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Science 27 August 1993:
Vol. 261. no. 5125, pp. 1169 - 1171
DOI: 10.1126/science.8356450
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Articles

Science, Vol 261, Issue 5125, 1169-1171
Copyright © 1993 by American Association for the Advancement of Science

articles

Identification of a structural glycoprotein of an RNA virus as a ribonuclease

R Schneider, G Unger, R Stark, E Schneider-Scherzer, and HJ Thiel

Department of Biochemistry, Faculty of Natural Sciences, University of Innsbruck, Austria.

One of the three structural glycoproteins of classical swine fever virus (CSFV) is E0, a disulfide-bonded homodimer that induces virus-neutralizing antibodies and occurs in a virion-bound as well as a secreted form. E0 was shown to be similar to a family of fungal and plant ribonucleases. Purified E0 from CSFV-infected cells was a potent ribonuclease specific for uridine and inhibitable by zinc ions.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Mutation of Cysteine 171 of Pestivirus Erns RNase Prevents Homodimer Formation and Leads to Attenuation of Classical Swine Fever Virus.
B. A. Tews, E.-M. Schurmann, and G. Meyers (2009)
J. Virol. 83, 4823-4834
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A type II secreted RNase of Legionella pneumophila facilitates optimal intracellular infection of Hartmannella vermiformis.
O. Rossier, J. Dao, and N. P. Cianciotto (2009)
Microbiology 155, 882-890
   Abstract »    Full Text »    PDF »
RNase-dependent inhibition of extracellular, but not intracellular, dsRNA-induced interferon synthesis by Erns of pestiviruses.
I. Magkouras, P. Matzener, T. Rumenapf, E. Peterhans, and M. Schweizer (2008)
J. Gen. Virol. 89, 2501-2506
   Abstract »    Full Text »    PDF »
The Pestivirus Glycoprotein Erns Is Anchored in Plane in the Membrane via an Amphipathic Helix.
B. A. Tews and G. Meyers (2007)
J. Biol. Chem. 282, 32730-32741
   Abstract »    Full Text »    PDF »
Bovine Viral Diarrhea Virus: Prevention of Persistent Fetal Infection by a Combination of Two Mutations Affecting Erns RNase and Npro Protease.
G. Meyers, A. Ege, C. Fetzer, M. von Freyburg, K. Elbers, V. Carr, H. Prentice, B. Charleston, and E.-M. Schurmann (2007)
J. Virol. 81, 3327-3338
   Abstract »    Full Text »    PDF »
The Carboxy-Terminal Sequence of the Pestivirus Glycoprotein Erns Represents an Unusual Type of Membrane Anchor.
C. Fetzer, B. A. Tews, and G. Meyers (2005)
J. Virol. 79, 11901-11913
   Abstract »    Full Text »    PDF »
Dual Mechanisms of Pestiviral Superinfection Exclusion at Entry and RNA Replication.
Y.-M. Lee, D. M. Tscherne, S.-I. Yun, I. Frolov, and C. M. Rice (2005)
J. Virol. 79, 3231-3242
   Abstract »    Full Text »    PDF »
Antibody Responses of Pigs to Defined Erns Fragments after Infection with Classical Swine Fever Virus.
M. Lin, E. Trottier, and J. Pasick (2005)
Clin. Vaccine Immunol. 12, 180-186
   Abstract »    Full Text »    PDF »
Identification of Antigenic Regions of the Erns Protein for Pig Antibodies Elicited during Classical Swine Fever Virus Infection.
M. Lin, E. Trottier, J. Pasick, and M. Sabara (2004)
J. Biochem. 136, 795-804
   Abstract »    Full Text »    PDF »
Determinants of Virulence of Classical Swine Fever Virus Strain Brescia.
H. G. P. van Gennip, A. C. Vlot, M. M. Hulst, A. J. de Smit, and R. J. M. Moormann (2004)
J. Virol. 78, 8812-8823
   Abstract »    Full Text »    PDF »
Comparison of the effects of RNase-negative and wild-type classical swine fever virus on peripheral blood cells of infected pigs.
M. von Freyburg, A. Ege, A. Saalmuller, and G. Meyers (2004)
J. Gen. Virol. 85, 1899-1908
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Classical Swine Fever Virus Glycoprotein Erns Is an Endoribonuclease with an Unusual Base Specificity.
Y. Hausmann, G. Roman-Sosa, H.-J. Thiel, and T. Rumenapf (2004)
J. Virol. 78, 5507-5512
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Role for Bovine Viral Diarrhea Virus Erns Glycoprotein in the Control of Activation of Beta Interferon by Double-Stranded RNA.
M. Iqbal, E. Poole, S. Goodbourn, and J. W. McCauley (2004)
J. Virol. 78, 136-145
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A Structural Model of Pestivirus Erns Based on Disulfide Bond Connectivity and Homology Modeling Reveals an Extremely Rare Vicinal Disulfide.
J. P. M. Langedijk, P. A. van Veelen, W. M. M. Schaaper, A. H. de Ru, R. H. Meloen, and M. M. Hulst (2002)
J. Virol. 76, 10383-10392
   Abstract »    Full Text »    PDF »
Identification of the glycosaminoglycan-binding site on the glycoprotein Erns of bovine viral diarrhoea virus by site-directed mutagenesis.
M. Iqbal and J. W. McCauley (2002)
J. Gen. Virol. 83, 2153-2159
   Abstract »    Full Text »    PDF »
Recovery of Virulent and RNase-Negative Attenuated Type 2 Bovine Viral Diarrhea Viruses from Infectious cDNA Clones.
C. Meyer, M. von Freyburg, K. Elbers, and G. Meyers (2002)
J. Virol. 76, 8494-8503
   Abstract »    Full Text »    PDF »
A time to kill: viral manipulation of the cell death program.
S. Hay and G. Kannourakis (2002)
J. Gen. Virol. 83, 1547-1564
   Abstract »    Full Text »    PDF »
Translocation Activity of C-terminal Domain of Pestivirus Erns and Ribotoxin L3 Loop.
J. P. M. Langedijk (2002)
J. Biol. Chem. 277, 5308-5314
   Abstract »    Full Text »    PDF »
Isolation and Characterization of Noncytopathic Pestivirus Mutants Reveals a Role for Nonstructural Protein NS4B in Viral Cytopathogenicity.
L. Qu, L. K. McMullan, and C. M. Rice (2001)
J. Virol. 75, 10651-10662
   Abstract »    Full Text »    PDF »
Interaction of Classical Swine Fever Virus with Membrane-Associated Heparan Sulfate: Role for Virus Replication In Vivo and Virulence.
M. M. Hulst, H. G. P. van Gennip, A. C. Vlot, E. Schooten, A. J. de Smit, and R. J. M. Moormann (2001)
J. Virol. 75, 9585-9595
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A Cellular J-Domain Protein Modulates Polyprotein Processing and Cytopathogenicity of a Pestivirus.
G. Rinck, C. Birghan, T. Harada, G. Meyers, H.-J. Thiel, and N. Tautz (2001)
J. Virol. 75, 9470-9482
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Characterization of Rny1, the Saccharomyces cerevisiae member of the T2 RNase family of RNases: Unexpected functions for ancient enzymes?.
G. C. MacIntosh, P. A. Bariola, E. Newbigin, and P. J. Green (2001)
PNAS 98, 1018-1023
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E2-p7 Region of the Bovine Viral Diarrhea Virus Polyprotein: Processing and Functional Studies.
T. Harada, N. Tautz, and H.-J. Thiel (2000)
J. Virol. 74, 9498-9506
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Passage of Classical Swine Fever Virus in Cultured Swine Kidney Cells Selects Virus Variants That Bind to Heparan Sulfate due to a Single Amino Acid Change in Envelope Protein Erns.
M. M. Hulst, H. G. P. van Gennip, and R. J. M. Moormann (2000)
J. Virol. 74, 9553-9561
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Classical Swine Fever Virus Erns Deletion Mutants: trans-Complementation and Potential Use as Nontransmissible, Modified, Live-Attenuated Marker Vaccines.
M. N. Widjojoatmodjo, H. G. P. van Gennip, A. Bouma, P. A. van Rijn, and R. J. M. Moormann (2000)
J. Virol. 74, 2973-2980
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Interactions of bovine viral diarrhoea virus glycoprotein Erns with cell surface glycosaminoglycans.
M. Iqbal, H. Flick-Smith, and J. W. McCauley (2000)
J. Gen. Virol. 81, 451-459
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Mutational Analysis of Bovine Viral Diarrhea Virus RNA-Dependent RNA Polymerase.
V. C. H. Lai, C. C. Kao, E. Ferrari, J. Park, A. S. Uss, J. Wright-Minogue, Z. Hong, and J. Y. N. Lau (1999)
J. Virol. 73, 10129-10136
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Mutations Abrogating the RNase Activity in Glycoprotein Erns of the Pestivirus Classical Swine Fever Virus Lead to Virus Attenuation.
G. Meyers, A. Saalmüller, and M. Büttner (1999)
J. Virol. 73, 10224-10235
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Establishment and Characterization of Cytopathogenic and Noncytopathogenic Pestivirus Replicons.
N. Tautz, T. Harada, A. Kaiser, G. Rinck, S.-E. Behrens, and H.-J. Thiel (1999)
J. Virol. 73, 9422-9432
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Purification and Characterization of a Polysome-associated Endoribonuclease That Degrades c-myc mRNA in Vitro.
C. H. Lee, P. Leeds, and J. Ross (1998)
J. Biol. Chem. 273, 25261-25271
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Characterization of an Autonomous Subgenomic Pestivirus RNA Replicon.
S.-E. Behrens, C. W. Grassmann, H.-J. Thiel, G. Meyers, and N. Tautz (1998)
J. Virol. 72, 2364-2372
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Inactivation of the RNase Activity of Glycoprotein Erns of Classical Swine Fever Virus Results in a Cytopathogenic Virus.
M. M. Hulst, F. E. Panoto, A. Hoekman, H. G. P. van Gennip, and R. J. M. Moormann (1998)
J. Virol. 72, 151-157
   Abstract »    Full Text »    PDF »
Nerve Growth Factor Binding Site on TrkA Mapped to a Single 24-Amino Acid Leucine-rich Motif.
Jör. M. Windisch, R. Marksteiner, and R. Schneider (1995)
J. Biol. Chem. 270, 28133-28138
   Abstract »    Full Text »    PDF »


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