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Detection of Antibodies to the Nucleocapsid Protein of PRRS Virus by a Competitive ELISA

  • Serge Dea
  • Louise Wilson
  • Dominic Therrien
  • Estela Cornaglia
Chapter
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 494)

Abstract

The mature virions of the porcine reproductive and respiratory syndrome virus (PRRSV), a new porcine arterivirus, is made of three major structural proteins: a 25 kDa envelope glycoprotein (GP5), an 18-19 kDa unglyco-sylated membrane protein (M), and a 15 kDa nucleocapsid (N) protein (Mardassi et al., 1995; Meulenberg et al., 1995). The N protein is the more abundant protein of the virion and is highly antigenic, which therefore makes it a suitable candidate for the detection of virus-specific antibodies and diagnosis of the disease (Loemba et al, 1996). It is also encoded by a relatively well conserved region of the viral genome, since a high degree of amino acid (aa) sequence identity has been observed among the N protein of North American (96-100%) and European (94-99%) strains (Meng et al., 1995; Suarez et al., 1994). Four to five domains of antigenic importance have been identified for the N protein, a common conformational antigenic site for European and North American strains being localized in the central region of the protein (Meulenberg et al., 1998; Wootton et al., 1998).

Keywords

Nucleocapsid Protein Competitive ELISA Respiratory Syndrome Virus Lelystad Virus North American Strain 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

References

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Copyright information

© Springer Science+Business Media New York 2001

Authors and Affiliations

  • Serge Dea
    • 1
  • Louise Wilson
    • 1
  • Dominic Therrien
    • 1
  • Estela Cornaglia
    • 2
  1. 1.Centre de Microbiologie et Biotechnologie, INRS-Institut Armand-FraappierUniversité du QuébecLavalCanada
  2. 2.Biovet Inc.St-HyacintheCanada

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