Systematic epitope analysis of the p26 EIAV core protein.
Abstract: The major core protein of equine infectious anemia virus (EIAV), p26, is one of the primary immunogenic structural proteins during a persistent infection of horses and is highly conserved among antigenically variants of viral isolates. In order to investigate its immune profile in more detail for a better diagnostic, an epitope mapping was carried out by means of two libraries of overlapping peptide fragments prepared by simultaneous and parallel SPPS on derivatized cellulose membranes (SPOT synthesis). Polyclonal equine sera from infected horses were used for the biological assay. Particularly two promising continuous epitopes (NAMRHL and MYACRD) were localized on the C-terminal extreme of p26, region 194-222. A cyclic synthetic fragment of 29 amino acid residues containing the identified epitopes was designed and studied. A significant conformational change towards a helical structure was observed when the peptide was cyclized by a bridge between Cys198 and Cys218. This observation correlated with an improvement of its ability to be recognized by specific antibodies in an EIA (Enzyme-linked Immunosorbent assay). These results suggest that the conformationally restricted synthetic antigen adequately mimics the native structure of this region of p26 core protein.
(c) 2007 John Wiley & Sons, Ltd.
Publication Date: 2007-08-21 PubMed ID: 17705340DOI: 10.1002/jmr.825Google Scholar: Lookup
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- Journal Article
- Research Support
- Non-U.S. Gov't
Summary
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The research aims to study the immune profile of the p26 protein of the equine infectious anemia virus (EIAV) by identifying specific parts of the protein that induce an immune response.
Objectives of the study
- The objective of this study was to improve the understanding of the immune response to the one of the primary immunogenic structural proteins of the equine infectious anemia virus (EIAV), which is a persistent infection in horses, known as p26.
- The researchers used a method called epitope mapping to identify specific parts of the p26 protein that were recognized by the antibodies in equine blood samples.
Methods used in the study
- The study used two libraries of overlapping peptide fragments prepared by simultaneous and parallel Solid Phase Peptide Synthesis (SPPS), on derivatized cellulose membranes, also known as SPOT synthesis.
- Equine blood samples from infected horses were used in a biological assay to study the immune response.
Key findings of the study
- Two promising continuous epitopes were found on the C-terminal region of the protein, in sections NAMRHL and MYACRD.
- The researchers designed and studied a cyclic synthetic fragment containing the identified epitopes.
- The researchers noted a significant conformational change towards a helical structure when the peptide was cyclized by a bridge between amino acids at positions 198 and 218.
- This conformational change also improved the peptide’s ability to be recognized by specific antibodies in an Enzyme-linked Immunosorbent Assay (EIA).
Conclusions of the study
- Overall, this study suggests that introducing a cyclic constraint into the peptide structure enhances its similarity to the native p26 protein structure.
- This has potential implications in diagnostics and vaccine development against EIAV, by mimicking the native structure of the protein and promoting a stronger immune response.
Cite This Article
APA
Soutullo A, Santi MN, Perin JC, Beltramini LM, Borel IM, Frank R, Tonarelli GG.
(2007).
Systematic epitope analysis of the p26 EIAV core protein.
J Mol Recognit, 20(4), 227-237.
https://doi.org/10.1002/jmr.825 Publication
Researcher Affiliations
- Laboratorio de Inmunoquímica, Dirección de Sanidad Animal, Ministerio de la Producción, Bv. Pellegrini 3100, Santa Fe, Argentina.
MeSH Terms
- Amino Acid Sequence
- Epitope Mapping / methods
- Models, Molecular
- Molecular Sequence Data
- Peptide Fragments / analysis
- Protein Array Analysis
- Protein Structure, Secondary
- Protein Structure, Tertiary
- Viral Core Proteins / analysis
- Viral Core Proteins / chemistry
- Viral Core Proteins / immunology
- Viral Core Proteins / metabolism
Citations
This article has been cited 4 times.- Malossi CD, Fioratti EG, Cardoso JF, Magro AJ, Kroon EG, Aguiar DM, Borges AMCM, Nogueira MF, Ullmann LS, Araujo JP Jr. High Genomic Variability in Equine Infectious Anemia Virus Obtained from Naturally Infected Horses in Pantanal, Brazil: An Endemic Region Case.. Viruses 2020 Feb 12;12(2).
- Trier NH, Holm BE, Slot O, Locht H, Lindegaard H, Svendsen A, Houen G. Physical Characteristics of a Citrullinated Pro-Filaggrin Epitope Recognized by Anti-Citrullinated Protein Antibodies in Rheumatoid Arthritis Sera.. PLoS One 2016;11(12):e0168542.
- Ferreira de Lima Neto D, Bonafe CF, Arns CW. Influence of high hydrostatic pressure on epitope mapping of tobacco mosaic virus coat protein.. Viral Immunol 2014 Mar;27(2):60-74.
- Faria AR, Costa MM, Giusta MS, Grimaldi G Jr, Penido ML, Gazzinelli RT, Andrade HM. High-throughput analysis of synthetic peptides for the immunodiagnosis of canine visceral leishmaniasis.. PLoS Negl Trop Dis 2011 Sep;5(9):e1310.
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