Development of multiple ELISAs for the detection of antibodies against classical swine fever virus in pig sera.

The major immunogenic proteins (E(rns), E2 and NS3) of classical swine fever virus (CSFV) (Shimen strain) were expressed in E. coli and purified by affinity chromatography. The recombinant antigens were applied to develop multiple enzyme-linked immunosorbent assays (ELISAs) for the detection of specific antibodies in pig sera.

A novel role of classical swine fever virus E(rns) glycoprotein in counteracting the newcastle disease virus (NDV)-mediated IFN-beta Induction.

E(rns) is an envelope glycoprotein of classical swine fever virus (CSFV) and has an unusual feature of RNase activity. In the present study, we demonstrate that E(rns) counteracts Newcastle disease virus (NDV)-mediated induction of IFN-beta. For this purpose, E(rns) fused to the enhanced green fluorescent protein (EGFP) was transiently expressed in porcine kidney 15 (PK15) cells.

Expression and functional characterization of classical swine fever virus E(rns) protein.

E(rns) is an envelope glycoprotein of classical swine fever virus (CSFV) with unusual RNase activity. Recently, E(rns) was found to have a new function of counteracting the beta-interferon (IFN-beta) induction pathway. In this study, wildtype ErnsSM and two mutated E(rns) proteins ErnsH297k and ErnsH346k were expressed in insect cells and purified for RNase activity and function analysis.