Study On Diagnoses And Immunization Of Rift Valley Fever

Expression of RVFV glycoproteins was investigated using baculovirus vectors.The results obtained for the recombinant baculoviruses containing the cDNA representing M residues(G(N+C)302-3884,GN418-1943,GC2043-3613) were compared to those of a cDNA constructions, rBacmid-G(N+C), rBacmid-GN, and rBacmid-GC. Western-bloting analyses and ELISA of the products of the rBac-G(N+C), rBac-GN, and rBac-GC recombinants did not identify any significant difference among of them in terms of the level of RVFV glycoprotein expression, except that the G(N+C) protein product was fewer respectively. The M segment could be completely and faithfully expressed in the vaccinia virus system by recombinant vaccinia virus rVV-G(N+C) and rVV-GN, the gene products apparently being correctly processed and modified,in the absence of the L and S genomic segments and their model system to further explore RVFV expression and gene product function is indicated. The recombinants rVV-G(N+C) and rVV-GN expression products were showed that have immune responses by Western-bloting analyses and ELISA. The availability of such a faithful model system offers particular advantages for the study of RVFV in that it reduces the need for direct manipulation of an exotic pathogen. Constructing DNA immune plasmids pCAGG-G(N+C), pCAGG-GN, and pCAGG-GC to immunize BALB/c mouse,have been shown that can induce neutralization antibody by neutralization test of RVFV envelope protein pseudotyping VSV, VSV?G*GFP-RVFV-G.