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

Akihiko Kawai; Jun Anzai; Yoshikazu Honda; Kinjiro Morimoto; Kenji Takeuchi; Takashi Kohno; Koji Wakisaka; Hideo Goto; Nobuyuki Minamoto

Akihiko Kawai, Jun Anzai, Yoshikazu Honda, Kinjiro Morimoto, Kenji Takeuchi, Takashi Kohno, Koji Wakisaka, Hideo Goto, Nobuyuki Minamoto

Author information

Akihiko Kawai
Department of Molecular Microbiology, Faculty of Pharmaceutical Sciences, Kyoto University
Jun Anzai
Department of Molecular Microbiology, Faculty of Pharmaceutical Sciences, Kyoto University
Yoshikazu Honda
Department of Molecular Microbiology, Faculty of Pharmaceutical Sciences, Kyoto University
International Laboratory for Research on Animal Diseases
Kinjiro Morimoto
Department of Molecular Microbiology, Faculty of Pharmaceutical Sciences, Kyoto University
Kenji Takeuchi
Department of Molecular Microbiology, Faculty of Pharmaceutical Sciences, Kyoto University
Dep. Microbiology, Fukui Medical College
Takashi Kohno
Department of Molecular Microbiology, Faculty of Pharmaceutical Sciences, Kyoto University
Biology Division, National Cancer Center Research Institute
Koji Wakisaka
Department of Molecular Microbiology, Faculty of Pharmaceutical Sciences, Kyoto University
Hideo Goto
Department of Molecular Microbiology, Faculty of Pharmaceutical Sciences, Kyoto University
Department of Veterinary Public Health, Faculty of Agriculture, Gifu University
Nobuyuki Minamoto
Department of Veterinary Public Health, Faculty of Agriculture, Gifu University

Keywords: Monoclonal antibody, Rabies virus nucleoprotein, Phosphoprotein, Phosphorylation, N gene expression

JOURNAL FREE ACCESS

1997 Volume 41 Issue 1 Pages 33-42

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Abstract

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.

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