentation. 12th International Conference on Computer Vision, Kyoto, 29 September - 2 October, 2009, 825-832.
[23] Veljko, V., Henry, L.N, Sanja, G., Nevena, V., Vladimir, P. and Claude, P.M. (2009) Identification of hemagglutinin structural domain and polymorphisms which may modulate swine H1N1 interactions with human receptor. BMC Structural Biology, 9, 62. doi:10.1186/1472-6807-9-62
[24] Veljkovic, V., Veljkovic, N., Muller, C.P., Müller, S., SGlisic, S., Perovic, V. and K?hler, H. (2009) Characterization of conserved properties of hemagglutinin of H5N1 and human influenza viruses: Possible consequences for therapy and infection control. BMC Structural Biology, 7, 9-21.
[25] Veljkovic, N., Glisic, S., Prljic, J., Perovic, V., Botta, M. and Veljkovic, V. (2008) Discovery of new therapeutic targets by the informational spectrum method. Current Protein Peptide Science, 9, 493-506. doi:10.2174/138920308785915245
[26] Cosic, I. (1997) The resonant recognition model of macromolecular bioreactivity: Theory and application. Birkhauser Verlag, Berlin.
[27] Veljkovic, V., Veljkovic, N., Este, J.A., Huther, A. and Dietrich, U. (2007) Application of the EIIP/ISM bioinformatics concept in development of new drugs. Current Medicinal Chemistry, 14, 441-453. doi:10.2174/092986707779941014
[28] Cover, T.A. and Thomas, J.A. (1991) Elements of information theory. John Wiley and Sons, New York. doi:10.1002/0471200611
[29] David, M. (2003) Information theory, inference, and learning algorithms. Cambridge University Press, Cambridge.
[30] Andrea, K., Gabriel, R.N., Ivan, K.H., and Sccarontefan, J. (2002) Sequence similarities and evolutionary relation- ships of influenza virus A hemagglutinins. Virus Genes, 24, 57-63. doi:10.1023/A:1014038120979
[31] Le, L., Lee, E.H., Hardy, D.J., Truong, T.N. and Schulten, K. (2010) Molecular dynamics simulations suggest that electrostatic funnel directs binding of Tamiflu to influenza N1 neuraminidases. PLoS Computational Biology, 6. e1000939. doi:10.1371/journal.pcbi.1000939
[32] Sung, J.C., Van, Wynsberghe, A.W., Amaro, R.E., Li, W.W. and McCammon, J.A. (2010) Role of secondary sialic acid binding sites in influenza N1 neuraminidase. Journal of American Chemical Society, 132, 2883-2885. doi:10.1021/ja9073672
[33] Zhou, H., Yu, Z., Hu, Y., Tu, J., Zou, W., et al. (2009) The special neuraminidase stalk-motif responsible for increased virulence and pathogenesis of H5N1 influenza A virus. PLoS One, 4, 6277. doi:10.1371/journal.pone.0006277
[34] Matsuoka, Y., Swayne, D.E., Thomas, C., Rameix-Welti, M.A., Naffakh, N., et al. (2009) Neuraminidase stalk length and additional glycosylation of the hemagglutinin influence the virulence of influenza H5N1 viruses for mice. Journal of Virology, 83, 4704-4708. doi:10.1128/JVI.01987-08

Copyright © 2024 by authors and Scientific Research Publishing Inc.

Creative Commons License

This work and the related PDF file are licensed under a Creative Commons Attribution 4.0 International License.