RNase of classical swine fever virus: biochemical characterization and inhibition by virus-neutralizing monoclonal antibodies.
AUTOR(ES)
Windisch, J M
RESUMO
The 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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=189824Documentos Relacionados
- Chimeric gag-V3 virus-like particles of human immunodeficiency virus induce virus-neutralizing antibodies.
- Interference of coronavirus infection by expression of immunoglobulin G (IgG) or IgA virus-neutralizing antibodies.
- Automated Microtransfer Technique for the Assay of Poliovirus- and Mumps Virus-Neutralizing Antibodies
- Estimation of virus-neutralizing antibody in microplates
- Enhanced Virus Clearance by Early Inducible Lymphocytic Choriomeningitis Virus-Neutralizing Antibodies in Immunoglobulin-Transgenic Mice
