ArticleClinical and diagnostic laboratory immunology2005
Antibody responses of pigs to defined Erns fragments after infection with classical swine fever virus.
Article in Clinical and diagnostic laboratory immunology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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9 citing papers in PubMed, 20 citations in OpenAlex.
- Development of a dual immunochromatographic test strip to detect E2 and EFrontiers in microbiology · 2024Article
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- Genotyping and Molecular Characterization of Classical Swine Fever Virus Isolated in China during 2016-2018.Viruses · 2021Article
- Recent Advances in the Diagnosis of Classical Swine Fever and Future Perspectives.Pathogens (Basel, Switzerland) · 2020Review
- A Novel Porcine Circovirus Distantly Related to Known Circoviruses Is Associated with Porcine Dermatitis and Nephropathy Syndrome and Reproductive Failure.Journal of virology · 2017Article
- Prokaryotic expression and purification of highly soluble partial glycoprotein erns of Indian strain of classical Swine Fever virus.Indian journal of virology : an official organ of Indian Virological Society · 2012Article
- A pair of ligation-independent Escherichia coli expression vectors for rapid addition of a polyhistidine affinity tag to the N- or C-termini of recombinant proteins.Journal of biomolecular techniques : JBT · 2009Article
- 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.Clinical and diagnostic laboratory immunology · 2005Article
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Antibody responses of pigs to defined Erns fragments, after classical swine fever virus (CSFV) infection, were studied by using an enzyme-linked immunosorbent assay (ELISA). Selection of various E(rns) fragments was based on an immunodominant Erns region encompassing three overlapping antigenic regions, amino acids 65 to 145 (Erns(aa)65-145) (AR1), 84 to 160 (Erns(aa)84-160) (AR2), and 109 to 220 (Erns(aa)109-220) (AR3), identified earlier by our group (M. Lin, E. Trottier, J. Pasick, and M. Sabara, J. Biochem., in press). Defined Erns fragments, including AR1, AR2, AR3, Erns(aa)65-160 (AR12), Erns(aa)84-220 (AR23), Erns(aa)65-220 (AR123), Erns(aa)109-145 (the consensus region defined by the three overlapping regions), and Erns(aa)109-160 (a fragment 15 amino acids larger than the consensus region), were expressed in Escherichia coli, purified by nickel chelate affinity chromatography, and used to measure antibody responses in 20 sera serially collected from pigs experimentally infected with CSFV. Based on the optimum cutoffs determined by receiver operating characteristic analysis after testing 238 negative field sera from Canadian sources, all the Erns fragments were capable of distinguishing positive from negative antibody responses with sensitivities ranging between 75 and 90% and specificities ranging between 83.2 and 100%. Detection of antibody responses to refolded Erns(aa)109-145 and Erns(aa)109-160 by ELISA (this study) but not by Western blots (Lin et al., in press) indicated that the epitopes within the consensus region are conformational. When cutoff values were raised to give a specificity of 100%, four Erns fragments (AR2, AR23, Erns(aa)109-145, and Erns(aa)109-160) offered much higher sensitivities (75 to 90%) than those obtained with other fragments (20 to 65%). Erns(aa)109-145 and Erns(aa)109-160 were capable of detecting antibody responses in infected pigs as early as 7 days postinfection. Demonstration of antibody responses to either one of the four fragments can thus be an alternative to use of the full-length protein in ELISA for serological diagnosis of CSFV infection. An advantage of such a test would be its utilization for serological survey in a classical swine fever-free country (e.g., Canada) in biocontainment level 2 laboratories.
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