ArticleVirus genes2013
Identification of a conserved B-cell epitope in the equine arteritis virus (EAV) N protein using the pepscan technique.
Article in Virus genes, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
3 citing papers in PubMed, 8 citations in OpenAlex.
- Article
- Research advances in hydrogen-deuterium exchange mass spectrometry for protein epitope mapping.Analytical and bioanalytical chemistry · 2021Review
- Identification of a potential neutralizing linear epitope of hemagglutinin-neuraminidase in Newcastle disease virus.Virology journal · 2021Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The nucleocapsid (N) gene of equine arteritis virus (EAV) is highly conserved between isolates, and the N protein is an important antigen that induces immunity when horses are infected with EAV. This study describes the identification of a linear B-cell epitope on the N protein using the pepscan technique with a monoclonal antibody (mAb) 2B1 directed against the N protein. The N protein was divided into 11 overlapping peptides, each containing 16 amino acids associated with six overlapping amino acids. The fragments were expressed as MBP fusion proteins that were then used to probe the 2B1 mAb. The minimal epitope sequence was confirmed step-by-step using single amino acid residue deletion. One completely conserved linear epitope ((38)KPPAQP(43)) was identified that matched with EAV-positive serum in Western blots, thereby revealing the importance of these six amino acids of the epitope for antibody-epitope binding activity. This finding not only contributes to our understanding of the antigenic structure of the N protein of EAV but also has potential for the development of diagnostic techniques.
Indexed as
Identifiers
What OpenQuestion holds
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.