ArticleVirus genes2017
Identification of epitopes on nonstructural protein 7 of porcine reproductive and respiratory syndrome virus recognized by monoclonal antibodies using phage-display technology.
Article in Virus genes, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 6 citations in OpenAlex.
- Genetic diversity and pathogenicity of novel recombinant strains of PRRSV lineages 1.5, lineages 1.8 and lineages 8 in South China.Frontiers in cellular and infection microbiology · 2026Article
- Linear epitopes of PRRSV-1 envelope proteins ectodomains are not correlated with broad neutralization.Porcine health management · 2024Article
- Research Progress on Porcine Reproductive and Respiratory Syndrome Virus NSP7 Protein.Animals : an open access journal from MDPI · 2023Review
- Research Progress on the detection methods of porcine reproductive and respiratory syndrome virus.Frontiers in microbiology · 2023Review
- H1N1 influenza virus epitopes classified by monoclonal antibodies.Experimental and therapeutic medicine · 2018Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Nonstructural protein 7 (nsp7) of porcine reproductive and respiratory syndrome virus (PRRSV) is considered to be a suitable reagent for the development of serological diagnostic assays. It can be expressed as a soluble recombinant protein in Escherichia coli, and its antibody response may continue up to 202 days post-infection. Furthermore, the region encoded by nsp7 is highly homologous among various strains within the genotype, and the results of nsp7-based enzyme-linked immunosorbent assay (ELISA) showed high agreement with previous Idexx ELISA results. All these evidences suggest the existence of important epitopes on nsp7, though the characteristics of these epitopes remain unclear. In the present study, we prepared three monoclonal antibodies against nsp7 protein and used them to screen the epitope-distribution characteristics of PRRSV nsp7 protein by phage-display technology. We identified a linear epitope NAWGDEDRLN at amino acids 153-162 type II PRRSV nsp7β subunit. This newly defined epitope showed excellent reactivity with PRSSV-positive serum samples. These results further our understanding of the antigenic structure of nsp7 protein, and provide efficient reagents for PRRSV serological tests.
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