Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

The Molecular Basis for Erns Dimerization in Classical Swine Fever Virus.

Viruses - 2 Nov 2021

Mischler Manjula, Meyers Gregor

Abstract excerpt

The pestivirus classical swine fever virus (CSFV) represents one of the most important pathogens of swine. Its virulence is dependent on the RNase activity of the essential structural glycoprotein Erns that uses an amphipathic helix as a membrane anchor and forms homodimers via disulfide bonds employing cysteine 171. Dimerization is not necessary for CSFV viability but for its virulence. Mutant Erns proteins...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Classical Swine Fever
Share to Classical Swine Fever Virus
Share to Cysteine

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Dimerization

Share to RNA Viruses

Share to Viral Envelope Proteins

Share to Virulence Factors

Share to Virus Replication

Source

Open in PubMed Open full text

Identifiers

PMID: 34835010
DOI: 10.3390/v13112204
PMCID: PMC8625691

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The Molecular Basis for Erns Dimerization in Classical Swine Fever Virus.PMID 34835010Read ↗

Restoration of glycoprotein Erns dimerization via pseudoreversion partially restores virulence of classical swine fever virus.Semantic proximity Read ↗

Mutation of cysteine 171 of pestivirus E rns RNase prevents homodimer formation and leads to attenuation of classical swine fever virus.Semantic proximity Read ↗

Alteration of a Second Putative Fusion Peptide of Structural Glycoprotein E2 of Classical Swine Fever Virus Alters Virus Replication and Virulence in Swine.Semantic proximity Read ↗

Evaluation of the Function of the ASFV KP177R Gene, Encoding for Structural Protein p22, in the Process of Virus Replication and in Swine Virulence.Semantic proximity Read ↗

Disulfide linkages mediating nucleocapsid protein dimerization are not required for porcine arterivirus infectivity.Semantic proximity Read ↗

Mutations in the carboxyl terminal region of E2 glycoprotein of classical swine fever virus are responsible for viral attenuation in swine.Semantic proximity Read ↗

Crystal Structure of the Dimerized N Terminus of Porcine Circovirus Type 2 Replicase Protein Reveals a Novel Antiviral Interface.Semantic proximity Read ↗

A DNA-launched reverse genetics system for porcine reproductive and respiratory syndrome virus reveals that homodimerization of the nucleocapsid protein is essential for virus infectivity.Semantic proximity Read ↗

Characterization of essential domains and plasticity of the classical Swine Fever virus Core protein.Semantic proximity Read ↗

Rescue of the highly virulent classical swine fever virus strain "Koslov" from cloned cDNA and first insights into genome variations relevant for virulence.Semantic proximity Read ↗

The E2 Glycoprotein of Classical Swine Fever Virus Is a Virulence Determinant in SwineSemantic proximity Read ↗

Classical Swine Fever Virus E <sup>rns</sup> Deletion Mutants: <i>trans</i> -Complementation and Potential Use as Nontransmissible, Modified, Live-Attenuated Marker VaccinesSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.