RNase of classical swine fever virus: biochemical characterization and inhibition by virus-neutralizing monoclonal antibodies
1996; American Society for Microbiology; Volume: 70; Issue: 1 Linguagem: Inglês
10.1128/jvi.70.1.352-358.1996
ISSN1098-5514
AutoresJ. Windisch, Rainer Schneider, R Stark, E. Weiland, Gregor Meyers, Heinz‐Jürgen Thiel,
Tópico(s)Plant Virus Research Studies
ResumoThe structural glycoprotein E0 of classical swine fever virus (CSFV) possesses an intrinsic RNase activity. Here we present the first comprehensive biochemical characterization of E0, using a recombinant glycoprotein expressed in insect cells. We were able to show that the presence of neither carbohydrate moieties nor disulfide bonds is a prerequisite for RNase activity. In addition, virus-neutralizing and nonneutralizing anti-E0 monoclonal antibodies were tested for their ability to influence RNase activity. In these experiments, the antibodies which effectively blocked the infection of STE cells also exerted a high degree of E0 RNase inhibition. This correlation suggests that the RNase activity of CSFV E0 plays a role in the viral life cycle.
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