J Bacteriol Virol.  2008 Dec;38(4):235-237. 10.4167/jbv.2008.38.4.235.

Purification of Protein Expressed from Three Different Regions of Norovirus (NoV)

Affiliations
  • 1Department of Food Science and Technology, Ewha Womans University, Seoul, Korea.
  • 2Department of Bioindustry, College of Life and Environment, Daegu University, Daegu, Korea.
  • 3Department of Microbiology, College of Medicine, the Catholic University of Korea, Seoul, Korea. paik@catholic.ac.kr
  • 4Department of Environmental Health Research, National Institute of Environmental Research, Incheon, Korea.
  • 5Catholic Hematopoietic Stem Cell Transplantation Center, the Catholic University of Korea, Seoul, Korea.

Abstract

Norovirus (NoV), which belongs to the family Caliciviridae, is one of the major causes of nonbacterial acute gastroenteritis in the world. In this study, we purified proteins from the epitope region of norovirus for development of the rapid diagnosis system using polyclonal antibodies. As antigens, parts of the ORF (open reading frame) 2, ORF2-P domain, ORF2-Epi, and ORF3 regions were selected and their expressions were induced. The antigenicity of the purified proteins was identified by Western blotting. Each of the purified proteins was injected into mice for the production of novel antibodies and after 3 months of immunization, sera from the mice were obtained. The polyclonal antibody titer was tested by enzyme-linked immunosorbent assay (ELISA) and antibody against ORF2-Epi showed the highest titer. Those polyclonal antibodies can be used in further immunoassay for the rapid detection of NoVs from food and clinical specimens.

Keyword

Norovirus; Purified protein; Polyclonal antibody; ELISA

MeSH Terms

Animals
Antibodies
Blotting, Western
Caliciviridae
Ecthyma, Contagious
Enzyme-Linked Immunosorbent Assay
Gastroenteritis
Humans
Immunization
Immunoassay
Mice
Norovirus
Proteins
Antibodies
Proteins
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