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The Journal of general virology1995; 76 ( Pt 10); 2607-2611; doi: 10.1099/0022-1317-76-10-2607

Proteolytic cleavage of VP2, an outer capsid protein of African horse sickness virus, by species-specific serum proteases enhances infectivity in Culicoides.

Abstract: Purified African horse sickness virus (AHSV) was fed, as part of a blood meal, to adult females from a susceptible colony of Culicoides variipennis, established in the insectories at the Institute for Animal Health, Pirbright Laboratory, UK. The meal consisted of heparinized blood obtained from ovine, bovine, equine (horse and donkey) or canine sources spiked with AHSV serotype 9 (AHSV9). The infectivity levels observed for C. variipennis varied significantly, according to the source of the blood sample. Comparison of the protein profiles obtained from AHSV9 incubated with the individual serum of plasma samples indicated that some species-specific serum proteases were able to cleave the outer capsid protein, VP2. The blood samples containing serum proteases that were able to cleave VP2 also showed an increase in infectivity for the insect vector when spiked with purified AHSV.
Publication Date: 1995-10-01 PubMed ID: 7595366DOI: 10.1099/0022-1317-76-10-2607Google Scholar: Lookup
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  • Journal Article
  • Research Support
  • Non-U.S. Gov't

Summary

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The research explores how proteins in different animal species can affect the infectivity of African horse sickness virus (AHSV) in a specific insect, Culicoides variipennis, which plays a role in the spread of the virus.

Study Design and Methodology

  • The researchers collected purified African horse sickness virus (AHSV) and used it in a blood meal fed to adult female Culicoides variipennis, insects from a susceptible colony in the UK.
  • The blood meal consisted of blood sourced from various animals—sheep, cows, horses, donkeys, and dogs—each spiked with a serotype of the AHSV virus, AHSV9.
  • The study aimed to compare the infectivity levels produced in C. variipennis after consumption of these different blood meals.

Findings of the Research

  • The infectivity levels of the virus, i.e., its ability to establish an infection in the insect vector, varied significantly depending on the source of the blood sample in the meal.
  • By comparing the protein profiles obtained from AHSV9 after incubation with blood of different species, they discovered that some species-specific serum proteases—a type of enzyme that cleaves proteins—were able to cleave the outer capsid protein of the virus, known as VP2.
  • The researchers found a correlation between the presence of these specific serum proteases and an increase in the virus’s infectivity for the insect vector. In other words, when AHSV was exposed to blood samples containing these proteases, it increased the ability of the virus to infect the C. variipennis insects.

Implications of the Study

  • The results of this study suggest that the species-specific serum proteases inherent in different animals’ blood could influence the spread and infection of AHSV.
  • This could have important implications for controlling and preventing the spread of AHSV, especially as it affects a variety of animals and can significantly affect populations of livestock like horses and cattle.
  • Further research could explore how modifying these serum proteases could potentially reduce infectivity of AHSV, providing a potential avenue for prevention and intervention in managing this disease.

Cite This Article

APA
Marchi PR, Rawlings P, Burroughs JN, Wellby M, Mertens PP, Mellor PS, Wade-Evans AM. (1995). Proteolytic cleavage of VP2, an outer capsid protein of African horse sickness virus, by species-specific serum proteases enhances infectivity in Culicoides. J Gen Virol, 76 ( Pt 10), 2607-2611. https://doi.org/10.1099/0022-1317-76-10-2607

Publication

ISSN: 0022-1317
NlmUniqueID: 0077340
Country: England
Language: English
Volume: 76 ( Pt 10)
Pages: 2607-2611

Researcher Affiliations

Marchi, P R
  • Institute for Animal Health, Pirbright Laboratory, Woking, Surrey, UK.
Rawlings, P
    Burroughs, J N
      Wellby, M
        Mertens, P P
          Mellor, P S
            Wade-Evans, A M

              MeSH Terms

              • African Horse Sickness Virus / pathogenicity
              • Animals
              • Blood
              • Capsid / metabolism
              • Capsid Proteins
              • Cattle
              • Ceratopogonidae / virology
              • Dogs
              • Endopeptidases / blood
              • Endopeptidases / metabolism
              • Equidae
              • Female
              • Horses
              • Insect Vectors / virology
              • Sheep
              • Species Specificity

              Citations

              This article has been cited 6 times.
              1. Vaughan JA, Newman RA, Turell MJ. Bird species define the relationship between West Nile viremia and infectiousness to Culex pipiens mosquitoes. PLoS Negl Trop Dis 2022 Oct;16(10):e0010835.
                doi: 10.1371/journal.pntd.0010835pubmed: 36201566google scholar: lookup
              2. Dennis SJ, Meyers AE, Hitzeroth II, Rybicki EP. African Horse Sickness: A Review of Current Understanding and Vaccine Development. Viruses 2019 Sep 11;11(9).
                doi: 10.3390/v11090844pubmed: 31514299google scholar: lookup
              3. Wilson AJ, Harrup LE. Reproducibility and relevance in insect-arbovirus infection studies. Curr Opin Insect Sci 2018 Aug;28:105-112.
                doi: 10.1016/j.cois.2018.05.007pubmed: 30551760google scholar: lookup
              4. Patel A, Roy P. The molecular biology of Bluetongue virus replication. Virus Res 2014 Mar;182:5-20.
              5. Manole V, Laurinmäki P, Van Wyngaardt W, Potgieter CA, Wright IM, Venter GJ, van Dijk AA, Sewell BT, Butcher SJ. Structural insight into African horsesickness virus infection. J Virol 2012 Aug;86(15):7858-66.
                doi: 10.1128/JVI.00517-12pubmed: 22593166google scholar: lookup
              6. Wilson A, Mellor PS, Szmaragd C, Mertens PP. Adaptive strategies of African horse sickness virus to facilitate vector transmission. Vet Res 2009 Mar-Apr;40(2):16.
                doi: 10.1051/vetres:2008054pubmed: 19094921google scholar: lookup