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

Enhanced Surface Accessibility of SARS-CoV-2 Omicron Spike Protein Due to an Altered Glycosylation Profile.

ACS infectious diseases - 14 Jun 2024

Wang Dongxia, Zhang Zijian, Baudys Jakub, Haynes Christopher, Osman Sarah H, Zhou Bin, Barr John R, Gumbart James C

Abstract excerpt

SARS-CoV-2 spike (S) proteins undergo extensive glycosylation, aiding in proper folding, enhancing stability, and evading host immune surveillance. In this study, we used mass spectrometric analysis to elucidate the N-glycosylation characteristics and disulfide bonding of recombinant spike proteins derived from the SARS-CoV-2 Omicron variant (B.1.1.529) in comparison with the D614G spike variant. Furthermore, we...

Read the complete abstract on PubMed

Topics

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

Share to COVID-19
Share to Glycosylation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Molecular Dynamics Simulation

Share to Mutation

Share to Polysaccharides

Share to Protein Conformation

Share to SARS-CoV-2

Share to Spike Glycoprotein, Coronavirus

Source

Open in PubMed Open full text

Identifiers

PMID: 38728322
DOI: 10.1021/acsinfecdis.4c00015
PMCID: PMC11184558

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 3 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Enhanced Surface Accessibility of SARS-CoV-2 Omicron Spike Protein Due to an Altered Glycosylation Profile.PMID 38728322Read ↗

Structural diversity of the SARS-CoV-2 Omicron spike.Semantic proximity Read ↗

Site specific N- and O-glycosylation mapping of the spike proteins of SARS-CoV-2 variants of concernSemantic proximity Read ↗

Site Specific N- and O-glycosylation mapping of the Spike Proteins of SARS-CoV-2 Variants of ConcernSemantic proximity Read ↗

Variations in O-Glycosylation Patterns Influence Viral Pathogenicity, Infectivity, and Transmissibility in SARS-CoV-2 VariantsSemantic proximity Read ↗

Insights into the structural peculiarities of the N-terminal and receptor binding domains of the spike protein from the SARS-CoV-2 Omicron variant.Semantic proximity Read ↗

Distinct shifts in site-specific glycosylation pattern of SARS-CoV-2 spike proteins associated with arising mutations in the D614G and Alpha variants.Semantic proximity Read ↗

Structural remodeling of SARS-CoV-2 spike protein glycans reveals the regulatory roles in receptor-binding affinitySemantic proximity Read ↗

Structural dynamics in the evolution of SARS-CoV-2 spike glycoprotein.Semantic proximity Read ↗

N-glycosylation profiles of the SARS-CoV-2 spike D614G mutant and its ancestral protein characterized by advanced mass spectrometrySemantic proximity Read ↗

N-glycosylation profiles of the SARS-CoV-2 spike D614G mutant and its ancestral protein characterized by advanced mass spectrometry.Semantic proximity Read ↗

Evolving spike-protein <i>N</i> -glycosylation in SARS-CoV-2 variantsSemantic proximity Read ↗

Virus-Receptor Interactions of Glycosylated SARS-CoV-2 Spike and Human Ace2 ReceptorSemantic proximity Read ↗

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