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

Compensatory epistasis maintains ACE2 affinity in SARS-CoV-2 Omicron BA.1

16 Nov 2022

Abstract excerpt

Abstract The Omicron BA.1 variant emerged in late 2021 and quickly spread across the world. Compared to the earlier SARS-CoV-2 variants, BA.1 has many mutations, some of which are known to enable antibody escape. Many of these antibody-escape mutations individually decrease the spike receptor-binding domain (RBD) affinity for ACE2, but BA.1 still binds ACE2 with high affinity. The fitness and evolution of the...

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 COVID-19 Clinical Research Studies
Share to SARS-CoV-2 and COVID-19 Research

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 36384919
DOI: 10.1038/s41467-022-34506-z

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Compensatory epistasis maintains ACE2 affinity in SARS-CoV-2 Omicron BA.1PMID 36384919Read ↗

Deep mutational scans for ACE2 binding, RBD expression, and antibody escape in the SARS-CoV-2 Omicron BA.1 and BA.2 receptor-binding domains.Semantic proximity Read ↗

Deep mutational scanning of SARS-CoV-2 Omicron BA.2.86 and epistatic emergence of the KP.3 variantSemantic proximity Read ↗

Deep mutational scanning of SARS-CoV-2 Omicron BA.2.86 and epistatic emergence of the KP.3 variantSemantic proximity Read ↗

The landscape of antibody binding affinity in SARS-CoV-2 Omicron BA.1 evolution.Semantic proximity Read ↗

Deep mutational scans for ACE2 binding, RBD expression, and antibody escape in the SARS-CoV-2 Omicron BA.1 and BA.2 receptor-binding domainsSemantic proximity Read ↗

Epistasis and background dependence in the evolution of Omicron variants of the SARS-CoV-2 Spike proteinSemantic proximity Read ↗

Epistasis and background dependence in the evolution of Omicron variants of the SARS-CoV-2 spike protein.Semantic proximity Read ↗

Ensemble-Based Mutational Profiling and Network Analysis of the SARS-CoV-2 Spike Omicron XBB Lineages for Interactions with the ACE2 Receptor and Antibodies: Cooperation of Binding Hotspots in Mediating Epistatic Couplings Underlies Binding Mechanism and Immune Escape.Semantic proximity Read ↗

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

Mutations in the SARS-CoV-2 spike receptor binding domain and their delicate balance between ACE2 affinity and antibody evasionSemantic proximity Read ↗

Immune evasion and ACE2 binding affinity contribute to SARS-CoV-2 evolution.Semantic proximity Read ↗

Molecular and structural insights into SARS-CoV-2 evolution: from BA.2 to XBB subvariants.Semantic proximity Read ↗

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