Monoclonal Antibody #5-2-26 Recognizes the Phosphatase-Sensitive Epitope of Rabies Virus Nucleoprotein

• Kawai Akihiko

  Department of Molecular Microbiology, Faculty of Pharmaceutical Sciences, Kyoto University

• Anzai Jun

  Department of Molecular Microbiology, Faculty of Pharmaceutical Sciences, Kyoto University

• Honda Yoshikazu

  Department of Molecular Microbiology, Faculty of Pharmaceutical Sciences, Kyoto University

• Morimoto Kinjiro

  Department of Molecular Microbiology, Faculty of Pharmaceutical Sciences, Kyoto University

• Takeuchi Kenji

  Department of Molecular Microbiology, Faculty of Pharmaceutical Sciences, Kyoto University

• Kohno Takashi

  Department of Molecular Microbiology, Faculty of Pharmaceutical Sciences, Kyoto University

• Wakisaka Koji

  Department of Molecular Microbiology, Faculty of Pharmaceutical Sciences, Kyoto University

• Goto Hideo

  Department of Molecular Microbiology, Faculty of Pharmaceutical Sciences, Kyoto University

• Minamoto Nobuyuki

  Department of Veterinary Public Health, Faculty of Agriculture, Gifu University

抄録

We prepared monoclonal antibodies (MAbs) against the rabies virus N protein, among which one antibody (MAb 5-2-26) was shown to lack reactivity with the phosphatase-treated N protein. The MAb was able to recognize the sodium dodecyl sulfate (SDS)-denatured N protein. The MAb did not recognize the N-protein analogues produced in Escherichia coli (E. coli), indicating that the N-gene products were not normally processed in E. coli after translation. On the other hand, the MAb reacted normally with N-gene products produced in COS-7 cells, but not with those produced in the presence of K-252a (a protein kinase inhibitor of a broad spectrum). The MAb displayed weak cross-reactivity with the Triton-insoluble network structures composed of several components, while another phosphoprotein (M1) of the virus was not recognized at all. These results suggest that MAb 5-2-26 preferentially recognizes a phosphatase-sensitive linear epitope of N protein, which may enable further investigations to be conducted on the mechanism of N-protein phosphorylation and its role(s) in virus replication.

収録刊行物

• MICROBIOLOGY and IMMUNOLOGY

  MICROBIOLOGY and IMMUNOLOGY 41 (1), 33-42, 1997

  Center For Academic Publications Japan

詳細情報

• CRID: 1573105977918735488
• NII論文ID: 130003484428
• ISSN: 03855600
• Web Site: https://jlc.jst.go.jp/DN/JALC/00083378454?from=CiNii
• 本文言語コード: en
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