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

Structural analysis of receptor engagement and antigenic drift within the BA.2 spike protein

1 Jan 2023

Abstract excerpt

The BA.2 sub-lineage of the Omicron (B.1.1.529) severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) variant rapidly supplanted the original BA.1 sub-lineage in early 2022. Both lineages threatened the efficacy of vaccine-elicited antibodies and acquired increased binding to several mammalian ACE2 receptors. Cryoelectron microscopy (cryo-EM) analysis of the BA.2 spike (S) glycoprotein in complex with...

Read the complete abstract on PubMed

Topics

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

Share to Escherichia coli research studies
Share to Monoclonal and Polyclonal Antibodies Research
Share to SARS-CoV-2 and COVID-19 Research

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 36640338
DOI: 10.1016/j.celrep.2022.111964

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structural analysis of receptor engagement and antigenic drift within the BA.2 spike proteinPMID 36640338Read ↗

Structural basis for the evolution and antibody evasion of SARS-CoV-2 BA.2.86 and JN.1 subvariants.Semantic proximity Read ↗

Cryo-EM structures of SARS-CoV-2 Omicron BA.2 spikeSemantic proximity Read ↗

Functional and Structural Basis of Omicron BA.3.2.1 SpikeSemantic proximity Read ↗

Antibody escape and cryptic cross-domain stabilization in the SARS-CoV-2 Omicron spike protein.Semantic proximity Read ↗

Antibody escape and cryptic cross-domain stabilization in the SARS-CoV-2 Omicron spike proteinSemantic proximity Read ↗

Structural basis of SARS-CoV-2 Omicron immune evasion and receptor engagementSemantic proximity Read ↗

Structural basis of SARS-CoV-2 Omicron immune evasion and receptor engagement.Semantic proximity Read ↗

A structure-function analysis shows SARS-CoV-2 BA.2.86 balances antibody escape and ACE2 affinity.Semantic proximity Read ↗

SARS-CoV-2 Omicron variant: Antibody evasion and cryo-EM structure of spike protein-ACE2 complex.Semantic proximity Read ↗

AlphaFold2-Enabled Atomistic Modeling of Structure, Conformational Ensembles, and Binding Energetics of the SARS-CoV-2 Omicron BA.2.86 Spike Protein with ACE2 Host Receptor and Antibodies: Compensatory Functional Effects of Binding Hotspots in Modulating Mechanisms of Receptor Binding and Immune Escape.Semantic proximity Read ↗

SARS-CoV-2 Omicron Variant: ACE2 Binding, Cryo-EM Structure of Spike Protein-ACE2 Complex and Antibody EvasionSemantic proximity Read ↗

SARS-CoV-2 Omicron XBB lineage spike structures, conformations, antigenicity, and receptor recognition.Semantic proximity Read ↗

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