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Home / Equine Research Bank / J Virol / Structural insight into African horsesickness virus infectio...
Journal of virology2012; 86(15); 7858-7866; doi: 10.1128/JVI.00517-12

Structural insight into African horsesickness virus infection.

Abstract: African horsesickness (AHS) is a devastating disease of horses. The disease is caused by the double-stranded RNA-containing African horsesickness virus (AHSV). Using electron cryomicroscopy and three-dimensional image reconstruction, we determined the architecture of an AHSV serotype 4 (AHSV-4) reference strain. The structure revealed triple-layered AHS virions enclosing the segmented genome and transcriptase complex. The innermost protein layer contains 120 copies of VP3, with the viral polymerase, capping enzyme, and helicase attached to the inner surface of the VP3 layer on the 5-fold axis, surrounded by double-stranded RNA. VP7 trimers form a second, T=13 layer on top of VP3. Comparative analyses of the structures of bluetongue virus and AHSV-4 confirmed that VP5 trimers form globular domains and VP2 trimers form triskelions, on the virion surface. We also identified an AHSV-7 strain with a truncated VP2 protein (AHSV-7 tVP2) which outgrows AHSV-4 in culture. Comparison of AHSV-7 tVP2 to bluetongue virus and AHSV-4 allowed mapping of two domains in AHSV-4 VP2, and one in bluetongue virus VP2, that are important in infection. We also revealed a protein plugging the 5-fold vertices in AHSV-4. These results shed light on virus-host interactions in an economically important orbivirus to help the informed design of new vaccines.
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Publication Date: 2012-05-16 PubMed ID: 22593166PubMed Central: PMC3421665DOI: 10.1128/JVI.00517-12Google Scholar: Lookup
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Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

The researchers explored the structure of the African horsesickness virus (AHSV), a deadly disease that affects horses, using electron cryomicroscopy and three-dimensional image reconstruction. The study offers new insight into the virus-host interactions that can help to design new vaccines.

Methodology and Key Findings

  • The research team used electron cryomicroscopy and three-dimensional image reconstruction to determine the structure of an AHSV serotype 4 (AHSV-4) reference strain.
  • They discovered that the segmented genome and transcriptase complex of the virus were enclosed in a triple-layered structure, known as AHS virions.
  • The innermost protein layer contained 120 copies of VP3. The viral polymerase, a capping enzyme, and a helicase were found attached to the inner surface of this layer along a 5-fold axis. This was surrounded by double-stranded RNA.
  • The team found that VP7 trimers formed a second layer (referred as T=13 layer) on top of the VP3 layer.
  • Comparing the structures of bluetongue virus and AHSV-4 allowed researchers to confirm that VP5 trimers form globular domains and VP2 trimers create triskelions on the surface of the virion.

Detailed Analysis and Conclusion

  • Researchers also identified a strain of AHSV-7 with a truncated VP2 protein, known as AHSV-7 tVP2. It was found that this strain outgrows AHSV-4 in culture.
  • Comparative analysis of the AHSV-7 tVP2 with the bluetongue virus and AHSV-4 enabled the mapping of two domains in AHSV-4 VP2. They also identified one domain in the bluetongue virus VP2 that plays a significant role in the infection process.
  • A protein blocking the 5-fold vertices in AHSV-4 was discovered.
  • These findings offer vital insights into how the virus interacts with its host. They can guide to the development of new vaccines to combat the African horsesickness disease.

Cite This Article

APA
Manole V, Laurinmäki P, Van Wyngaardt W, Potgieter CA, Wright IM, Venter GJ, van Dijk AA, Sewell BT, Butcher SJ. (2012). Structural insight into African horsesickness virus infection. J Virol, 86(15), 7858-7866. https://doi.org/10.1128/JVI.00517-12

Publication

Journal of virology
ISSN: 1098-5514
NlmUniqueID: 0113724
Country: United States
Language: English
Volume: 86
Issue: 15
Pages: 7858-7866

Researcher Affiliations

Manole, Violeta
  • Institute of Biotechnology, University of Helsinki, Helsinki, Finland.
Laurinmäki, Pasi
    Van Wyngaardt, Wouter
      Potgieter, Christiaan A
        Wright, Isabella M
          Venter, Gert J
            van Dijk, Alberdina A
              Sewell, B Trevor
                Butcher, Sarah J

                  MeSH Terms

                  • African Horse Sickness / metabolism
                  • African Horse Sickness Virus / metabolism
                  • African Horse Sickness Virus / ultrastructure
                  • Animals
                  • Capsid Proteins / chemistry
                  • Capsid Proteins / metabolism
                  • Chlorocebus aethiops
                  • Horses / virology
                  • Models, Molecular
                  • RNA, Double-Stranded / chemistry
                  • RNA, Double-Stranded / metabolism
                  • RNA, Viral / chemistry
                  • RNA, Viral / metabolism
                  • RNA-Dependent RNA Polymerase / chemistry
                  • RNA-Dependent RNA Polymerase / metabolism
                  • Structure-Activity Relationship
                  • Vero Cells
                  • Viral Core Proteins / chemistry
                  • Viral Core Proteins / metabolism
                  • Virion / metabolism
                  • Virion / ultrastructure

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