ArticleCell reports2022
Structural and functional impact by SARS-CoV-2 Omicron spike mutations.
Article in Cell reports, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 103 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
103 citing papers in PubMed, 164 citations in OpenAlex.
- Enriching Public Pathogen Genomic Records With Patient Metadata: Quantitative Study and Exploratory Case Analysis.JMIR bioinformatics and biotechnology · 2026Article
- Structural dynamics and allosteric communication of a SARS-like bat coronavirus spike glycoprotein.Biophysical journal · 2026Article
- Lock out: targeting TMPRSS2 to block influenza and coronaviruses.Journal of virology · 2026Review
- D614G reshapes allosteric networks and opening mechanisms of SARS-CoV-2 spikes.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Stringent selection drives convergence toward omicron-like SARS-CoV-2 receptor-binding motifs.Nature communications · 2026Article
- Recurrent SARS-CoV-2 Omicron broadly neutralizing humanized antibodies in different single human VProceedings of the National Academy of Sciences of the United States of America · 2026Article
- Impaired neutralizing antibody responses against the BA1.1, BA.2, and BA.5 Omicron SARS-CoV-2 subvariants in hospitalized adults infected with pre-Omicron variants in Argentina.Microbiology spectrum · 2026Article
- Mutation and ACE2-induced allosteric network rewiring in Delta and Omicron SARS-CoV-2 spike proteins.Biophysical journal · 2026Article
- Conserved CD4 T-cell responses correlate with antibody neutralization in solid organ transplant recipients after bivalent SARS-CoV-2 vaccination.Frontiers in immunology · 2026Article
- Identification and genomic characterization of BA.3.2: a highly divergent BA.3-related SARS-CoV-2 lineage from southern Africa.Virus evolution · 2026Article
- Immunologic and biophysical features of the BNT162b2 JN.1 and KP.2 adapted COVID-19 vaccines.Nature communications · 2025Article
- LL-37 Inhibits TMPRSS2-Mediated S2' Site Cleavage and SARS-CoV-2 Infection but Not Omicron Variants.Cell proliferation · 2025Article
- Mutation and ACE2-induced Allosteric Network Rewiring in Delta and Omicron SARS-CoV-2 Spike Proteins.bioRxiv : the preprint server for biology · 2025Article
- A Metadata-Driven Framework for Strengthening Pathogen Genomics Lessons from SARS-CoV-2.medRxiv : the preprint server for health sciences · 2025Article
- Multiplex Magnetic Biosensor Microarrays Facilitate Personalized Vaccination Schedules for SARS-CoV-2 Variants.Biochip journal · 2025Article
- Domain-Specific Impacts of Spike Protein Mutations on Infectivity and Antibody Escape in SARS-CoV-2 Omicron BA.1.Journal of microbiology and biotechnology · 2025Article
- The P132H mutation of SARS-CoV-2 NSP5 relieves its inhibition on interferon-β activation via blocking MAVS degradation.Cellular and molecular life sciences : CMLS · 2025Article
- SARS-CoV-2 spike protein: structure, viral entry and variants.Nature reviews. Microbiology · 2025Review
- Modulation of SARS-CoV-2 spike binding to ACE2 through conformational selection.Nature nanotechnology · 2025Article
- A 22 month prospective assessment of neutralizing and IgG antibody levels against SARS-CoV-2 variants following homologous and heterologous BNT162b2 boosting.Scientific reports · 2025Article
43 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
18 authors at 7 institutions in 1 country.
Funding
Abstract
The Omicron variant of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), bearing an unusually high number of mutations, has become a dominant strain in many countries within several weeks. We report here structural, functional, and antigenic properties of its full-length spike (S) protein with a native sequence in comparison with those of previously prevalent variants. Omicron S requires a substantially higher level of host receptor ACE2 for efficient membrane fusion than other variants, possibly explaining its unexpected cellular tropism. Mutations not only remodel the antigenic structure of the N-terminal domain of the S protein but also alter the surface of the receptor-binding domain in a way not seen in other variants, consistent with its remarkable resistance to neutralizing antibodies. These results suggest that Omicron S has acquired an extraordinary ability to evade host immunity by excessive mutations, which also compromise its fusogenic capability.
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