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

Glycans of SARS-CoV-2 Spike Protein in Virus Infection and Antibody Production

13 Apr 2021

Abstract excerpt

Viral protein glycosylation represents a successful strategy employed by the parasite to take advantage of host-cell machinery for modification of its own proteins. The resulting glycans have unneglectable roles in viral infection and immune response. The spike (S) protein of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), which presents on the surface of matured virion and mediates viral entry into...

Read the complete abstract on PubMed

Topics

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

Share to Immunotherapy and Immune Responses
Share to SARS-CoV-2 and COVID-19 Research
Share to vaccines and immunoinformatics approaches

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 33928117
DOI: 10.3389/fmolb.2021.629873

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Glycans of SARS-CoV-2 Spike Protein in Virus Infection and Antibody ProductionPMID 33928117Read ↗

Vulnerabilities in coronavirus glycan shields despite extensive glycosylationSemantic proximity Read ↗

Site-specific analysis of the SARS-CoV-2 glycan shieldSemantic proximity Read ↗

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

Protein <i>N</i> -glycosylation is essential for SARS-CoV-2 infectionSemantic proximity Read ↗

Spike N354 glycosylation augments SARS-CoV-2 fitness for human adaptation through multiple mechanismsSemantic proximity Read ↗

The SARS-CoV-2 Spike Glycoprotein Biosynthesis, Structure, Function, and Antigenicity: Implications for the Design of Spike-Based Vaccine ImmunogensSemantic proximity Read ↗

Spike N354 glycosylation augments SARS-CoV-2 fitness for human adaptation through structural plasticitySemantic proximity Read ↗

N-Glycome Profile of the Spike Protein S1: Systemic and Comparative Analysis from Eleven Variants of SARS-CoV-2Semantic proximity Read ↗

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

Glycosylation and Serological Reactivity of an Expression-enhanced SARS-CoV-2 Viral Spike MimeticSemantic proximity Read ↗

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