E Nobusawa

Summary

Affiliation: Nagoya City University
Country: Japan

Publications

  1. ncbi request reprint Change in receptor-binding specificity of recent human influenza A viruses (H3N2): a single amino acid change in hemagglutinin altered its recognition of sialyloligosaccharides
    E Nobusawa
    Department of Virology, School of Nursing, Nagoya City University, Mizuho cho, Mizuho ku, Nagoya City, 467 8601, Japan
    Virology 278:587-96. 2000
  2. pmc Comparison of the mutation rates of human influenza A and B viruses
    Eri Nobusawa
    Department of Microbiology and Infection, Nagoya City University Graduate School of Medical Science, Kawasumi 1, Mizuho cho, Mizuho ku, Nagoya City 467 8601, Japan
    J Virol 80:3675-8. 2006
  3. ncbi request reprint Analysis of the desialidation process of the haemagglutinin protein of influenza B virus: the host-dependent desialidation step
    C Luo
    Department of Virology, Medical School, Nagoya City University, 1 Kawasumi, Mizuho chou, Mizuho ku, Nagoya 467 8601, Japan
    J Gen Virol 83:1729-34. 2002
  4. ncbi request reprint [Influenza encephalopathy and encephalitis]
    E Nobusawa
    Department of Virology, Nagoya City University, Medical School
    No To Hattatsu 32:142-7. 2000
  5. doi request reprint Protective effect of nasal immunization of influenza virus hemagglutinin with recombinant cholera toxin B subunit as a mucosal adjuvant in mice
    Masanori Isaka
    Department of Bacteriology, Nagoya City University Graduate School of Medical Sciences, Nagoya, Aichi, Japan
    Microbiol Immunol 52:55-63. 2008
  6. ncbi request reprint [Analysis of the amino acid changes of the hemagglutinin of H5 avian influenza virus]
    Wen Qiong Xiu
    Department of Viral Diseases, Fujian Center for Disease Control and Prevention, Fuzhou 350001, China
    Bing Du Xue Bao 24:34-40. 2008
  7. ncbi request reprint Comparison of epitope structures of H3HAs through protein modeling of influenza A virus hemagglutinin: mechanism for selection of antigenic variants in the presence of a monoclonal antibody
    Setsuko Nakajima
    Department of Virology, Medical School, Nagoya City University, Mizuho ku, Aichi, Japan
    Microbiol Immunol 51:1179-87. 2007
  8. ncbi request reprint [Accumulation of amino acid substitutions promotes irreversible structural changes in the hemagglutinin of human influenza AH3 virus during evolution]
    Katsuhisa Nakajima
    Department of Virology, Medical School, Nagoya City University, 1 Kawasumi, Mizuho cho, Mizhuo ku, Nagoya 467, Japan
    Uirusu 56:91-8. 2006
  9. ncbi request reprint A point mutation at the C terminus of the cytoplasmic domain of influenza B virus haemagglutinin inhibits syncytium formation
    Makoto Ujike
    Department of Microbiology and Infection, Nagoya City University Graduate School of Medical Science, Kawasumi 1, Mizuho cho, Mizuho ku, Nagoya 467 8601, Japan
    J Gen Virol 87:1669-76. 2006
  10. pmc Accumulation of amino acid substitutions promotes irreversible structural changes in the hemagglutinin of human influenza AH3 virus during evolution
    Katsuhisa Nakajima
    Department of Virology, Medical School, Nagoya City University, 1 Kawasumi, Mizuho chou, Mizuho ku, Nagoya 467 8601, Japan
    J Virol 79:6472-7. 2005

Collaborators

Detail Information

Publications15

  1. ncbi request reprint Change in receptor-binding specificity of recent human influenza A viruses (H3N2): a single amino acid change in hemagglutinin altered its recognition of sialyloligosaccharides
    E Nobusawa
    Department of Virology, School of Nursing, Nagoya City University, Mizuho cho, Mizuho ku, Nagoya City, 467 8601, Japan
    Virology 278:587-96. 2000
    ..These findings suggested that the E190D change might have rendered the HA able to distinguish sialyloligosaccharides on the derivatized CRBC containing the SAalpha2,6Galbeta1,4GlcNAc sequence from those on the native CRBC...
  2. pmc Comparison of the mutation rates of human influenza A and B viruses
    Eri Nobusawa
    Department of Microbiology and Infection, Nagoya City University Graduate School of Medical Science, Kawasumi 1, Mizuho cho, Mizuho ku, Nagoya City 467 8601, Japan
    J Virol 80:3675-8. 2006
    ..A total of 813,663 nucleotides were sequenced, giving rates of 2.0 x 10(-6) and 0.6 x 10(-6) mutations per site per infectious cycle, which, when extended to 1 year, agree well with the published annual evolutionary rates...
  3. ncbi request reprint Analysis of the desialidation process of the haemagglutinin protein of influenza B virus: the host-dependent desialidation step
    C Luo
    Department of Virology, Medical School, Nagoya City University, 1 Kawasumi, Mizuho chou, Mizuho ku, Nagoya 467 8601, Japan
    J Gen Virol 83:1729-34. 2002
    ....
  4. ncbi request reprint [Influenza encephalopathy and encephalitis]
    E Nobusawa
    Department of Virology, Nagoya City University, Medical School
    No To Hattatsu 32:142-7. 2000
    ..Whether this altered receptor binding specificity is related to the occurrence of influenza encephalitis and encephalopathy is now under investigation...
  5. doi request reprint Protective effect of nasal immunization of influenza virus hemagglutinin with recombinant cholera toxin B subunit as a mucosal adjuvant in mice
    Masanori Isaka
    Department of Bacteriology, Nagoya City University Graduate School of Medical Sciences, Nagoya, Aichi, Japan
    Microbiol Immunol 52:55-63. 2008
    ....
  6. ncbi request reprint [Analysis of the amino acid changes of the hemagglutinin of H5 avian influenza virus]
    Wen Qiong Xiu
    Department of Viral Diseases, Fujian Center for Disease Control and Prevention, Fuzhou 350001, China
    Bing Du Xue Bao 24:34-40. 2008
    ..Some interesting positions need to be analyzed more finely. Some amino acid changes identified in vitro experiment may serve as molecular markers for assessing the pandemic potential of H5N1 field isolates...
  7. ncbi request reprint Comparison of epitope structures of H3HAs through protein modeling of influenza A virus hemagglutinin: mechanism for selection of antigenic variants in the presence of a monoclonal antibody
    Setsuko Nakajima
    Department of Virology, Medical School, Nagoya City University, Mizuho ku, Aichi, Japan
    Microbiol Immunol 51:1179-87. 2007
    ..One amino acid substitution in an escape mutant and another amino acid substitution in a binding-positive mutant seemed to be explained by the changes noted on this model...
  8. ncbi request reprint [Accumulation of amino acid substitutions promotes irreversible structural changes in the hemagglutinin of human influenza AH3 virus during evolution]
    Katsuhisa Nakajima
    Department of Virology, Medical School, Nagoya City University, 1 Kawasumi, Mizuho cho, Mizhuo ku, Nagoya 467, Japan
    Uirusu 56:91-8. 2006
    ..Furthermore, discordance of amino acid substitutions suggests that tolerable amino acid substitutions in different order have a probability of promoting irreversible divergence of the HA protein to different subtypes...
  9. ncbi request reprint A point mutation at the C terminus of the cytoplasmic domain of influenza B virus haemagglutinin inhibits syncytium formation
    Makoto Ujike
    Department of Microbiology and Infection, Nagoya City University Graduate School of Medical Science, Kawasumi 1, Mizuho cho, Mizuho ku, Nagoya 467 8601, Japan
    J Gen Virol 87:1669-76. 2006
    ....
  10. pmc Accumulation of amino acid substitutions promotes irreversible structural changes in the hemagglutinin of human influenza AH3 virus during evolution
    Katsuhisa Nakajima
    Department of Virology, Medical School, Nagoya City University, 1 Kawasumi, Mizuho chou, Mizuho ku, Nagoya 467 8601, Japan
    J Virol 79:6472-7. 2005
    ..These results suggest that the accumulation of amino acid substitutions in the HA protein during evolution promoted irreversible structural changes and therefore that antigenic changes in the H3HA protein may not be limited...
  11. ncbi request reprint Influence of additional acylation site(s) of influenza B virus hemagglutinin on syncytium formation
    Makoto Ujike
    Department of Microbiology and Infection, Nagoya City University Graduate School of Medical Science, Nagoya, Aichi 467 8601, Japan
    Microbiol Immunol 49:355-9. 2005
    ..However, the ability of these mutants to form syncytia was impaired, indicating that the increase in the hydrophobicity of these domains (especially the CT) affected fusion pore dilation...
  12. pmc Influence of acylation sites of influenza B virus hemagglutinin on fusion pore formation and dilation
    Makoto Ujike
    Department of Microbiology and Infection, Graduate School of Medical Science, Nagoya City University, Kawasumi 1, Mizuho cho, Mizuho ku, Nagoya City 467 8601, Japan
    J Virol 78:11536-43. 2004
    ....
  13. pmc Restriction of amino acid change in influenza A virus H3HA: comparison of amino acid changes observed in nature and in vitro
    Katsuhisa Nakajima
    Department of Virology, Nagoya City University, 1 Kawasumi, Mizuho chou, Mizuho ku, Nagoya 467 8601, Japan
    J Virol 77:10088-98. 2003
    ..These gap positions may play an important role in maintaining the function of the HA protein, and therefore amino acid changes are restricted at these locations...
  14. ncbi request reprint Analysis of epitope recognition of antibodies induced by DNA immunization against hemagglutinin protein of influenza A virus
    Ken Tonegawa
    Department of Internal Medicine and Bioregulation, Nagoya City University Graduate School of Medical Sciences, 1 Kawasumi, Mizuho chou, Mizuho ku, Nagoya, 467 8601, Aichi, Japan
    Vaccine 21:3118-25. 2003
    ..In addition, antisera obtained from mice immunized with HA1 DNA reacted with each of the known antigenic sites on the HA1 domain, similar to the results obtained with HA DNA immunization...
  15. doi request reprint Effects of single-point amino acid substitutions on the structure and function neuraminidase proteins in influenza A virus
    Takuya Yano
    Department of Virology, Medical School, Nagoya City University, Nagoya, Japan
    Microbiol Immunol 52:216-23. 2008
    ..An increase in discordance was correlated with the interval in years between virus strains, and the discordance rate was estimated to be 0.6-0.7% per year...