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Journal of Clinical Microbiology, March 2001, p. 906-912, Vol. 39, No. 3
0095-1137/01/$04.00+0   DOI: 10.1128/JCM.39.3.906-912.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Enzyme-Linked Immunosorbent Assay Using a Virus Type-Specific Peptide Based on a Subdomain of Envelope Protein Erns for Serologic Diagnosis of Pestivirus Infections in Swine

J. P. M. Langedijk,1,* W. G. J. Middel,1 R. H. Meloen,2 J. A. Kramps,3 and J. A. de Smit1

Department of Mammalian Virology,1 and Department of Production,3 Institute for Animal Science and Health (ID-Lelystad), and Pepscan Systems B.V.,2 Lelystad, The Netherlands

Received 7 July 2000/Returned for modification 8 September 2000/Accepted 17 October 2000

Peptides deduced from the C-terminal end (residues 191 to 227) of pestivirus envelope protein Erns were used to develop enzyme-linked immunosorbent assays (ELISAs) to measure specifically antibodies against different types of pestiviruses. The choice of the peptide was based on the modular structure of the Erns protein, and the peptide was selected for its probable independent folding and good exposure, which would make it a good candidate for an antigenic peptide to be used in a diagnostic test. A solid-phase peptide ELISA which was cross-reactive for several types of pestivirus antibodies and which can be used for the general detection of pestivirus antibodies was developed. To identify type-specific pestivirus antibodies, a liquid-phase peptide ELISA, with a labeled, specific classical swine fever virus (CSFV) peptide and an unlabeled bovine viral diarrhea virus peptide to block cross-reactivity, was developed. Specificity and sensitivity of the liquid-phase peptide ELISA for CSFV were 98 and 100%, respectively. Because the peptide is a fragment of the Erns protein, it can be used to differentiate between infected and vaccinated animals when a vaccine based on the E2 protein, which is another pestivirus envelope protein, is used.

* Corresponding author. Mailing address: Department of Mammalian Virology, Institute for Animal Science and Health (ID-Lelystad), Edelhertweg 15, P.O. Box 65, 8200 AB Lelystad, The Netherlands. Phone: 31-320-238349. Fax: 31-320-239050. E-mail: j.p.m.langedijk{at}id.wag-ur.nl.

Journal of Clinical Microbiology, March 2001, p. 906-912, Vol. 39, No. 3
0095-1137/01/$04.00+0   DOI: 10.1128/JCM.39.3.906-912.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Tews, B. A., Meyers, G. (2007). The Pestivirus Glycoprotein Erns Is Anchored in Plane in the Membrane via an Amphipathic Helix. J. Biol. Chem. 282: 32730-32741 [Abstract] [Full Text]  
  • Lin, M., Trottier, E., Mallory, M. (2005). Enzyme-Linked Immunosorbent Assay Based on a Chimeric Antigen Bearing Antigenic Regions of Structural Proteins Erns and E2 for Serodiagnosis of Classical Swine Fever Virus Infection. CVI 12: 877-881 [Abstract] [Full Text]  
  • Lin, M., Trottier, E., Pasick, J. (2005). Antibody Responses of Pigs to Defined Erns Fragments after Infection with Classical Swine Fever Virus. CVI 12: 180-186 [Abstract] [Full Text]  
  • Lin, M., Trottier, E., Pasick, J., Sabara, M. (2004). Identification of Antigenic Regions of the Erns Protein for Pig Antibodies Elicited during Classical Swine Fever Virus Infection. J Biochem 136: 795-804 [Abstract] [Full Text]  
  • Langedijk, J. P. M., van Veelen, P. A., Schaaper, W. M. M., de Ru, A. H., Meloen, R. H., Hulst, M. M. (2002). A Structural Model of Pestivirus Erns Based on Disulfide Bond Connectivity and Homology Modeling Reveals an Extremely Rare Vicinal Disulfide. J. Virol. 76: 10383-10392 [Abstract] [Full Text]  


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