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Home / Equine Research Bank / J Virol / Structural Protein VP2 of African Horse Sickness Virus Is No...
Journal of virology2017; 91(4); doi: 10.1128/JVI.01328-16

Structural Protein VP2 of African Horse Sickness Virus Is Not Essential for Virus Replication In Vitro.

Abstract: The Reoviridae family consists of nonenveloped multilayered viruses with a double-stranded RNA genome consisting of 9 to 12 genome segments. The Orbivirus genus of the Reoviridae family contains African horse sickness virus (AHSV), bluetongue virus, and epizootic hemorrhagic disease virus, which cause notifiable diseases and are spread by biting Culicoides species. Here, we used reverse genetics for AHSV to study the role of outer capsid protein VP2, encoded by genome segment 2 (Seg-2). Expansion of a previously found deletion in Seg-2 indicates that structural protein VP2 of AHSV is not essential for virus replication in vitro In addition, in-frame replacement of RNA sequences in Seg-2 by that of green fluorescence protein (GFP) resulted in AHSV expressing GFP, which further confirmed that VP2 is not essential for virus replication. In contrast to virus replication without VP2 expression in mammalian cells, virus replication in insect cells was strongly reduced, and virus release from insect cells was completely abolished. Further, the other outer capsid protein, VP5, was not copurified with virions for virus mutants without VP2 expression. AHSV without VP5 expression, however, could not be recovered, indicating that outer capsid protein VP5 is essential for virus replication in vitro Our results demonstrate for the first time that a structural viral protein is not essential for orbivirus replication in vitro, which opens new possibilities for research on other members of the Reoviridae family. Members of the Reoviridae family cause major health problems worldwide, ranging from lethal diarrhea caused by rotavirus in humans to economic losses in livestock production caused by different orbiviruses. The Orbivirus genus contains many virus species, of which bluetongue virus, epizootic hemorrhagic disease virus, and African horse sickness virus (AHSV) cause notifiable diseases according to the World Organization of Animal Health. Recently, it has been shown that nonstructural proteins NS3/NS3a and NS4 are not essential for virus replication in vitro, whereas it is generally assumed that structural proteins VP1 to -7 of these nonenveloped, architecturally complex virus particles are essential. Here we demonstrate for the first time that structural protein VP2 of AHSV is not essential for virus replication in vitro Our findings are very important for virologists working in the field of nonenveloped viruses, in particular reoviruses.
Copyright © 2017 American Society for Microbiology.
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Publication Date: 2017-01-31 PubMed ID: 27903804PubMed Central: PMC5286882DOI: 10.1128/JVI.01328-16Google 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 research primarily focuses on understanding the role of a specific structural protein, VP2, in the replication of the African Horse Sickness Virus (AHSV). The study elucidates that VP2 is not essential for the in vitro replication of AHSV. However, another outer capsid protein, VP5, was found to be crucial for the virus’s reproduction. This new insight broadens the understanding of how nonenveloped viruses, like AHSV, function and replicate, offering avenues for further exploration in viral research.

Reoviridae Viruses

  • The Reoviridae family consists of nonenveloped, multilayered viruses with a double-stranded RNA genome typically comprising 9 to 12 genome segments.
  • Orbiviruses, a genre within this family, include AHSV, bluetongue virus, and epizootic hemorrhagic disease virus; all are transmitted by biting Culicoides species and cause notifiable diseases.
  • These viruses underpin significant health issues worldwide, such as lethal diarrhea caused by rotavirus in humans to economic losses in livestock production due to different orbiviruses.

Reverse Genetics and the Role of VP2

  • The researchers utilized reverse genetics to examine the function of the outer capsid protein VP2, encoded by genome segment 2 (Seg-2).
  • The study found that the VP2 protein is not indispensably required for virus replication in vitro. However, the replication in insect cells was greatly diminished without VP2, and virus release from insect cells was completely inhibited.
  • These findings suggest that while VP2 may not be essential for viral replication, it plays a significant role in infection transmission among insect vectors.

Role of VP5

  • The study also observed the role of VP5, the other outer capsid protein in the AHSV.
  • It was discovered that the absence of VP2 expression hindered the co-purification of VP5 with virions for virus mutants.
  • However, AHSV could not be recovered in instances where VP5 was not expressed, indicating its vital function for virus replication in vitro.

Significance of the Study

  • This research provides the first instance of a structural viral protein not being necessary for orbivirus replication.
  • These findings are of immense relevance for virologists working with nonenveloped viruses, specifically reoviruses, as they might help develop preventive measures or treatments for diseases caused by these viruses.
  • The study also offers a fresh perspective and lays a foundation for more research into the roles of other capsid and nonstructural proteins in the lifecycle of African Horse Sickness Virus and similar viruses.

Cite This Article

APA
van Gennip RGP, van de Water SGP, Potgieter CA, van Rijn PA. (2017). Structural Protein VP2 of African Horse Sickness Virus Is Not Essential for Virus Replication In Vitro. J Virol, 91(4). https://doi.org/10.1128/JVI.01328-16

Publication

Journal of virology
ISSN: 1098-5514
NlmUniqueID: 0113724
Country: United States
Language: English
Volume: 91
Issue: 4

Researcher Affiliations

van Gennip, René G P
  • Department of Virology, Central Veterinary Institute of Wageningen University and Research Centre, Lelystad, The Netherlands rene.vangennip@wur.nl.
van de Water, Sandra G P
  • Department of Virology, Central Veterinary Institute of Wageningen University and Research Centre, Lelystad, The Netherlands.
Potgieter, Christiaan A
  • Department of Biochemistry, Centre for Human Metabolomics, North-West University, Potchefstroom, South Africa.
  • Deltamune, Lyttelton, South Africa.
van Rijn, Piet A
  • Department of Virology, Central Veterinary Institute of Wageningen University and Research Centre, Lelystad, The Netherlands.
  • Department of Biochemistry, Centre for Human Metabolomics, North-West University, Potchefstroom, South Africa.

MeSH Terms

  • African Horse Sickness / virology
  • African Horse Sickness Virus / classification
  • African Horse Sickness Virus / physiology
  • Animals
  • Capsid Proteins / genetics
  • Capsid Proteins / metabolism
  • Cricetinae
  • Gene Expression
  • Gene Expression Regulation, Viral
  • Genome, Viral
  • Horses
  • Mice
  • Mutation
  • Phenotype
  • RNA, Double-Stranded
  • RNA, Viral
  • Sequence Deletion
  • Serogroup
  • Transcription, Genetic
  • Virus Release
  • Virus Replication

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