Molecular analysis of the proviral DNA of equine infectious anemia virus in mules in Greece.
- Comparative Study
- Journal Article
- Research Support
- Non-U.S. Gov't
Summary
This research article discusses a molecular analysis of certain genetic sequences in mules affected by the equine infectious anemia virus (EIAV) in Greece. The analysis found significant variations in these sequences, particularly the gp90 surface protein, when compared to each other and to already published strains of the virus.
Understanding the Research
This research is focused on EIAV, a virus that can severely impact a horse’s immune system and cause high mortality rates in animals, particularly mules in this study. The researchers had previously reported on the clinical and laboratory findings of infected animals and decided to delve deeper into their genetic structure.
They investigated the genetic segments of EIAV that play a critical role in the structure and functionality of the virus. These include:
- The integrase – an enzyme vital for the virus’s ability to integrate its genetic material with that of the host cell.
- The gp90 – a surface protein on the virus that allows it to bind to and infect host cells.
- The tat – a regenerative protein that boosts virus production in infected cells.
- The fusion domain of gp45 – another surface protein that fuses the virus with the cell membrane, enabling entry into the host cell.
Major Findings
The researchers sequenced these fragments from the viral genome in the infected mules, both naturally infected and experimentally inoculated. They discovered significant variations among these samples and also when compared to previously documented EIAV strains.
For the gp90 surface protein:
- In the naturally infected animals (wild type), there were substitutions in the V5 hypervariable domain – a region of the protein that can readily change and evolve.
- In the experimentally inoculated animals and the donor strain, variations occurred due to insertions/duplications in the V3 principal neutralizing domain, which plays a crucial role in controlling and suppressing the virus, and further substitutions in the V5 hypervariable domain.
- When compared to previously documented strains, the wild type samples displayed single amino acid substitutions across the whole protein and multiple substitutions in the V4-V6 variable domains. These changes can significantly affect the virus’s characteristics and its interaction with the immune system.
Conclusion
The study showed that the EIAV strains in the Greek mules were more similar to two American strains (WSU5 and Massachusetts) than to the two Japanese (V26 and V70) or the third American strain (Wyoming_wi) used for comparison in the study. These findings may be valuable for understanding the spread and evolution of EIAV and could potentially influence strategies for controlling and treating the infection.
Cite This Article
Publication
Researcher Affiliations
- Laboratory of Microbiology and Infectious Diseases, Faculty of Veterinary Medicine, Aristotle University of Thessaloniki, Thessaloniki GR-54124, Greece.
MeSH Terms
- Amino Acid Sequence
- Animals
- DNA, Viral / genetics
- Equidae / virology
- Genes, Viral
- Greece
- Infectious Anemia Virus, Equine / classification
- Infectious Anemia Virus, Equine / genetics
- Infectious Anemia Virus, Equine / isolation & purification
- Molecular Sequence Data
- Protein Structure, Tertiary
- Proviruses / genetics
- Proviruses / isolation & purification
- Sequence Homology, Amino Acid
- Viral Proteins / chemistry
- Viral Proteins / genetics
Citations
This article has been cited 2 times.- Han X, Zhang P, Yu W, Xiang W, Li X. Amino acid mutations in the env gp90 protein that modify N-linked glycosylation of the Chinese EIAV vaccine strain enhance resistance to neutralizing antibodies. Virus Genes 2016 Dec;52(6):814-822.
- Gonzálvez M, Franco JJ, Cano-Terriza D, Barbero-Moyano J, Jose-Cunilleras E, García J, Alguacil E, García-Bocanegra I. Equine Infectious Anemia Virus in Equids: A Large-Scale Serosurvey in Western Europe. Animals (Basel) 2025 Dec 4;15(23).