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Volume 55, Number 4 >

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

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Title: Characterization and epitope mapping of monoclonal antibodies to the nucleocapsid protein of severe acute respiratory syndrome coronavirus
Authors: Kariwa, Hiroaki Browse this author →KAKEN DB
Noda, Hiroshi Browse this author
Nakauchi, Mina Browse this author
Ishizuka, Mariko Browse this author
Hashiguchi, Kazuaki Browse this author
Hashimoto, Shingo Browse this author
Yoshii, Kentaro Browse this author →KAKEN DB
Asano, Atsushi Browse this author
Agui, Takashi Browse this author →KAKEN DB
Kogaki, Hiroyuki Browse this author
Kurano, Yoshihiro Browse this author
Uchida, Yoshiaki Browse this author
Fujii, Nobuyuki Browse this author
Okada, Masahisa Browse this author
Takashima, Ikuo Browse this author
Keywords: severe acute respiratory syndrome (SARS)
monoclonal antibody
Issue Date: 7-Mar-2008
Publisher: The Graduate School of Veterinary Medicine, Hokkaido University
Journal Title: Japanese Journal of Veterinary Research
Volume: 55
Issue: 4
Start Page: 115
End Page: 127
Abstract: 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.
Type: bulletin (article)
Appears in Collections:Japanese Journal of Veterinary Research > Volume 55, Number 4

Submitter: 獣医学部図書室

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