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Lentivirus cross-reactive determinants present in the capsid protein of equine infectious anaemia virus.
Abstract: In this study we used immune sera from equine infectious anaemia virus (EIAV)-infected horses which uniquely display broad reactivity with different lentivirus capsid proteins (CA) to characterize the cross-reactive determinants of lentivirus CA proteins. In particular, the role of the major homology region (MHR) of lentivirus CA proteins in this serological cross-reactivity was evaluated using both equine immune serum and murine monoclonal antibodies (MAbs) directed against the MHR segment of different lentiviruses. The results of our studies indicate that about 80% of sera from long-term experimentally infected ponies or naturally infected horses react with human immunodeficiency virus type 1 CA in Western immunoblot assays. In addition, the cross-reactive determinants on the EIAV CA were localized within the immunodominant carboxyl terminus of the protein (residues 277 to 367). However, the cross-reactive determinants recognized by the equine sera do not appear to correlate with linear peptides from the carboxyl terminus of the EIAV CA, including the MHR. These results suggest cross-reactivity between more distant lentiviruses is associated with non-linear determinants. In contrast, MHR-specific MAbs did react with linear peptides by ELISA and distinguished the primate lentiviruses from EIAV and feline immunodeficiency virus. These data support the concept of a highly conserved structural and antigenic organization among the CA proteins of lentiviruses from different species.
Publication Date: 1994-03-01 PubMed ID: 7510329DOI: 10.1099/0022-1317-75-3-657Google Scholar: Lookup The Equine Research Bank provides access to a large database of publicly available scientific literature. Inclusion in the Research Bank does not imply endorsement of study methods or findings by Mad Barn.
- Journal Article
- Research Support
- U.S. Gov't
- P.H.S.
Summary
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The research illustrated that sera from horses infected with equine infectious anaemia virus (EIAV) reacted extensively with the capsid proteins of various lentiviruses. The focal point of this analysis was the role of the major homology region (MHR) of lentivirus capsid proteins in this cross-reactivity. The outcome suggests that the reaction between remotely related lentiviruses is linked to non-linear determinants and reinforces the concept of a remarkably conserved structural organisation among lentiviruses from different species.
Study Objective and Methods
- The primary aim of the research was to characterise the cross-reactive determinants of lentivirus capsid (CA) proteins using immune sera from horses infected with equine infectious anaemia virus (EIAV), which uniquely reacts broadly with different lentivirus capsid proteins.
- The role of the major homology region (MHR), an essential region of lentivirus CA proteins, in this serological cross-reactivity was explored using equine immune serum and murine monoclonal antibodies (MAbs) directed against the MHR segment of different lentiviruses.
Results of the Study
- Approximately 80% of sera from long-term experimentally infected ponies or naturally infected horses responded with the human imunodeficiency virus type 1 CA in Western immunoblot assays. This indicates a strong cross-reactivity between the human immunodeficiency virus and EIAV.
- The cross-reactive determinants were localized within the immunodominant carboxyl terminus of the EIAV CA protein, specifically at residues 277 to 367.
- However, the cross-reactive determinants identified by the equine sera do not correlate with linear peptides from the carboxyl terminus of the EIAV CA, including the MHR. This suggests the cross-reactivity response does not work in a simple linear manner.
- In contrast, MHR-specific MAbs did react with linear peptides by ELISA (enzyme-linked immunosorbent assay) and differentiated primate lentiviruses from EIAV and feline immunodeficiency virus, suggesting a difference in their antigenic structures.
Implications of the Study
- The results of the study support the idea of a highly conserved structural and antigenic organization among the capsid proteins of lentiviruses from different species. This means that despite being diverse in their host species, these viruses share common structural features, which can trigger immune responses across these species.
- This consensus in structure can provide valuable insights for the development of a vaccine or treatment for infections caused by lentiviruses.
Cite This Article
APA
Grund CH, Lechman ER, Issel CJ, Montelaro RC, Rushlow KE.
(1994).
Lentivirus cross-reactive determinants present in the capsid protein of equine infectious anaemia virus.
J Gen Virol, 75 ( Pt 3), 657-662.
https://doi.org/10.1099/0022-1317-75-3-657 Publication
Researcher Affiliations
- Department of Molecular Genetics and Biochemistry, School of Medicine, University of Pittsburgh, Pennsylvania 15261.
MeSH Terms
- Amino Acid Sequence
- Animals
- Antibodies, Monoclonal
- Antigens, Viral / immunology
- Capsid / immunology
- Cross Reactions / immunology
- Epitopes / immunology
- Equine Infectious Anemia / immunology
- Horses
- Infectious Anemia Virus, Equine / immunology
- Lentivirus / immunology
- Molecular Sequence Data
- Prevalence
- Sensitivity and Specificity
Grant Funding
- R01 AI 25850 / NIAID NIH HHS
Citations
This article has been cited 10 times.- Craigo JK, Ezzelarab C, Cook SJ, Chong L, Horohov D, Issel CJ, Montelaro RC. Envelope determinants of equine lentiviral vaccine protection. PLoS One 2013;8(6):e66093.
- Issel CJ, Scicluna MT, Cook SJ, Cook RF, Caprioli A, Ricci I, Rosone F, Craigo JK, Montelaro RC, Autorino GL. Challenges and proposed solutions for more accurate serological diagnosis of equine infectious anaemia. Vet Rec 2013 Feb 23;172(8):210.
- Craigo JK, Ezzelarab C, Montelaro RC. Development of a high throughput, semi-automated, infectious center cell-based ELISA for equine infectious anemia virus. J Virol Methods 2012 Nov;185(2):221-7.
- Craigo JK, Zhang B, Barnes S, Tagmyer TL, Cook SJ, Issel CJ, Montelaro RC. Envelope variation as a primary determinant of lentiviral vaccine efficacy. Proc Natl Acad Sci U S A 2007 Sep 18;104(38):15105-10.
- Craigo JK, Durkin S, Sturgeon TJ, Tagmyer T, Cook SJ, Issel CJ, Montelaro RC. Immune suppression of challenged vaccinates as a rigorous assessment of sterile protection by lentiviral vaccines. Vaccine 2007 Jan 15;25(5):834-45.
- Stewart M, Desport M, Hartaningsih N, Wilcox G. TaqMan real-time reverse transcription-PCR and JDVp26 antigen capture enzyme-linked immunosorbent assay to quantify Jembrana disease virus load during the acute phase of in vivo infection. J Clin Microbiol 2005 Nov;43(11):5574-80.
- Craigo JK, Li F, Steckbeck JD, Durkin S, Howe L, Cook SJ, Issel C, Montelaro RC. Discerning an effective balance between equine infectious anemia virus attenuation and vaccine efficacy. J Virol 2005 Mar;79(5):2666-77.
- Lonning SM, Zhang W, McGuire TC. Gag protein epitopes recognized by CD4(+) T-helper lymphocytes from equine infectious anemia virus-infected carrier horses. J Virol 1999 May;73(5):4257-65.
- Langemeier JL, Cook SJ, Cook RF, Rushlow KE, Montelaro RC, Issel CJ. Detection of equine infectious anemia viral RNA in plasma samples from recently infected and long-term inapparent carrier animals by PCR. J Clin Microbiol 1996 Jun;34(6):1481-7.
- Darcel C. Lymphoid leukosis viruses, their recognition as 'persistent' viruses and comparisons with certain other retroviruses of veterinary importance. Vet Res Commun 1996;20(1):83-108.
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