ArticleJournal of virology2009
Mutation of cysteine 171 of pestivirus E rns RNase prevents homodimer formation and leads to attenuation of classical swine fever virus.
Article in Journal of virology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 51 citations in OpenAlex.
- Review
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- Host cell factors involved in classical swine fever virus entry.Veterinary research · 2023Review
- A dsRNA-binding mutant reveals only a minor role of exonuclease activity in interferon antagonism by the arenavirus nucleoprotein.PLoS pathogens · 2023Article
- Fifty Shades of EViruses · 2022Article
- The Molecular Basis for EViruses · 2021Article
- Characterization of Membrane Topology and Retention Signal of Pestiviral Glycoprotein E1.Journal of virology · 2021Article
- Interaction of Pestiviral E1 and E2 Sequences in Dimer Formation and Intracellular Retention.International journal of molecular sciences · 2021Article
- The EViruses · 2021Article
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- Downstream Sequences Control the Processing of the Pestivirus EJournal of virology · 2020Article
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- HCV Pit Stop at the Lipid Droplet: Refuel Lipids and Put on a Lipoprotein Coat before Exit.Cells · 2019Review
- Homodimerisation-independent cleavage of dsRNA by a pestiviral nicking endoribonuclease.Scientific reports · 2018Article
- NVirus genes · 2018Article
- Classical Swine Fever-An Updated Review.Viruses · 2017Review
- Pig BVDV-2 non-structural protein (NVirus genes · 2017Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Pestiviruses represent important pathogens of farm animals that have evolved unique strategies and functions to stay within their host populations. E(rns), a structural glycoprotein of pestiviruses, exhibits RNase activity and represents a virulence factor of the viruses. E(rns) forms disulfide linked homodimers that are found in virions and virus-infected cells. Mutation or deletion of cysteine 171, the residue engaged in intermolecular disulfide bond formation, results in loss of dimerization as tested in coprecipitation and native protein gel electrophoresis analyses. Nevertheless, stable virus mutants with changes affecting cysteine codon 171 could be recovered in tissue culture. These mutants grew almost as well as the parental viruses and exhibited an RNase-positive phenotype. E(rns) dimerization-negative mutants of classical swine fever virus were found to be attenuated in pigs even though the virus clearly replicated and induced a significant neutralizing antibody response in the animals.
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Registered trials
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