Du Plessis, M.Cloete, M.Aitchison, HenryVan Dijk, A.A.Verwoerd, Daniel Wynand2012-12-122012-12-1220121998Du Plessis, M, Cloete, M, Aitchison, H & Van Dijk, AA 1998, 'Protein aggregation complicates the development of baculovirus-expressed African horsesickness virus serotype 5 VP2 subunit vaccines’. Onderstepoort Journal of Veterinary Research, vol. 65, no. 4, pp. 321-3290330-2465http://hdl.handle.net/2263/20714The articles have been scanned in colour with a HP Scanjet 5590; 600dpi. Adobe Acrobat X Pro was used to OCR the text and also for the merging and conversion to the final presentation PDF-format.This paper describes the expression of a cloned African horsesickness virus (AHSV) serotype 5 VP2- gene by a baculovirus recombinant that was generated by the BAC-TO-BAC™ system. Immunization of horses with crude cell lysates containing recombinant baculovirus-expressed AHSV5 VP2 did induce neutralizing antibodies, but afforded only partial protection against virulent virus challenge. Further analysis of partially protective crude cell lysates revealed that baculovirus-expressed AHSV5 VP2 was predominantly present in the form of insoluble aggregates. Only approximately 10% of VP2 was present in a soluble form. Immunization of guinea-pigs with aggregated and soluble forms of AHSV5 VP2 established that only soluble VP2 was capable of inducing neutralizing antibodies. This finding adds a new dimension to the development of AHSV VP2s as subunit vaccines. Further investigation is needed to limit formation of insoluble aggregates and optimize conditions for producing VP2 in a form capable of inducing protective immunity.en© ARC-Onderstepoort (original). © University of Pretoria. Dept of Library Services (digital).Veterinary medicineAfrican horsesickness virus (AHSV)BaculovirusSerotype 5 VP2VaccinesVeterinary medicine -- South AfricaArticle