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Characterization and epitope mapping of monoclonal antibodies to the nucleocapsid protein of severe acute respiratory syndrome coronavirus.

Characterization and epitope mapping of monoclonal antibodies to the nucleocapsid protein of severe acute respiratory syndrome coronavirus. Research Abstract Details 

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  • Characterization and epitope mapping of monoclonal antibodies to the nucleocapsid protein of severe acute respiratory syndrome coronavirus. Abstract Text:

    hiroaki kariwaHiroaki Kariwa,hiroshi nodaHiroshi Noda,mina nakauchiMina Nakauchi,mariko ishizukaMariko Ishizuka,kazuaki hashiguchiKazuaki Hashiguchi,shingo hashimotoShingo Hashimoto,kentaro yoshiiKentaro Yoshii,atsushi asanoAtsushi Asano,takashi aguiTakashi Agui,hiroyuki kogakiHiroyuki Kogaki,yoshihiro kuranoYoshihiro Kurano,yoshiaki uchidaYoshiaki Uchida,nobuyuki fujiiNobuyuki Fujii,masahisa okadaMasahisa Okada,ikuo takashimaIkuo Takashima,

    The sudden emergence of severe acute respiratory syndrome (SARS) at the end of 2002 resulted in 774 reported deaths from more than 8000 cases worldwide. As no effective vaccines or antiviral agents are available, the most effective measure to prevent the expansion of a SARS epidemic is the rapid diagnosis and isolation of SARS patients. To establish specific diagnostic methods, we generated nine clones of monoclonal antibodies to nucleocapsid protein (NP) of SARS-coronavirus (SARS-CoV). On immunofluorescent antibody assay and Western blotting analysis, none of the monoclonal antibodies showed cross-reactivity to authentic and recombinant NPs of human coronavirus (HCoV) 229E strain. To determine the region on the NP molecule where the monoclonal antibodies bind, we generated four truncated recombinant NPs and analyzed the reactivity between monoclonal antibodies and truncated NPs. Two monoclonal antibodies reacted with a truncated NP covering from amino acid residues 111 to 230, and seven reacted with another truncated NP covering from amino acid residues 221 to 340. Epitope mapping analysis indicated that monoclonal antibody SN5-25 recognized the amino acid sequence Q(245)TVTKK(250) On SARS-NP. Within the epitope, Q245, T246, V247, K249, and K250 appeared to form an essential motif for monoclonal antibody SN5-25 to bind. The information about binding sites and epitopes of monoclonal antibodies may be useful for the development of new diagnostic methods for SARS and for analyzing the function of N protein of SARS-CoV.

    Characterization and epitope mapping of monoclonal antibodies to the nucleocapsid protein of severe acute respiratory syndrome coronavirus. Publishing Authors By Initials

    h kariwaH Kariwa,h nodaH Noda,m nakauchiM Nakauchi,m ishizukaM Ishizuka,k hashiguchiK Hashiguchi,s hashimotoS Hashimoto,k yoshiiK Yoshii,a asanoA Asano,t aguiT Agui,h kogakiH Kogaki,y kuranoY Kurano,y uchidaY Uchida,n fujiiN Fujii,m okadaM Okada,i takashimaI Takashima,

    For similar abstracts research abstracts see: abstracts research

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    Characterization and epitope mapping of monoclonal antibodies to the nucleocapsid protein of severe acute respiratory syndrome coronavirus. Journal Published:

    PUBLICATION TYPE: Research Support, Non-U.S. Gov

    Journal: The Japanese journal of veterinary research

    VOLUME: 55

    Page Numbers: 115-27

    Journal Abbreviation: Jpn. J. Vet. Res.

    ISSN: 0047-1917

    DAY: 2

    MONTH: Feb

    YEAR: 2008

    Characterization and epitope mapping of monoclonal antibodies to the nucleocapsid protein of severe acute respiratory syndrome coronavirus. Information

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    LANGUAGE: eng

    NlmUniqueID: 376567

    Characterization and epitope mapping of monoclonal antibodies to the nucleocapsid protein of severe acute respiratory syndrome coronavirus. Keywords Mesh Terms:

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    Grant and Affiliation Information for Characterization and epitope mapping of monoclonal antibodies to the nucleocapsid protein of severe acute respiratory syndrome coronavirus.

    AFFILIATION: Laboratory of Public Health, Department of Environmental Veterinary Sciences, Graduate School of Veterinary Medicine, Hokkaido University, Sapporo 060-0818, Japan. kariwa@vetemed.hokudai.ac.jp

    Country: Japan

    Japan Research PublicationJapan Research Publication

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    MEDLINETA: Jpn J Vet Res

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