PMID: 9420210Jan 7, 1998Paper

Inactivation of the RNase activity of glycoprotein E(rns) of classical swine fever virus results in a cytopathogenic virus

Journal of Virology
M M HulstR J Moormann

Abstract

Envelope glycoprotein E(rns) of classical swine fever virus (CSFV) has been shown to contain RNase activity and is involved in virus infection. Two short regions of amino acids in the sequence of E(rns) are responsible for RNase activity. In both regions, histidine residues appear to be essential for catalysis. They were replaced by lysine residues to inactivate the RNase activity. The mutated sequence of E(rns) was inserted into the p10 locus of a baculovirus vector and expressed in insect cells. Compared to intact E(rns), the mutated proteins had lost their RNase activity. The mutated proteins reacted with E(rns)-specific neutralizing monoclonal and polyclonal antibodies and were still able to inhibit infection of swine kidney cells (SK6) with CSFV, but at a concentration higher than that measured for intact E(rns). This result indicated that the conformation of the mutated proteins was not severely affected by the inactivation. To study the effect of these mutations on virus infection and replication, a CSFV mutant with an inactivated E(rns) (FLc13) was generated with an infectious DNA copy of CSFV strain C. The mutant virus showed the same growth kinetics as the parent virus in cell culture. However, in contrast to the pare...Continue Reading

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Citations

Jan 12, 2005·Clinical and Diagnostic Laboratory Immunology·Min LinJohn Pasick
Jul 29, 2004·Journal of Virology·H G P Van GennipR J M Moormann
Nov 25, 2000·DNA Sequence : the Journal of DNA Sequencing and Mapping·D Pietrowski, M Förster
Nov 5, 1999·Annual Review of Microbiology·A RoulstonP E Branton
Jul 26, 2012·PloS One·Natalie Luhtala, Roy Parker
Jul 21, 2000·DNA Sequence : the Journal of DNA Sequencing and Mapping·D Pietrowski, M Förster

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