FREE SHIPPING over $40
OVER 10000 FIVE-STAR REVIEWS
5% OFF ALL SUBSCRIPTIONS
100% HAPPINESS GUARANTEE
Analyze Diet
0
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.
Get Full Text
Publication Date: 2017-01-31 PubMed ID: 27903804PubMed Central: PMC5286882DOI: 10.1128/JVI.01328-16Google 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.
LinkedInCopy
  • Journal Article
  • Research Support
  • Non-U.S. Gov't

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

References

This article includes 67 references
  1. Attoui H, Mertens P, Becnel J, Belaganahalli S, Bergoin M, Brussaard CP, Chappel JD, Ciarlet M, del Vas M. Orthoreovirus, Reoviridae. 2011 p 546–554 In King AMQ, Adams MJ, Carstens EB, Lefkowitz EJ (ed), Virus taxonomy. Classification and nomenclature of viruses. Ninth Report of the International Committee on Taxonomy of Viruses. Elsevier Academic Press, San Diego, CA.
  2. Attoui H, Maan S, Anthony S, Mertens PPC. Bluetongue virus, other orbiviruses and other reoviruses: their relationships and taxonomy. 2009 p 23–46 In Mellor P, Baylis M, Mertens P (ed), Biology of animal infections: bluetongue. Academic Press, Amsterdam, The Netherlands.
  3. Mertens PPC, Maan S, Samuel A, Attoui H. Orbivirus, Reoviridae. 2005 p 466–483 In Fauquet CM, Mayo MA, Maniloff J, Desselberger U, Ball LA (ed), Virus taxonomy. Eighth Report of the International Committee on Taxonomy of Viruses. Elsevier/Academic Press, London, United Kingdom.
  4. Howell PG. The isolation and identification of further antigenic types of African horsesickness virus. Onderstepoort J Vet Res 1962 29:139–149.
  5. McIntosh BM. Immunological types of horsesickness virus and their significance in immunization. Onderstepoort J Vet Res 1958 27:465–538.
  6. Erasmus BJ. The pathogenesis of African horsesickness. 1972 p 1–11 In Proceedings of the 3rd International Conference on Equine Infectious Diseases, Paris, France.
  7. Coetzer JA, Erasmus BJ. African horsesickness. 1994 p 460–475 In Tustin RC, Coetzer JAW (ed), Infectious disease of livestock with special reference to southern Africa, vol 1 Oxford University Press, Oxford, United Kingdom.
  8. Howell PG. The 1960 epizootic of African horsesickness in the Middle East and SW Asia. J South Afr Vet Assoc 1960 31:329–335.
  9. Lubroth J. African horsesickness and the epizootic in Spain 1987. Equine Pract 1988 10:26–33.
  10. Mellor PS, Hamblin C. African horse sickness. Vet Res 2004 35:445–466.
    doi: 10.1051/vetres:2004021pubmed: 15236676google scholar: lookup
  11. Mirchamsy H, Hazrati A. A review of the aetiology and pathologyof African horsesickness. Arch Hessarek Iran 1973 25:23–46.
  12. Rafyi A. Horse sickness. Bull Off Int Epizoot 1961 56:216–250.
  13. Meiswinkel R, Paweska JT. Evidence for a new field Culicoides vector of African horse sickness in South Africa. Prev Vet Med 2003 60:243–253.
    doi: 10.1016/S0167-5877(02)00231-3pubmed: 12900162google scholar: lookup
  14. Mellor PS, Boorman J, Baylis M. Culicoides biting midges: their role as arbovirus vectors. Annu Rev Entomol 2000 45:307–340.
    doi: 10.1146/annurev.ento.45.1.307pubmed: 10761580google scholar: lookup
  15. Venter GJ, Wright IM, Van Der Linde TC, Paweska JT. The oral susceptibility of South African field populations of Culicoides to African horse sickness virus. Med Vet Entomol 2009 23:367–378.
    doi: 10.1111/j.1365-2915.2009.00829.xpubmed: 19941602google scholar: lookup
  16. Hewat EA, Booth TF, Roy P. Structure of bluetongue virus particles by cryoelectron microscopy. J Struct Biol 1992 109:61–69.
    doi: 10.1016/1047-8477(92)90068-Lpubmed: 1337461google scholar: lookup
  17. Roy P. Functional mapping of bluetongue virus proteins and their interactions with host proteins during virus replication. Cell Biochem Biophys 2008 50:143–157.
    doi: 10.1007/s12013-008-9009-4pubmed: 18299997google scholar: lookup
  18. Roy P. Bluetongue virus proteins and particles and their role in virus entry, assembly, and release. Adv Virus Res 2005 64:69–123.
    doi: 10.1016/S0065-3527(05)64004-3pubmed: 16139593google scholar: lookup
  19. Belhouchet M, Mohd Jaafar F, Firth AE, Grimes JM, Mertens PP, Attoui H. Detection of a fourth orbivirus non-structural protein. PLoS One 2011 6:e25697.
    doi: 10.1371/journal.pone.0025697pmc: PMC3192121pubmed: 22022432google scholar: lookup
  20. Ratinier M, Caporale M, Golder M, Franzoni G, Allan K, Nunes SF, Armezzani A, Bayoumy A, Rixon F, Shaw A, Palmarini M. Identification and characterization of a novel non-structural protein of bluetongue virus. PLoS Pathog 2011 7:e1002477.
    doi: 10.1371/journal.ppat.1002477pmc: PMC3248566pubmed: 22241985google scholar: lookup
  21. Zwart L, Potgieter CA, Clift SJ, van Staden V. Characterising non-structural protein NS4 of African horse sickness virus. PLoS One 2015 10:e0124281.
    doi: 10.1371/journal.pone.0124281pmc: PMC4411093pubmed: 25915516google scholar: lookup
  22. Stewart M, Hardy A, Barry G, Pinto RM, Caporale M, Melzi E, Hughes J, Taggart A, Janowicz A, Varela M, Ratinier M, Palmarini M. Characterization of a second open reading frame in genome segment 10 of bluetongue virus. J Gen Virol 2015 96:3280–3293.
    doi: 10.1099/jgv.0.000267pmc: PMC4806581pubmed: 26290332google scholar: lookup
  23. van Gennip RG, van de Water SG, van Rijn PA. Bluetongue virus nonstructural protein NS3/NS3a is not essential for virus replication. PLoS One 2014 9:e85788.
    doi: 10.1371/journal.pone.0085788pmc: PMC3896414pubmed: 24465709google scholar: lookup
  24. Lourenco S, Roy P. In vitro reconstitution of bluetongue virus infectious cores. Proc Natl Acad Sci U S A 2011 108:13746–13751.
    doi: 10.1073/pnas.1108667108pmc: PMC3158217pubmed: 21808007google scholar: lookup
  25. van de Water SG, van Gennip RG, Potgieter CA, Wright IM, van Rijn PA. VP2 exchange and NS3/NS3a deletion in African horse sickness virus (AHSV) in development of disabled infectious single animal vaccine candidates for AHSV. J Virol 2015 89:8764–8772.
    doi: 10.1128/JVI.01052-15pmc: PMC4524073pubmed: 26063433google scholar: lookup
  26. Feenstra F, Drolet BS, Boonstra J, van Rijn PA. Non-structural protein NS3/NS3a is required for propagation of bluetongue virus in Culicoides sonorensis. Parasit Vectors 2015 8:476.
    doi: 10.1186/s13071-015-1063-3pmc: PMC4573936pubmed: 26383094google scholar: lookup
  27. Huismans H, Erasmus BJ. Identification of the serotype-specific and group-specific antigens of bluetongue virus. Onderstepoort J Vet Res 1981 48:51–58.
    pubmed: 6273773
  28. Maan S, Maan NS, Samuel AR, Rao S, Attoui H, Mertens PP. Analysis and phylogenetic comparisons of full-length VP2 genes of the 24 bluetongue virus serotypes. J Gen Virol 2007 88:621–630.
    doi: 10.1099/vir.0.82456-0pubmed: 17251581google scholar: lookup
  29. Burrage TG, Trevejo R, Stone-Marschat M, Laegreid WW. Neutralizing epitopes of African horsesickness virus serotype 4 are located on VP2. Virology 1993 196:799–803.
    doi: 10.1006/viro.1993.1537pubmed: 7690505google scholar: lookup
  30. Castillo-Olivares J, Calvo-Pinilla E, Casanova I, Bachanek-Bankowska K, Chiam R, Maan S, Nieto JM, Ortego J, Mertens PP. A modified vaccinia Ankara virus (MVA) vaccine expressing African horse sickness virus (AHSV) VP2 protects against AHSV challenge in an IFNAR−/− mouse model. PLoS One 2011 6:e16503.
    doi: 10.1371/journal.pone.0016503pmc: PMC3027694pubmed: 21298069google scholar: lookup
  31. Martinez-Torrecuadrada JL, Casal JI. Identification of a linear neutralization domain in the protein VP2 of African horse sickness virus. Virology 1995 210:391–399.
    doi: 10.1006/viro.1995.1355pubmed: 7542417google scholar: lookup
  32. Scanlen M, Paweska JT, Verschoor JA, van Dijk AA. The protective efficacy of a recombinant VP2-based African horsesickness subunit vaccine candidate is determined by adjuvant. Vaccine 2002 20:1079–1088.
    doi: 10.1016/S0264-410X(01)00445-5pubmed: 11803068google scholar: lookup
  33. Martinez-Torrecuadrada JL, Langeveld JP, Meloen RH, Casal JI. Definition of neutralizing sites on African horse sickness virus serotype 4 VP2 at the level of peptides. J Gen Virol 2001 82:2415–2424.
    doi: 10.1099/0022-1317-82-10-2415pubmed: 11562535google scholar: lookup
  34. DeMaula CD, Bonneau KR, MacLachlan NJ. Changes in the outer capsid proteins of bluetongue virus serotype ten that abrogate neutralization by monoclonal antibodies. Virus Res 2000 67:59–66.
    doi: 10.1016/S0168-1702(00)00130-1pubmed: 10773319google scholar: lookup
  35. Wilson WC, Bernard KA, Israel BA, Mecham JO. Bluetongue virus serotype 17 sequence variation associated with neutralization. DNA Seq 2008 19:237–240.
    doi: 10.1080/10425170701550524pubmed: 17852347google scholar: lookup
  36. Gould AR, Eaton BT. The amino acid sequence of the outer coat protein VP2 of neutralizing monoclonal antibody-resistant, virulent and attenuated bluetongue viruses. Virus Res 1990 17:161–172.
    doi: 10.1016/0168-1702(90)90062-Gpubmed: 1706548google scholar: lookup
  37. Pierce CM, Rossitto PV, MacLachlan NJ. Homotypic and heterotypic neutralization determinants of bluetongue virus serotype 17. Virology 1995 209:263–267.
    doi: 10.1006/viro.1995.1253pubmed: 7538255google scholar: lookup
  38. Kanai Y, van Rijn PA, Maris-Veldhuis M, Kaname Y, Athmaram TN, Roy P. Immunogenicity of recombinant VP2 proteins of all nine serotypes of African horse sickness virus. Vaccine 2014 32:4932–4937.
    doi: 10.1016/j.vaccine.2014.07.031pmc: PMC4148702pubmed: 25045805google scholar: lookup
  39. Huismans H, van der Walt NT, Cloete M, Erasmus BJ. Isolation of a capsid protein of bluetongue virus that induces a protective immune response in sheep. Virology 1987 157:172–179.
    doi: 10.1016/0042-6822(87)90326-6pubmed: 3029956google scholar: lookup
  40. Martinez-Torrecuadrada JL, Iwata H, Venteo A, Casal I, Roy P. Expression and characterization of the two outer capsid proteins of African horsesickness virus: the role of VP2 in virus neutralization. Virology 1994 202:348–359.
    doi: 10.1006/viro.1994.1351pubmed: 8009847google scholar: lookup
  41. Potgieter AC, Cloete M, Pretorius PJ, van Dijk AA. A first full outer capsid protein sequence data-set in the Orbivirus genus (family Reoviridae): cloning, sequencing, expression and analysis of a complete set of full-length outer capsid VP2 genes of the nine African horsesickness virus serotypes. J Gen Virol 2003 84:1317–1326.
    doi: 10.1099/vir.0.18919-0pubmed: 12692299google scholar: lookup
  42. Maan S, Maan NS, Ross-smith N, Batten CA, Shaw AE, Anthony SJ, Samuel AR, Darpel KE, Veronesi E, Oura CA, Singh KP, Nomikou K, Potgieter AC, Attoui H, van Rooij E, van Rijn P, De Clercq K, Vandenbussche F, Zientara S, Breard E, Sailleau C, Beer M, Hoffman B, Mellor PS, Mertens PP. Sequence analysis of bluetongue virus serotype 8 from the Netherlands 2006 and comparison to other European strains. Virology 2008 377:308–318.
    doi: 10.1016/j.virol.2008.04.028pubmed: 18570969google scholar: lookup
  43. Hassan SS, Roy P. Expression and functional characterization of bluetongue virus VP2 protein: role in cell entry. J Virol 1999 73:9832–9842.
    pmc: PMC113032pubmed: 10559295
  44. Zhang X, Boyce M, Bhattacharya B, Schein S, Roy P, Zhou ZH. Bluetongue virus coat protein VP2 contains sialic acid-binding domains, and VP5 resembles enveloped virus fusion proteins. Proc Natl Acad Sci U S A 2010 107:6292–6297.
    doi: 10.1073/pnas.0913403107pmc: PMC2852009pubmed: 20332209google scholar: lookup
  45. Bhattacharya B, Noad RJ, Roy P. Interaction between bluetongue virus outer capsid protein VP2 and vimentin is necessary for virus egress. Virol J 2007 4:7.
    doi: 10.1186/1743-422X-4-7pmc: PMC1783847pubmed: 17224050google scholar: lookup
  46. Celma CC, Roy P. A viral nonstructural protein regulates bluetongue virus trafficking and release. J Virol 2009 83:6806–6816.
    doi: 10.1128/JVI.00263-09pmc: PMC2698550pubmed: 19369335google scholar: lookup
  47. Mertens PP, Burroughs JN, Walton A, Wellby MP, Fu H, O'Hara RS, Brookes SM, Mellor PS. Enhanced infectivity of modified bluetongue virus particles for two insect cell lines and for two Culicoides vector species. Virology 1996 217:582–593.
    doi: 10.1006/viro.1996.0153pubmed: 8610450google scholar: lookup
  48. Manole V, Laurinmaki 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 86:7858–7866.
    doi: 10.1128/JVI.00517-12pmc: PMC3421665pubmed: 22593166google scholar: lookup
  49. Potgieter AC, Page NA, Liebenberg J, Wright IM, Landt O, van Dijk AA. Improved strategies for sequence-independent amplification and sequencing of viral double-stranded RNA genomes. J Gen Virol 2009 90:1423–1432.
    doi: 10.1099/vir.0.009381-0pubmed: 19264638google scholar: lookup
  50. Bentley L, Fehrsen J, Jordaan F, Huismans H, du Plessis DH. Identification of antigenic regions on VP2 of African horsesickness virus serotype 3 by using phage-displayed epitope libraries. J Gen Virol 2000 81:993–1000.
    doi: 10.1099/0022-1317-81-4-993pubmed: 10725425google scholar: lookup
  51. Feenstra F, van Gennip RG, van de Water SG, van Rijn PA. RNA elements in open reading frames of the bluetongue virus genome are essential for virus replication. PLoS One 2014 9:e92377.
    doi: 10.1371/journal.pone.0092377pmc: PMC3962428pubmed: 24658296google scholar: lookup
  52. Shaw AE, Veronesi E, Maurin G, Ftaich N, Guiguen F, Rixon F, Ratinier M, Mertens P, Carpenter S, Palmarini M, Terzian C, Arnaud F. Drosophila melanogaster as a model organism for bluetongue virus replication and tropism. J Virol 2012 86:9015–9024.
    doi: 10.1128/JVI.00131-12pmc: PMC3416142pubmed: 22674991google scholar: lookup
  53. van Rijn PA, van de Water SGP, van Gennip HGP. Bluetongue virus with mutated genome segment 10 to differentiate infected from vaccinated animals: a genetic DIVA approach. Vaccine 2013 31:5005–5008.
    doi: 10.1016/j.vaccine.2013.08.089pubmed: 24021311google scholar: lookup
  54. Sung PY, Roy P. Sequential packaging of RNA genomic segments during the assembly of bluetongue virus. Nucleic Acids Res 2014 42:13824–13838.
    doi: 10.1093/nar/gkᅱpmc: PMC4267631pubmed: 25428366google scholar: lookup
  55. Boyce M, McCrae MA. Rapid mapping of functional cis-acting RNA elements by recovery of virus from a degenerate RNA population: application to genome segment 10 of bluetongue virus. J Gen Virol 2015 96:3072–3082.
    doi: 10.1099/jgv.0.000259pubmed: 26248463google scholar: lookup
  56. Mertens PP, Burroughs JN, Anderson J. Purification and properties of virus particles, infectious subviral particles, and cores of bluetongue virus serotypes 1 and 4. Virology 1987 157:375–386.
    doi: 10.1016/0042-6822(87)90280-7pubmed: 3029978google scholar: lookup
  57. Bhattacharya B, Roy P. Bluetongue virus outer capsid protein VP5 interacts with membrane lipid rafts via a SNARE domain. J Virol 2008 82:10600–10612.
    doi: 10.1128/JVI.01274-08pmc: PMC2573168pubmed: 18753209google scholar: lookup
  58. Celma CC, Roy P. Interaction of calpactin light chain (S100A10/p11) and a viral NS protein is essential for intracellular trafficking of nonenveloped bluetongue virus. J Virol 2011 85:4783–4791.
    doi: 10.1128/JVI.02352-10pmc: PMC3126219pubmed: 21411520google scholar: lookup
  59. French TJ, Inumaru S, Roy P. Expression of two related nonstructural proteins of bluetongue virus (BTV) type 10 in insect cells by a recombinant baculovirus: production of polyclonal ascitic fluid and characterization of the gene product in BTV-infected BHK cells. J Virol 1989 63:3270–3278.
    pmc: PMC250898pubmed: 2545903
  60. Guirakhoo F, Catalan JA, Monath TP. Adaptation of bluetongue virus in mosquito cells results in overexpression of NS3 proteins and release of virus particles. Arch Virol 1995 140:967–974.
    doi: 10.1007/BF01314973pubmed: 7605208google scholar: lookup
  61. Noad R, Roy P. Bluetongue virus replication and assembly. 2009 p 53–76 In Mellor P, Baylis M, Mertens P (ed), Biology of animal infections: bluetongue. Academic Press, Amsterdam, The Netherlands.
  62. Sato M, Tanaka H, Yamada T, Yamamoto N. Persistent infection of BHK21/WI-2 cells with rubella virus and characterization of rubella variants. Arch Virol 1977 54:333–343.
    doi: 10.1007/BF01314778pubmed: 562143google scholar: lookup
  63. Wechsler SJ, McHolland LE, Tabachnick WJ. Cell lines from Culicoides variipennis (Diptera: Ceratopogonidae) support replication of bluetongue virus. J Invertebr Pathol 1989 54:385–393.
    doi: 10.1016/0022-2011(89)90123-7pubmed: 2553822google scholar: lookup
  64. van Gennip RG, Veldman D, van de Water SG, van Rijn PA. Genetic modification of bluetongue virus by uptake of “synthetic” genome segments. Virol J 2010 7:261.
    doi: 10.1186/1743-422X-7-261pmc: PMC2958914pubmed: 20929545google scholar: lookup
  65. van Gennip RG, van de Water SG, Potgieter CA, Wright IM, Veldman D, van Rijn PA. Rescue of recent virulent and avirulent field strains of bluetongue virus by reverse genetics. PLoS One 2012 7:e30540.
    doi: 10.1371/journal.pone.0030540pmc: PMC3281837pubmed: 22363444google scholar: lookup
  66. Wensvoort G, Bloemraad M, Terpstra C. An enzyme immunoassay employing monoclonal antibodies and detecting specifically antibodies to classical swine fever virus. Vet Microbiol 1988 17:129–140.
    doi: 10.1016/0378-1135(88)90004-1pubmed: 2459837google scholar: lookup
  67. Boyce M, Roy P. Recovery of infectious bluetongue virus from RNA. J Virol 2007 81:2179–2186.
    doi: 10.1128/JVI.01819-06pmc: PMC1865916pubmed: 17151117google scholar: lookup

Citations

This article has been cited 5 times.
  1. Zhang M, Wang XF, Guo SF, Wang L, Fu BF, Wang JW, Song YF, Yang XY, Hao SY, Zhang QY, Zhang B, Yang CH. Identification and Genetic Characterization of a Strain of African Horse Sickness Virus Serotype 1 and Its Safety Evaluation in a Mouse Model. Microorganisms 2025 Oct 6;13(10).
    doi: 10.3390/microorganisms13102314pubmed: 41156774google scholar: lookup
  2. Calvo-Pinilla E, Marín-López A, Utrilla-Trigo S, Jiménez-Cabello L, Ortego J. Reverse genetics approaches: a novel strategy for African horse sickness virus vaccine design. Curr Opin Virol 2020 Oct;44:49-56.
    doi: 10.1016/j.coviro.2020.06.003pubmed: 32659516google scholar: lookup
  3. van Gennip RGP, Drolet BS, Rozo Lopez P, Roost AJC, Boonstra J, van Rijn PA. Vector competence is strongly affected by a small deletion or point mutations in bluetongue virus. Parasit Vectors 2019 Oct 11;12(1):470.
    doi: 10.1186/s13071-019-3722-2pubmed: 31604476google scholar: lookup
  4. Aksular M, Calvo-Pinilla E, Marín-López A, Ortego J, Chambers AC, King LA, Castillo-Olivares J. A single dose of African horse sickness virus (AHSV) VP2 based vaccines provides complete clinical protection in a mouse model. Vaccine 2018 Nov 12;36(46):7003-7010.
    doi: 10.1016/j.vaccine.2018.09.065pubmed: 30309744google scholar: lookup
  5. Arias M, de la Torre A, Dixon L, Gallardo C, Jori F, Laddomada A, Martins C, Parkhouse RM, Revilla Y, Rodriguez FAJ. Approaches and Perspectives for Development of African Swine Fever Virus Vaccines. Vaccines (Basel) 2017 Oct 7;5(4).
    doi: 10.3390/vaccines5040035pubmed: 28991171google scholar: lookup
Subscribe to our newsletter
Join 99,727 horse owners like you who receive our email updates on horse health and nutrition.