A human monoclonal antibody neutralizing SARS-CoV-2 Omicron variants containing the L452R mutation.

doi:10.1128/jvi.01223-24

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

Community

Back to search

Article

A human monoclonal antibody neutralizing SARS-CoV-2 Omicron variants containing the L452R mutation.

Journal of virology - 17 Dec 2024

Stein Saskia C, Hansen Guido, Ssebyatika George, Ströh Luisa J, Ochulor Okechukwu, Herold Elisabeth, Schwarzloh Britta, Mutschall Doris, Zischke Jasmin, Cordes Anne K, Schneider Talia, Hinrichs Imke, Blasczyk Rainer, Kleine-Weber Hannah, Hoffmann Markus, Klein Florian, Kaiser Franziska K, Gonzalez-Hernandez Mariana, Armando Federico, Ciurkiewicz Malgorzata, Beythien Georg, Pöhlmann Stefan, Baumgärtner Wolfgang, Osterhaus Albert, Schulz Thomas F, Krey Thomas

Abstract excerpt

The effectiveness of SARS-CoV-2 therapeutic antibodies targeting the spike (S) receptor-binding domain (RBD) has been hampered by the emergence of variants of concern (VOCs), which have acquired mutations to escape neutralizing antibodies (nAbs). These mutations are not evenly distributed on the RBD surface but cluster on several distinct surfaces, suggesting an influence of the targeted epitope on the capacity...

Read the complete abstract on PubMed

Topics

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

Share to Antibodies, Neutralizing

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Antibodies, Viral

Share to COVID-19

Share to Cricetinae

Share to Epitopes

Share to Neutralization Tests

Share to SARS-CoV-2

Share to Spike Glycoprotein, Coronavirus

Source

Open in PubMed Open full text

Identifiers

PMID: 39494911
DOI: 10.1128/jvi.01223-24
PMCID: PMC11650997

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

A human monoclonal antibody neutralizing SARS-CoV-2 Omicron variants containing the L452R mutation.PMID 39494911Read ↗

Uncovering a conserved vulnerability site in SARS‐CoV‐2 by a human antibodySemantic proximity Read ↗

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

Structural basis for broad sarbecovirus neutralization by a human monoclonal antibodySemantic proximity Read ↗

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

Identification of broad, potent antibodies to functionally constrained regions of SARS-CoV-2 spike following a breakthrough infectionSemantic proximity Read ↗

Landscape of human antibody recognition of the SARS-CoV-2 receptor binding domainSemantic proximity Read ↗

Structural insights for neutralization of BA.1 and BA.2 Omicron variants by a broadly neutralizing SARS-CoV-2 antibodySemantic proximity Read ↗

Atlas of currently available human neutralizing antibodies against SARS-CoV-2 and escape by Omicron sub-variants BA.1/BA.1.1/BA.2/BA.3Semantic proximity Read ↗

Epimaps of the SARS-CoV-2 Receptor-Binding Domain Mutational Landscape: Insights into Protein Stability, Epitope Prediction, and Antibody Binding.Semantic proximity Read ↗

Potent Neutralization of Omicron and other SARS-CoV-2 Variants of Concern by Biparatopic Human VH DomainsSemantic proximity Read ↗

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

A human monoclonal antibody targeting a conserved pocket in the SARS-CoV-2 receptor-binding domain coreSemantic proximity Read ↗

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