ArticleNature communications2024
Structural basis for the evolution and antibody evasion of SARS-CoV-2 BA.2.86 and JN.1 subvariants.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
44 citing papers in PubMed.
- Deep mutational scanning reveals the antibody escape and infectivity landscape of SARS-CoV-2 Omicron JN.1 and XEC receptor-binding domains.Emerging microbes & infections · 2026Article
- An Engineered HR1-Stem Helix-HR2 Trimeric Platform for Developing Broad-Spectrum Coronavirus Vaccines.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Immune evasion, infectivity, and membrane fusion of SARS-CoV-2 variants LP.8.1.1, XEC.25.1, XFG, and NB.1.8.1.Microbiology spectrum · 2026Article
- Article
- Broad Neutralizing Antibodies Against SARS-CoV-2: Current Progress and Engineering Strategies.Viruses · 2026Review
- A CD54-targeted magneto-responsive nanotheranostic for precision treatment of viral pneumonia via CTSB-mediated PANoptosis inhibition.Journal of nanobiotechnology · 2026Article
- Broadly neutralizing monoclonal antibodies derived from mRNA LNP immunization exhibit potent neutralizing ability against JN.1, KP.3.1.1 and XEC new Omicron variants.The Journal of general virology · 2026Article
- Monoclonal antibodies from COVID-19 convalescent patients target cryptic epitopes for broad SARS-CoV-2 neutralization.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Exploring the diverse binding ability of SARS-CoV-2 variant RBDs to different antibody classes: a computational study.RSC advances · 2026Article
- Comparative analysis of immune escape and BCR repertoire remodeling after Omicron BF.7 and JN.1 infections.Frontiers in immunology · 2026Article
- Determinants of success and failure of antibody-based strategies against respiratory viruses: insights from RSV and SARS-CoV-2.Frontiers in immunology · 2026Review
- Highly Efficient Site-Specific and Cassette Mutagenesis of Plasmids Harboring GC-Rich Sequences.Cells · 2025Article
- A non-spike nucleocapsid R204P mutation in SARS-CoV-2 Omicron XEC enhances inflammation and pathogenicity.Nature communications · 2025Article
- Characterization and immunogenicity of nanoparticle vaccines based on Clade 2 and Clade 3 sarbecovirus S2 proteins.NPJ vaccines · 2025Article
- Pathogenicity, virological features, and immune evasion of SARS-CoV-2 JN.1-derived variants including JN.1.7, KP.2, KP.3, and KP.3.1.1.Nature communications · 2025Article
- Spike mutations that affect the function and antigenicity of recent KP.3.1.1-like SARS-CoV-2 variants.Journal of virology · 2025Article
- Perspective Overview of Changing Population Immunity to COVID-19 in the Context of Infection, Vaccination, and Emerging SARS-CoV-2 Variants.Pathogens (Basel, Switzerland) · 2025Review
- SARS-CoV-2 Evolution in an HIV-Endemic Setting: A Genomic Epidemiology Study from Botswana.medRxiv : the preprint server for health sciences · 2025Article
- Review
- Evolution of BA.2.86 to JN.1 reveals that functional changes in non-structural viral proteins are required for fitness of SARS-CoV-2.Journal of virology · 2025Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
15 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Omicron subvariants of SARS-CoV-2, especially for BA.2.86 and JN.1, have rapidly spread across multiple countries, posing a significant threat in the ongoing COVID-19 pandemic. Distinguished by 34 additional mutations on the Spike (S) protein compared to its BA.2 predecessor, the implications of BA.2.86 and its evolved descendant, JN.1 with additional L455S mutation in receptor-binding domains (RBDs), are of paramount concern. In this work, we systematically examine the neutralization susceptibilities of SARS-CoV-2 Omicron subvariants and reveal the enhanced antibody evasion of BA.2.86 and JN.1. We also determine the cryo-EM structures of the trimeric S proteins from BA.2.86 and JN.1 in complex with the host receptor ACE2, respectively. The mutations within the RBDs of BA.2.86 and JN.1 induce a remodeling of the interaction network between the RBD and ACE2. The L455S mutation of JN.1 further induces a notable shift of the RBD-ACE2 interface, suggesting the notably reduced binding affinity of JN.1 than BA.2.86. An analysis of the broadly neutralizing antibodies possessing core neutralizing epitopes reveals the antibody evasion mechanism underlying the evolution of Omicron BA.2.86 subvariant. In general, we construct a landscape of evolution in virus-receptor of the circulating Omicron subvariants.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.