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

Removal of a N-linked glycosylation site of classical swine fever virus strain Brescia Erns glycoprotein affects virulence in swine.

Virology - 5 Jan 2008

Sainz I Fernandez, Holinka L G, Lu Z, Risatti G R, Borca M V

Abstract excerpt

E(rns) glycoprotein, along with E(1) and E(2), is one of the three envelope glycoproteins of classical swine fever virus (CSFV). E(rns) is a heavily glycosylated protein involved in several functions, including virus attachment and entry to target cells, production of neutralizing antibodies, and virulence. The role of added glycans to CSFV strain Brescia E(rns) on virus virulence was assessed in swine. A panel...

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

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Glycosylation

Share to Macrophages

Share to Polysaccharides

Share to Vaccines, Attenuated

Share to Viral Envelope Proteins

Share to Viral Vaccines

Source

Identifiers

PMID: 17904607
DOI: 10.1016/j.virol.2007.08.028

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Removal of a N-linked glycosylation site of classical swine fever virus strain Brescia Erns glycoprotein affects virulence in swine.PMID 17904607Read ↗

N-linked glycosylation status of classical swine fever virus strain Brescia E2 glycoprotein influences virulence in swine.Semantic proximity Read ↗

The Unique Glycosylation at Position 986 on the E2 Glycoprotein of Classical Swine Fever Virus Is Responsible for Viral Attenuation and Protection against Lethal Challenge.Semantic proximity Read ↗

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

Recoding structural glycoprotein E2 in classical swine fever virus (CSFV) produces complete virus attenuation in swine and protects infected animals against disease.Semantic proximity Read ↗

N-glycosylation of the PEDV spike protein modulates viral replication and pathogenicitySemantic proximity Read ↗

The N545S and K717N substitution at the N-glycosylation sites of the S2 subunit of avian infectious bronchitis virus can significantly enhance viral pathogenicitySemantic proximity Read ↗

Modification of N-glycosylation site in the spike protein enhances the neutralizing antibody response against PEDV.Semantic proximity Read ↗

Baculovirus expression and antigenic characterization of classical swine fever virus E2 proteins.Semantic proximity Read ↗

The glycosylation variant at residue 381 of the spike protein contributes to virulence shifts in porcine epidemic diarrhea virus during both natural field transmission and laboratory cell passaging with poor cross-protection.Semantic proximity Read ↗

Different evolutionary patterns of classical swine fever virus envelope proteins.Semantic proximity Read ↗

Molecular evolution and antigenic mapping of classical swine fever virus: a comprehensive analysis of E2 genomic variability and selection dynamics.Semantic proximity Read ↗

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