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Journal of Virology, May 2004, p. 5507-5512, Vol. 78, No. 10
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.10.5507-5512.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Classical Swine Fever Virus Glycoprotein E^rns Is an Endoribonuclease with an Unusual Base Specificity

Institut für Virologie, Justus-Liebig-Universität, D-35392 Giessen, Germany

Received 2 October 2003/ Accepted 22 January 2004

The glycoprotein E^rns of pestiviruses is a virion-associated and -secreted RNase that is involved in virulence. The requirements at the cleavage site in heteropolymeric RNA substrates were studied for E^rns. Limited digestion of heteropolymeric RNA substrates indicated a cleavage 5' of uridine residues irrespective of the preceding nucleotide (Np/U). To further study specificity radiolabeled RNA, molecules of 45 to 56 nucleotides in length were synthesized that contained no or a single Np/U cleavage site. Cleavage was only observed in substrates containing an ApU, CpU, GpU, or UpU dinucleotide and occurred in two steps, an initial NpU-specific and a consecutive unspecific degradation. The NpU-specific cleavage was resistant to 7 M urea while the second-order cleavage was sensitive to denaturation. Kinetic analyses revealed that E^rns is a highly active endoribonuclease (k_cat/K_m = 2 x 10⁶ to 10 x 10⁶ M^–1 s^–1) with a strong affinity to NpU containing single-stranded RNA substrates (K_m = 85 to 260 nM).

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