ArticleVirus genes2015
Phage display for identifying peptides that bind the spike protein of transmissible gastroenteritis virus and possess diagnostic potential.
Article in Virus genes, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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Who cites it
8 citing papers in PubMed, 17 citations in OpenAlex.
- A novel linear B-cell epitope on S2 protein of transmissible gastroenteritis virus identified using a monoclonal antibody.BMC veterinary research · 2025Article
- Immunoinformatics method to design universal multi-epitope nanoparticle vaccine for TGEV S protein.Scientific reports · 2025Article
- Development and Immunogenicity Study of Subunit Vaccines Based on Spike Proteins of Porcine Epidemic Diarrhea Virus and Porcine Transmissible Gastroenteritis Virus.Veterinary sciences · 2025Article
- Phage Display Technology in Biomarker Identification with Emphasis on Non-Cancerous Diseases.Molecules (Basel, Switzerland) · 2024Review
- Phage Display Technique as a Tool for Diagnosis and Antibody Selection for Coronaviruses.Current microbiology · 2021Review
- Porcine IL-12 plasmid as an adjuvant improves the cellular and humoral immune responses of DNA vaccine targeting transmissible gastroenteritis virus spike gene in a mouse model.The Journal of veterinary medical science · 2019Article
- A Single Domain-Based Anti-Her2 Antibody Has Potent Antitumor Activities.Translational oncology · 2018Article
- Phage display as a promising approach for vaccine development.Journal of biomedical science · 2016Review
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The spike (S) protein of porcine transmissible gastroenteritis virus (TGEV) is located within the viral envelope and is the only structural protein that possesses epitopes capable of inducing virus-neutralizing antibodies. Among the four N-terminal antigenic sites A, B, C, and D, site A and to a lesser extent site D (S-AD) induce key neutralizing antibodies. Recently, we expressed S-AD (rS-AD) in recombinant form. In the current study, we used the rS-AD as an immobilized target to identify peptides from a phage-display library with application for diagnosis. Among the 9 phages selected that specifically bound to rS-AD, the phage bearing the peptide TLNMHLFPFHTG bound with the highest affinity and was subsequently used to develop a phage-based ELISA for TGEV. When compared with conventional antibody-based ELISA, phage-mediated ELISA was more sensitive; however, it did not perform better than semi-quantitative RT-PCR, though phage-mediated ELISA was quicker and easier to set up.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.