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 basis of increased binding affinities of spikes from SARS-CoV-2 Omicron variants to rabbit and hare ACE2s reveals the expanding host tendency.

mBio - 14 Feb 2024

Shi Kaiyuan, Li Linjie, Luo Chunliang, Xu Zepeng, Huang Baihan, Ma Sufang, Liu Kefang, Yu Guanghui, Gao George F

Abstract excerpt

The potential host range of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has been expanding alongside its evolution during the pandemic, with rabbits and hares being considered important potential hosts, supported by a report of rabbit sero-prevalence in nature. We measured the binding affinities of rabbit and hare angiotensin-converting enzyme 2 (ACE2) with receptor-binding domains (RBDs) from...

Read the complete abstract on PubMed

Topics

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

Share to Angiotensin-Converting Enzyme 2
Share to COVID-19

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to ACE2 gene

Share to Mutation

Share to Protein Binding

Share to Rabbits

Share to SARS-CoV-2

Share to Spike Glycoprotein, Coronavirus

Source

Open in PubMed Open full text

Identifiers

PMID: 38112468
DOI: 10.1128/mbio.02988-23
PMCID: PMC10870819

Genes

ACE2

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

Structural basis of increased binding affinities of spikes from SARS-CoV-2 Omicron variants to rabbit and hare ACE2s reveals the expanding host tendency.PMID 38112468Read ↗

Broad host range of SARS-CoV-2 predicted by comparative and structural analysis of ACE2 in vertebrates.Semantic proximity Read ↗

Structural basis of white-tailed deer, Odocoileus virginianus , ACE2 recognizing all the SARS-CoV-2 variants of concern with high affinitySemantic proximity Read ↗

Evolution of SARS-CoV-2 Spikes shapes their binding affinities to animal ACE2 orthologs.Semantic proximity Read ↗

Evolutionary trajectory of receptor binding specificity and promiscuity of the spike protein of SARS-CoV-2Semantic proximity Read ↗

Featuring ACE2 binding SARS-CoV and SARS-CoV-2 through a conserved evolutionary pattern of amino acid residuesSemantic proximity Read ↗

A novel structure-based approach for identification of vertebrate susceptibility to SARS-CoV-2: implications for future surveillance programmesSemantic proximity Read ↗

Broader-species receptor binding and structural bases of Omicron SARS-CoV-2 to both mouse and palm-civet ACE2sSemantic proximity Read ↗

Identifying zoonotic origin of SARS-CoV-2 by modeling the binding affinity between Spike receptor-binding domain and host ACE2Semantic proximity Read ↗

Evaluating the transmission feasibility of SARS-CoV-2 Omicron (B.1.1.529) variant to 143 mammalian hosts: insights from S protein RBD and host ACE2 interaction studies.Semantic proximity Read ↗

Effect of SARS-CoV-2 spike mutations on animal ACE2 usage and in vitro neutralization sensitivitySemantic proximity Read ↗

Spike structures, receptor binding, and immune escape of recently circulating SARS-CoV-2 Omicron BA.2.86, JN.1, EG.5, EG.5.1, and HV.1 sub-variants.Semantic proximity Read ↗

Identifying the Zoonotic Origin of SARS-CoV-2 by Modeling the Binding Affinity between the Spike Receptor-Binding Domain and Host ACE2Semantic proximity Read ↗

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