Serum and mucosal antibodies of infected foals recognized two distinct epitopes of VapA of Rhodococcus equi.
Abstract: Virulence-associated protein A (VapA) of Rhodococcus equi has been proposed for use both as a vaccine and as a target for antibodies in immunotherapy and diagnostic tests. Epitope mapping of VapA allowed the identification of two B cell epitopes associated with R. equi pneumonia. The peptide NLQKDEPGRASDT was confirmed as an immunodominant N-terminal B cell epitope recognized by all sera from infected foals while VSFQYNAVGPYLNINFFDSS (C-terminal B cell epitope) was exclusively recognized by IgA from the tracheal aspirates. Moreover, specific antibodies produced against the VapA-specific peptide reacted with a major protein (approximately 20 kDa) from R. equi antigens separated by two-dimensional gel electrophoresis. The strong reactivity of mucosal IgA from infected foals with the conserved peptides might constitute an attractive target for diagnosis and vaccine.
Publication Date: 2002-11-22 PubMed ID: 12443830DOI: 10.1111/j.1574-695X.2002.tb00637.xGoogle Scholar: Lookup
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- Journal Article
- Research Support
- Non-U.S. Gov't
Summary
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The study explores how antibodies in foals infected with Rhodococcus equi bacteria identify two unique segments of the bacterium’s virulence-associated protein A (VapA), offering potential routes for immunotherapy, vaccination, and diagnostic testing.
Understanding VapA of Rhodococcus equi
- The research revolves around a specific protein attached to the Rhodococcus equi bacterium, known as virulence-associated protein A (VapA).
- VapA is of significant interest to researchers because it has previously been suggested as a possible component in vaccines, as well as a target for antibodies in immunotherapy treatments and diagnostic tests for R. equi infection.
Identifying B cell epitopes
- The current study gained new insights into the operation of VapA through a technique known as epitope mapping, which identifies the specific parts of a protein that antibodies detect and interact with.
- This process resulted in the detection of two ‘B cell epitopes’ or the parts of VapA that B cells—the white blood cells responsible for secreting antibodies—recognize.
- These findings could help scientists understand how to potentially manipulate immune responses in cases of R. equi infection.
Interactions between antibodies and epitopes
- The two identified epitopes interacted with distinct antibodies found in infected foals.
- One segment, designated by the peptide NLQKDEPGRASDT, was identified by all sera (the portion of blood containing antibodies) taken from infected foals.
- Contrastingly, the other segment identified by the peptide VSFQYNAVGPYLNINFFDSS, was solely recognized by the antibody IgA gathered from tracheal aspirates.
Diagnostic and therapeutic implications
- One of the practical applications of these findings could be in creating diagnostic tests for R. equi.
- Additionally, it could potentially offer a target for designing effective immunotherapy treatments or vaccines against the bacteria.
- Overall, this research enhances our understanding of how the immune system of foals responds to R. equi infection and identifies potential avenues for future study and therapeutic development.
Cite This Article
APA
Taouji S, Bréard E, Peyret-Lacombe A, Pronost S, Fortier G, Collobert-Laugier C.
(2002).
Serum and mucosal antibodies of infected foals recognized two distinct epitopes of VapA of Rhodococcus equi.
FEMS Immunol Med Microbiol, 34(4), 299-306.
https://doi.org/10.1111/j.1574-695X.2002.tb00637.x Publication
Researcher Affiliations
- AFSSA, Laboratoire d'Etudes et de Recherches en Pathologie Equine, IPC, 14430 Goustranville, Dozulé, France. s.taouji@dozule.afssa.fr
MeSH Terms
- Actinomycetales Infections / immunology
- Actinomycetales Infections / veterinary
- Amino Acid Sequence
- Animals
- Antibodies, Viral / blood
- Antibodies, Viral / immunology
- Bacterial Proteins / chemistry
- Bacterial Proteins / genetics
- Bacterial Proteins / immunology
- Epitope Mapping
- Epitopes, B-Lymphocyte
- Horse Diseases / immunology
- Horse Diseases / microbiology
- Horses
- Immunodominant Epitopes
- Immunoglobulin A, Secretory / immunology
- Membrane Glycoproteins / chemistry
- Membrane Glycoproteins / genetics
- Membrane Glycoproteins / immunology
- Molecular Sequence Data
- Peptides / chemical synthesis
- Peptides / chemistry
- Peptides / immunology
- Rabbits
- Respiratory System / immunology
- Rhodococcus equi / immunology
- Virulence Factors
Citations
This article has been cited 4 times.- Alves GG, Machado-de-Ávila RA, Chávez-Olórtegui CD, Silva ROS, Lobato FCF. Mapping of the continuous epitopes displayed on the Clostridium perfringens type D epsilon-toxin. Braz J Microbiol 2017 Jul-Sep;48(3):570-575.
- Lewis MJ, Wagner B, Irvine RM, Woof JM. IgA in the horse: cloning of equine polymeric Ig receptor and J chain and characterization of recombinant forms of equine IgA. Mucosal Immunol 2010 Nov;3(6):610-21.
- Roncada P, Bonizzi L, Fortin R, Menandro ML, Greppi GF. A proteomic approach to investigate immunity against R. Equi in foals. Vet Res Commun 2005 Aug;29 Suppl 2:215-9.
- Kohler AK, Stone DM, Hines MT, Byrne BA, Alperin DC, Norton LK, Hines SA. Rhodococcus equi secreted antigens are immunogenic and stimulate a type 1 recall response in the lungs of horses immune to R. equi infection. Infect Immun 2003 Nov;71(11):6329-37.
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