Identification and characterization of a common B-cell epitope on EIAV capsid proteins.
Abstract: The equine infectious anemia virus (EIAV) capsid protein (p26) is one of the major immunogenic proteins during EIAV infection and is widely used for the detection of EIAV antibodies in horses. However, few reports have described the use of EIAV-specific monoclonal antibodies (MAbs) in etiological and immunological detection. Previously, we developed an antigen capture enzyme-linked immunosorbent assay (AC-ELISA) for the quantification of the EIAV p26 protein level. However, the epitopes recognized by the MAbs were not identified, and the utilization of the MAbs needs to be evaluated. In this study, we characterized two monoclonal antibodies (9H8 and 1G11 MAbs) against EIAV p26. Two B-cell epitopes are located in amino acid residues, NLDKIAEE (HE) and KNAMRHLRPEDTLEEKMYAC (GE) for the 9H8 and 1G11 MAbs, respectively. The 1G11 epitope (GE) varied among viruses isolated worldwide but can be recognized by anti-EIAV sera from different regions, including China, the USA, and Argentina. Meanwhile, 1G11 MAb could react with the mutants of almost all the EIAV strains. Furthermore, we found that the histidine at position 204 (H204), leucine at position 205 (L205), and aspartic acid at position 209 (D209) of EIAV p26 individually played pivotal roles in binding with the 1G11 MAb. Our results revealed that the GE peptide might be a common B-cell binding epitope of EIAV antibodies. This is also the first report to identify a broad-spectrum monoclonal antibody (1G11) against p26 of EIAV. These findings may provide a useful basis for the development of new diagnostic assays for EIAV.
Publication Date: 2016-09-23 PubMed ID: 27660181DOI: 10.1007/s00253-016-7817-9Google Scholar: Lookup
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- Journal Article
Summary
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This research involves understanding more about the antibodies produced by horses in response to equine infectious anemia virus (EIAV). The team examined how these antibodies interact with specific segments of protein found on the virus’ outer layer – uncovering potential targets for future treatments or diagnostic tests.
Study Background and Significance
- The equine infectious anemia virus (EIAV) is a serious disease in horses. It’s capsid (outer layer) protein p26 induces a significant immune response in infected animals.
- Being able to identify and characterize any potential antibodies against this capsid protein could potentially lead to the development of new diagnostic tools or treatments against EIAV.
- Antibodies have previously been generated for this purpose, but their specific targets (epitopes) on the capsid protein have not been fully elucidated.
Research Methodology
- This study used two different monoclonal antibodies that had previously shown reactivity against the EIAV capsid protein. These antibodies, named 9H8 and 1G11, were used to identify which segments of the protein they recognized.
- The team also analyzed how these antibodies reacted with viral strains from different geographical regions and with various strain mutants.
- The individual roles of specific residues in the capsid protein, particularly those at positions 204, 205, and 209, in binding with these antibodies were also extensively explored.
Major Findings
- Two epitopes were identified for these antibodies, marked by the amino acid residues NLDKIAEE (HE) and KNAMRHLRPEDTLEEKMYAC (GE).
- The GE epitope in particular demonstrated variability among viral mutations from around the world, but it could still be recognized by anti-EIAV sera from different regions.
- The monoclonal antibody 1G11 had a wide range of reactivity, recognizing mutations in almost all EIAV strains. Thus, it is deemed a broad-spectrum monoclonal antibody.
- Individual roles for the protein residues at positions 204, 205, and 209 in antibody binding were identified, highlighting important targets for potential interventions.
Conclusions and Implications
- The study suggests that the epitope GE could be a common binding site for broadly reactive B-cell antibodies, which are the type of antibodies that respond to infections and can potentially neutralize them.
- The identification of a broad-spectrum antibody offers promising implications for the development of new diagnostic tools or treatments for EIAV.
Cite This Article
APA
Hu Z, Chang H, Chu X, Li S, Wang M, Wang X.
(2016).
Identification and characterization of a common B-cell epitope on EIAV capsid proteins.
Appl Microbiol Biotechnol, 100(24), 10531-10542.
https://doi.org/10.1007/s00253-016-7817-9 Publication
Researcher Affiliations
- State Key Laboratory of Veterinary Biotechnology, Harbin Veterinary Research Institute, the Chinese Academy of Agriculture Sciences, 427 Maduan Street, Harbin, 150001, People's Republic of China.
- State Key Laboratory of Veterinary Biotechnology, Harbin Veterinary Research Institute, the Chinese Academy of Agriculture Sciences, 427 Maduan Street, Harbin, 150001, People's Republic of China.
- State Key Laboratory of Veterinary Biotechnology, Harbin Veterinary Research Institute, the Chinese Academy of Agriculture Sciences, 427 Maduan Street, Harbin, 150001, People's Republic of China.
- State Key Laboratory of Veterinary Biotechnology, Harbin Veterinary Research Institute, the Chinese Academy of Agriculture Sciences, 427 Maduan Street, Harbin, 150001, People's Republic of China.
- State Key Laboratory of Veterinary Biotechnology, Harbin Veterinary Research Institute, the Chinese Academy of Agriculture Sciences, 427 Maduan Street, Harbin, 150001, People's Republic of China.
- State Key Laboratory of Veterinary Biotechnology, Harbin Veterinary Research Institute, the Chinese Academy of Agriculture Sciences, 427 Maduan Street, Harbin, 150001, People's Republic of China. xjw@hvri.ac.cn.
MeSH Terms
- Antibodies, Monoclonal / immunology
- Antibodies, Viral / immunology
- Argentina
- China
- Epitope Mapping
- Epitopes, B-Lymphocyte / immunology
- Infectious Anemia Virus, Equine / immunology
- Infectious Anemia Virus, Equine / isolation & purification
- United States
- Viral Core Proteins / immunology
Citations
This article has been cited 6 times.- Hu Z, Guo K, Du C, Sun J, Naletoski I, Chu X, Lin Y, Wang X, Barrandeguy M, Samuel M, Wang W, Lau PI, Wernery U, Raghavan R, Wang X. Development and evaluation of a blocking ELISA for serological diagnosis of equine infectious anemia.. Appl Microbiol Biotechnol 2023 May;107(10):3305-3317.
- Duan Y, Wang X, Sun K, Lin Y, Wang X, Chen K, Yang G, Wang X, Du C. SYNJ2BP Improves the Production of Lentiviral Envelope Protein by Facilitating the Formation of Mitochondrion-Associated Endoplasmic Reticulum Membrane.. J Virol 2022 Oct 26;96(20):e0054922.
- Li W, Li M, Zhang H, Li C, Xu H, Gong B, Fu J, Guo Z, Peng J, Zhou G, Tian Z, Wang Q. A Novel Immunochromatographic Strip Based on Latex Microspheres for the Rapid Detection of North American-Type Porcine Reproductive and Respiratory Syndrome Virus.. Front Microbiol 2022;13:882112.
- Ren H, Yin X, Su C, Guo M, Wang XF, Na L, Lin Y, Wang X. Equine lentivirus counteracts SAMHD1 restriction by Rev-mediated degradation of SAMHD1 via the BECN1-dependent lysosomal pathway.. Autophagy 2021 Oct;17(10):2800-2817.
- 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).
- Ji S, Na L, Ren H, Wang Y, Wang X. Equine Myxovirus Resistance Protein 2 Restricts Lentiviral Replication by Blocking Nuclear Uptake of Capsid Protein.. J Virol 2018 Sep 15;92(18).
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