Recombinant Jembrana disease virus proteins as antigens for the detection of antibody to bovine lentiviruses
Burkala, E.J., Narayani, I., Hartaningsih, N., Kertayadnya, G., Berryman, D.I. and Wilcox, G.E. (1998) Recombinant Jembrana disease virus proteins as antigens for the detection of antibody to bovine lentiviruses. Journal of Virological Methods, 74 (1). pp. 39-46.
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Abstract
Jembrana disease virus (JDV) is a recently identified bovine lentivirus causing an acute severe disease syndrome in banteng cattle (Bos javanicus) and a milder disease syndrome in Bos taurus cattle in Indonesia. The virus is closely related genetically to the previously identified bovine lentivirus, bovine immunodeficiency virus (BIV). Recombinant clones were produced which contained the capsid (CA) and transmembrane (TM) subunits of the respective gag and env open reading frames of JDV. The proteins were expressed as fusions to the glutathione-s-transferase (GST) enzyme in Escherichia coli and purification was achieved using affinity chromatography via immobilized reduced glutathione. The soluble recombinant CA and TM antigens of JDV were reacted in western immunoblots with both serum antibodies from JDV-infected Bos javanicus cattle and Bos taurus cattle immunized with BIV. The recombinant CA protein of JDV reacted equally well with both the JDV and BIV antisera. The recombinant TM protein of JDV also reacted with antibody from the JDV infected cattle and with the BIV antisera. The results indicated conservation of immunogenic epitopes of the CA and TM proteins of the two viruses. The production of the recombinant proteins should enable the development of rapid and sensitive serological tests for JDV and BIV, and tools for further study of the immune response to JDV and the differential epidemiology of JDV infections in cattle.
Item Type: | Journal Article |
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Murdoch Affiliation(s): | School of Veterinary and Biomedical Sciences |
Publisher: | Elsevier BV |
Copyright: | © 1998 Elsevier Science B.V. |
URI: | http://researchrepository.murdoch.edu.au/id/eprint/17858 |
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