BMC Genomics 2009, 10(Suppl 3):S24 http://www.biomedcentral.com/1471-2164/10/S3/S24 Figure 5 Simulation results of four Puerto-34 HA systems. non-mutated Puerto-34 (black), G224S (green), Q222L(red) and Q222L/G224S (blue) binding to a(2,3) receptor (top) and a(2,6) receptor (bottom). Competing interests The authors declare that they have no competing interests. Authors’ contributions NJ, DC and WM performed modeling, MD simulations and generated figures. ST, PJS and CS helped with data analysis and drafting of the manuscript. ST and CS obtained funding. All authors read and approved the final manuscript. Note Other papers from the meeting have been published as part of BMC Bioinformatics Volume 10 Supplement 15, 2009: Eighth International Conference on Bioinfor- matics (InCoB2009): Bioinformatics, available online at http://www.biomedcentral.com/1471-2105/10? issue=S15. Acknowledgements This work is partially supported by the Kasetsart University Research and Development Institute (grant number S-17.49); Bilateral Research Cooperation (BRC2/2551) from the Faculty of Science, Kasetsart University; the National Center for Genetic Engineering and Biotechnol- ogy (BT-B-01-IG-11-5001); the Thailand Research Fund (DBG4880017 to C.S.); the Commission on Higher Education (CHE-PhD-SW_20060163); the National Research University Project and the postgraduate education and research program in petroleum and petrochemical technology (MUA- ADB). The MD simulations were carried out on the computer clusters at the National Center for Genetic Engineering and Biotechnology (BIOTEC) and the Thai National Grid Center. The authors would like to thank Prof. Dr. Supot and Assoc. Prof. Dr. Supa Hannongbua for their support. We are grateful for A. Univ. Prof. Dr. Peter Wolschann for his inexhaustible kindness and encouragement. This article has been published as part of BMC Genomics Volume 10 Supplement 3, 2009: Eighth International Conference on Bioinformatics (InCoB2009): Computational Biology. The full contents of the supplement are available online at http://www.biomedcentral.com/1471-2164/10? issue=S3. References 1. Weiss RA: Cross-species infections. Curr Top Microbiol Immunol 2003, 278:47–71. 2. Rabadan R, Levine AJ and Robins H: Comparison of avian and human influenza A viruses reveals a mutational bias on the viral genomes. J Virol 2006, 80:11887–11891. 3. Lee CW, Suarez DL, Tumpey TM, Sung HW, Kwon YK, Lee YJ, Choi JG, Joh SJ, Kim MC, Lee EK, Park JM, Lu X, Katz JM, Spackman E, Swayne DE and Kim JH: Characterization of highly pathogenic H5N1 avian influenza A viruses isolated from South Korea. J Virol 2005, 79:3692–3702. 4. Zhou H, Jin M, Chen H, Huag Q and Yu Z: Genome-sequence Analysis of the Pathogenic H5N1 Avian Influenza A Virus Isolated in China in 2004. Virus Genes 2006, 32:85–95. 5. Ha Y, Stevens DJ, Skehel JJ and Wiley DC: X-ray structures of H5 avian and H9 swine influenza virus hemagglutinins bound to avian and human receptor analogs. Proc Natl Acad Sci USA 2001, 98:11181–11186. 6. Viseshakul N, Thanawongnuwech R, Amonsin A, Suradhat S, Payungporn S, Keawchareon J, Oraveerakul K, Wongyanin P, Plitkul S, Theamboonlers A and Poovorawan Y: The genome sequence analysis of H5N1 avian influenza A virus isolated from the outbreak among poultry populations in Thailand. Virology 2004, 328:169–176. 7. Nobusawa E, Aoyama T, Kato H, Suzuki Y, Tateno Y and Nakajima K: Comparison of complete amino acid sequences and recep- tor-binding properties among 13 serotypes of hemaggluti- nins of influenza A viruses. Virology 1991, 182:475–485. 8. Minyong L and Binghe W: Computational studies of H5N1 hemagglutinin binding with SA-a-2, 3-Gal and SA-a-2, 6-Gal. Biochem Biophys Res Commun 2006, 347:662–668. 9. Ito T, Suzuki Y, Suzuki T, Takada A, Horimoto T, Wells K, Kida H, Otsuki K, Kiso M, Ishida H and Kawaoka Y: Recognition of N- glycolylneuraminic acid linked to galactose by the alpha2,3 linkage is associated with intestinal replication of influenza A virus in ducks. J Virol 2000, 74:9300–9305. 10. Ha Y, Stevens D, Skehel JJ and Wiley DC: H5 avian and H9 swine influenza virus haemagglutinin structures: possible origin of influenza subtypes. EMBO J 2002, 21:865–875. 11. Stevens J, Blixt O, Tumpey TM, Taubenberger JK, Paulson JC and Wilson IA: Structure and receptor specificity of the hemag- glutinin from an H5N1 influenza virus. Science 2006, 312:404–410. 12. Stevens J, Blixt O, Glaser L, Taubenberger JK, Palese P, Paulson JC and Wilson IA: Glycan microarray analysis of the hemagglu- tinins from modern and pandemic influenza viruses reveals different receptor specificities. J Mol Biol 2006, 355:1143–1455. Page 8 of 9 (page number not for citation purposes)