RNase of classical swine fever virus: biochemical characterization and inhibition by virus-neutralizing monoclonal antibodies.
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.
Institute of Biochemistry, University of Innsbruck, Austria.
J M
JM
Windisch
R
R
Schneider
R
R
Stark
E
E
Weiland
G
G
Meyers
H J
HJ
Thiel
D000818:Animals; D000911:Antibodies, Monoclonal / Q000276:immunology; D002413:Cations, Divalent / Q000494:pharmacology; D002614:Chelating Agents / Q000494:pharmacology; D006692:Classical Swine Fever Virus / Q000201:enzymology* / Q000276:immunology; D006031:Glycosylation; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D009500:Neutralization Tests; D011993:Recombinant Fusion Proteins / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000378:metabolism; D012260:Ribonucleases / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000276:immunology; D012965:Sodium Chloride / Q000494:pharmacology; D013379:Substrate Specificity; D013439:Sulfhydryl Reagents / Q000494:pharmacology; D013696:Temperature
D000911:Antibodies, Monoclonal; D002413:Cations, Divalent; D002614:Chelating Agents; D011993:Recombinant Fusion Proteins; D013439:Sulfhydryl Reagents; D012965:Sodium Chloride; D012260:Ribonucleases