ArticleThe Biochemical journal2003
Fine mapping of sequential neutralization epitopes on the subunit protein VP8 of human rotavirus.
Article in The Biochemical journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed, 37 citations in OpenAlex.
- Novel Universal Recombinant Rotavirus A Vaccine Candidate: Evaluation of Immunological Properties.Viruses · 2024Article
- Article
- Novel antigen panel for modern broad-spectrum recombinant rotavirus A vaccine.Clinical and experimental vaccine research · 2021Article
- Design strategies to address the effect of hydrophobic epitope on stability and in vitro assembly of modular virus-like particle.Protein science : a publication of the Protein Society · 2016Article
- A new rotavirus VP6-based foreign epitope presenting vector and immunoreactivity of VP4 epitope chimeric proteins.Viral immunology · 2014Article
- A dual chicken IgY against rotavirus and norovirus.Antiviral research · 2013Article
- Norovirus P particle, a novel platform for vaccine development and antibody production.Journal of virology · 2011Article
- Passive protection effect of chicken egg yolk immunoglobulins on enterovirus 71 infected mice.Vaccine · 2010Article
- Molecular characterization of a new variant of rotavirus P[8]G9 predominant in a sentinel-based survey in central Italy.Journal of clinical microbiology · 2007Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The epitopes of the HRV (human rotavirus), especially those involved in virus neutralization, have not been determined in their entirety, and would have significant implications for HRV vaccine development. In the present study, we report on the epitope mapping and identification of sequential neutralization epitopes, on the Wa strain HRV subunit protein VP8, using synthetic overlapping peptides. Polyclonal antibodies against recombinant Wa VP8 were produced previously in chicken, and purified from egg yolk, which showed neutralizing activity against HRV in vitro. Overlapping VP8 peptide fragments were synthesized and probed with the anti-VP8 antibodies, revealing five sequential epitopes on VP8. Further analysis suggested that three of the five epitopes detected, M1-L10, I55-D66 and L223-P234, were involved in virus neutralization, indicating that sequential epitopes may also be important for the HRV neutralization. The interactions of the antibodies with the five epitopes were characterized by an examination of the critical amino acids involved in antibody binding. Epitopes comprised primarily of hydrophobic amino acid residues, followed by polar and charged residues. The more critical amino acids appeared to be located near the centre of the epitopes, with proline, isoleucine, serine, glutamine and arginine playing an important role in the binding of antibody to the VP8 epitopes.
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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.