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

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


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).


Nucleocapsid Protein Competitive ELISA Respiratory Syndrome Virus Lelystad Virus North American Strain 
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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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