RECOMBINANT LUMPY SKIN DISEASE VIRUS PROTEINS LSDV095 AND LSDV103 AS POTENTIAL ANTIGENS FOR DIFFERENTIAL DIAGNOSIS OF CAPRIPOXVIRUS INFECTIONS
Main Article Content
Authors
O.V. Chervyakova
Research Institute for Biological Safety Problems, Gvardeiskiy, Korday district, Zhambyl region, 080409, Kazakhstan
R.K. Nissanova
Research Institute for Biological Safety Problems, Gvardeiskiy, Korday district, Zhambyl region, 080409, Kazakhstan
G. Shynybekova
Research Institute for Biological Safety Problems, Gvardeiskiy, Korday district, Zhambyl region, 080409, Kazakhstan
E.T. Tailakova
Research Institute for Biological Safety Problems, Gvardeiskiy, Korday district, Zhambyl region, 080409, Kazakhstan
K.T. Sultankulova
Research Institute for Biological Safety Problems, Gvardeiskiy, Korday district, Zhambyl region, 080409, Kazakhstan
M.B. Orynbayev
Research Institute for Biological Safety Problems, Gvardeiskiy, Korday district, Zhambyl region, 080409, Kazakhstan
Abstract
Capripoxviruses cause infections in ruminants that are a significant threat to animal husbandry in many countries worldwide. Though the problem is sufficiently studied, to date there are no high-producing serological diagnostic tests available that can differentiate between capripoxvirus infections. To develop efficient serological tests, two recombinant lumpy skin disease virus proteins (LSDV095 and LSDV103) were expressed in Escherichia coli and purified using affinity chromatography. It was shown that both proteins were antigenically active against control sera, using western blotting and an indirect ELISA. As antigens, the recombinant proteins LSDV095 and LSDV103 detected antibodies only in the sera of animals infected with virulent capripoxvirus strains. The LSDV103 protein reacted only with the sera of animals infected with the virulent sheep pox and goat pox viruses. The results of this study allow the preliminary conclusion that the recombinant protein LSDV103 can be used for interspecies differentiation of capripoxvirus infections.
Keywords
capripoxvirus, lumpy skin disease virus, sheep pox virus, goat pox virus, recombinant antigens, ELISA, western blot
Article Details
References
Buller R.M., Arif B.M., Black D.N., Dumbell K.R., Esposito J.J., Lefkowitz E.J., McFadden G., Moss B., Mercer A.A., Moyer R.W., Skinner M.A., Tripathy D.N. Family Poxviridae. In Virus taxonomy: Classification and Nomenclature of Viruses, eighth Report of the International Committee on Taxonomy of Viruses, ed. Fauquet, C.M., Mayo, M.A., Maniloff, J., Desselberger, U., Ball, L.A., Elsevier Academic Press, San Diego, 2005, pp.117-133.
Beard P. Sheep pox and goat pox. OIE, Manual of Diagnostic Tests and Vaccines for Terrestrial Animals (Mammals, Birds and Bees). 2017. URL (accessed 3 October 2018).
Beard P. Lumpy skin disease. OIE, Manual of Diagnostic Tests and Vaccines for Terrestrial Animals (Mammals, Birds and Bees). 2017. URL (accessed 3 October 2018).
Lamien C.E., Lelenta M., Goger W., Silber R., Tuppurainen E., Matijevic M., Luckins A.G., Diallo A. Real time PCR method for simultaneous detection, quantitation and differentiation of capripoxviruses. J. Virol. Methods, 2011, vol. 171, pp. 134-140. Crossref.
Stubbs S., Oura C.A., Henstocka M., Bowden T.R., King D.P., Tuppurainen E.S. Validation of a high-throughput real-time polymerase chain reaction assay for the detection of capripoxviral DNA. J. Virol. Methods, 2012, vol. 179, pp. 419-422. Crossref.
Bhanot V., Balamurugan V., Bhanuprakash V., Venkatesan G., Sen A., Yadav V., Yogisharadhya R., Singh R.K. Expression of P32 protein of goatpox virus in Pichia pastoris and its potential use as a diagnostic antigen in ELISA. J. Virol. Methods, 2009, vol. 162, no. 1-2, pp. 251-257. Crossref.
Bowden T. R., Coupar B. E., Babiuk S. L., White J. R., Boyd V., Duch C. J., Boyle D.B. Detection of antibodies specific for sheeppox and goatpox viruses using recombinant capripoxvirus antigens in an indirect enzyme-linked immunosorbent assay. J. Virol. Methods, 2009, vol. 161, no. 1, pp. 19-29. Crossref.
Tailakova E.T., Chervyakova O.V. Bacterial expression of the sheeppox virus genes encoding antigenic proteins SPPV095 and SPPV141 for development of a new generation of specific prophylaxis means. Biotechnology. Theory and Practice, 2016, vol. 2, pp. 81-87. Crossref.
Carn V.M., Kitching R.P., Hammond J.M., Chand P. Use of a recombinant antigen in an indirect ELISA for detection of bovine antibody to Capripoxvirus. J. Virol. Methods, 1995, vol. 49, no. 3, pp. 285–294. Crossref.
Babiuk S., Wallace D. B., Smith S. J., Bowden T. R., Dalman B., Parkyn G., Copps J., Boyle D.B. Detection of antibodies against capripoxviruses using an inactivated sheeppox virus ELISA. Transboundary and Emerging Diseases, 2009, vol. 56, pp. 132-141. Crossref.
Orlova Ye.S., Shcherbakov A.V., Yakovleva A.S., Basova D.K., Diyev V.I., Kanshina A.V. P17, P18 and P32 recombinant proteins of sheep pox virus as potential antigens for enzyme-linked immunosorbent assay. Annals of the Federal Center for Animal Health Care, 2006, vol. 4, pp, 30–35. URL