Linear and Conformation-Dependent Antigenic Sites on the Nucleoprotein of Rabies Virus

• Minamoto Nobuyuki

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

• Tanaka Harumi

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

• Hishida Miyuki

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

• Goto Hideo

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

• Ito Hiroshi

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

• Naruse Shinji

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

• Yamamoto Keiko

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

• Sugiyama Makoto

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

• Kinjo Toshio

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

• Mannen Kazuaki

  Animal Laboratory Center, Oita Medical University

• Mifune Kumato

  Department of Microbiology, Oita Medical University

抄録

A set of 29 monoclonal antibodies (MAbs) specific for the rabies virus nucleoprotein (N protein) was prepared and used to analyze the topography of antigenic sites. At least four partially overlapping antigenic sites were delineated on the N protein of rabies virus by competitive binding assays. Indirect immunofluorescent antibody tests using MAbs with a series of rabies and rabies-related viruses showed that epitopes shared by various fixed and street strains of rabies virus were mainly localized at antigenic sites II and III, while epitopes representing the genus-specific antigen of Lyssavirus were widely presented at sites I, III and IV. All but one of seven MAbs specific for antigenic sites I, IV and bridge site (I and II) reacted with the antigen that had been denatured by sodium dodecyl sulfate or 2-mercaptoethanol, as well as with the denatured N protein in Western blotting assays. However, none of the MAbs against antigenic sites II and III reacted with the denatured antigen. These data indicate that antigenic sites I and IV, and sites II and III on the N protein of rabies virus are composed of linear and conformation-dependent epitopes, respectively.

収録刊行物

• MICROBIOLOGY and IMMUNOLOGY

  MICROBIOLOGY and IMMUNOLOGY 38 (6), 449-455, 1994

  Center For Academic Publications Japan

詳細情報

• CRID: 1570854178105359616
• NII論文ID: 130003484111
• ISSN: 03855600
• Web Site: https://jlc.jst.go.jp/DN/JALC/00080518334?from=CiNii
• 本文言語コード: en
• データソース種別:
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