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

Identification of a broad sarbecovirus neutralizing antibody targeting a conserved epitope on the receptor-binding domain

1 Jan 2024

Abstract excerpt

Omicron, as the emerging variant with enhanced vaccine tolerance, has sharply disrupted most therapeutic antibodies. Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) belongs to the subgenus Sarbecovirus, members of which share high sequence similarity. Herein, we report one sarbecovirus antibody, 5817, which has broad-spectrum neutralization capacity against SARS-CoV-2 variants of concern (VOCs) and...

Read the complete abstract on PubMed

Topics

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

Share to Animal Virus Infections Studies
Share to SARS-CoV-2 and COVID-19 Research
Share to Viral gastroenteritis research and epidemiology

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 38175758
DOI: 10.1016/j.celrep.2023.113653

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

Identification of a broad sarbecovirus neutralizing antibody targeting a conserved epitope on the receptor-binding domainPMID 38175758Read ↗

Molecular basis of broad neutralization against SARS-CoV-2 variants including Omicron by a human antibodySemantic proximity Read ↗

Comprehensive structural analysis reveals broad-spectrum neutralizing antibodies against SARS-CoV-2 Omicron variantsSemantic proximity Read ↗

A cocktail containing two synergetic antibodies broadly neutralizes SARS-CoV-2 and its variants including Omicron BA.1 and BA.2Semantic proximity Read ↗

A Bispecific Antibody Targeting RBD and S2 Potently Neutralizes SARS-CoV-2 Omicron and Other Variants of ConcernSemantic proximity Read ↗

Structural basis of a two-antibody cocktail exhibiting highly potent and broadly neutralizing activities against SARS-CoV-2 variants including diverse Omicron sublineagesSemantic proximity Read ↗

Potent monoclonal antibodies neutralize Omicron sublineages and other SARS-CoV-2 variantsSemantic proximity Read ↗

Broadly neutralizing and protective nanobodies against SARS-CoV-2 Omicron subvariants BA.1, BA.2, and BA.4/5 and diverse sarbecovirusesSemantic proximity Read ↗

Structural Study of SARS-CoV-2 Antibodies Identifies a Broad-Spectrum Antibody That Neutralizes the Omicron Variant by Disassembling the Spike TrimerSemantic proximity Read ↗

Selection and structural bases of potent broadly neutralizing antibodies from 3-dose vaccinees that are highly effective against diverse SARS-CoV-2 variants, including Omicron sublineagesSemantic proximity Read ↗

A potent SARS-CoV-2 antibody neutralizes Omicron variant by disassembling the spike trimerSemantic proximity Read ↗

Structural and mutational analyses define distinct molecular routes to broad SARS-CoV-2 receptor-binding domain recognitionSemantic proximity Read ↗

Potent neutralization by a receptor binding domain monoclonal antibody with broad specificity for SARS-CoV-2 JN.1 and other variantsSemantic proximity Read ↗

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