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Antigen?Cantibody interactions of influenza virus hemagglutinin revealed by the fragment molecular orbital calculation |
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| Authors: | Akio Yoshioka Kazutomo Takematsu Ikuo Kurisaki Kaori Fukuzawa Yuji Mochizuki Tatsuya Nakano Eri Nobusawa Katsuhisa Nakajima Shigenori Tanaka |
| Institution: | 1. Graduate School of System Informatics, Kobe University, 1-1 Rokkodai, Nada-ku, Kobe, 657-8501, Japan 2. Graduate School of Human Development and Environment, Kobe University, 3-11 Tsurukabuto, Nada-ku, Kobe, 657-8501, Japan 3. Graduate School of Science and Technology, Kobe University, 1-1 Rokkodai, Nada-ku, Kobe, 657-8501, Japan 4. Mizuho Information and Research Institute Inc., 2-3 Kanda Nishiki-Cho, Chiyoda-ku, Tokyo, 101-8443, Japan 5. Department of Chemistry and Research Center for Smart Molecules, Faculty of Science, Rikkyo University, 3-34-1 Nishi-ikebukuro, Toshima-ku, Tokyo, 171-8501, Japan 6. Division of Medicinal Safety Science, National Institute of Health Sciences, 1-18-1 Kamiyoga, Setagaya-ku, Tokyo, 158-8501, Japan 7. National Institute of Infectious Diseases, 1-23-1 Toyama, Shinjuku-ku, Tokyo, 162-8640, Japan 8. Department of Virology, Medical School, Nagoya City University, 1 Kawasumi, Mizuho-cho, Mizuho-ku, Nagoya, 467-8601, Japan |
| Abstract: | Effective interactions between amino acid residues in antigen?Cantibody complex of influenza virus hemagglutinin (HA) protein can be evaluated in terms of the inter-fragment interaction energy (IFIE) analysis with the fragment molecular orbital (FMO) method, in which each fragment contains the side chain of corresponding amino acid residue. We have carried out the FMO-MP2 (second-order Moeller?CPlesset) calculation for the complex of HA antigen and Fab antibody of influenza virus H3N2 A/Aichi/2/68 and obtained the IFIE values between each amino acid residue in HA and the whole antibody as the sums over the residues contained in the latter. Combining this IFIE data with experimental data for hemadsorption activity of HA mutants, we succeeded in theoretically explaining the mutations in HA observed after the emergence of influenza virus H3N2 A/Aichi/2/68 in an earlier study, except for those of THR83. In the present study, we employ an alternative way of fragment division in the FMO calculation at the carbonyl C site of the peptide bond instead of the C?? site used in the previous work, which provides revised IFIE values consistent with all the historical mutation data in the antigenic region E of HA including the case of THR83 in the present prediction scheme for probable mutations in HA. |
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