MISC

1994年

LINEAR AND CONFORMATION-DEPENDENT ANTIGENIC SITES ON THE NUCLEOPROTEIN OF RABIES VIRUS

MICROBIOLOGY AND IMMUNOLOGY
  • N MINAMOTO
  • ,
  • H TANAKA
  • ,
  • M HISHIDA
  • ,
  • H GOTO
  • ,
  • H ITO
  • ,
  • S NARUSE
  • ,
  • K YAMAMOTO
  • ,
  • M SUGIYAMA
  • ,
  • T KINJO
  • ,
  • K MANNEN
  • ,
  • K MIFUNE

38
6
開始ページ
449
終了ページ
455
記述言語
英語
掲載種別
DOI
10.1111/j.1348-0421.1994.tb01806.x
出版者・発行元
CENTER ACADEMIC PUBL JAPAN

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.


リンク情報
DOI
https://doi.org/10.1111/j.1348-0421.1994.tb01806.x
Web of Science
https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:A1994NR50100006&DestApp=WOS_CPL

エクスポート
BibTeX RIS