ArticleScience translational medicine2022
A human antibody reveals a conserved site on beta-coronavirus spike proteins and confers protection against SARS-CoV-2 infection.
Article in Science translational medicine, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 140 papers.
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Who cites it
140 citing papers in PubMed, 193 citations in OpenAlex.
- Structural serology of polyclonal antibody responses to mRNA-1273 and NVX-CoV2373 COVID-19 vaccines.Cell reports · 2025Trial
- An IgG-like fusion protein comprising an anti-spike S2 antibody and ACE2 exhibits potent and broad neutralization against SARS-CoV-2 and variants of concern.Antibody therapeutics · 2026Article
- Discovery of human antibody specific to the spike glycoprotein subunit 2 of SARS-CoV-2 and characterization of its broad-spectrum neutralizing activity.Infectious medicine · 2026Article
- An Engineered HR1-Stem Helix-HR2 Trimeric Platform for Developing Broad-Spectrum Coronavirus Vaccines.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Functional and structural basis of Omicron BA.3.2.1 spike.Cell reports · 2026Article
- Directed evolution of a stem-helix-targeting antibody enables MERS-CoV cross-neutralization through enhanced binding affinity.PLoS pathogens · 2026Article
- The SARS-CoV-2 S2'-helix compared to stem helix confers higher genetic barrier to antibody resistance.PLoS pathogens · 2026Article
- Structural and functional characterization of a conserved cryptic epitope on SARS-CoV-2 spike S2 subunit.PLoS pathogens · 2026Article
- A designed overlapping variant immunogen pool elicits broad sarbecovirus neutralization.bioRxiv : the preprint server for biology · 2026Article
- Broad Neutralizing Antibodies Against SARS-CoV-2: Current Progress and Engineering Strategies.Viruses · 2026Review
- CD4 T-cell platform for delivering interferons as an antiviral countermeasure with a focus on SARS-CoV-2.Molecular medicine (Cambridge, Mass.) · 2026Article
- mRNA-delivered neutralizing antibodies confer protection against SARS-CoV-2 in animal models.Journal of virology · 2026Article
- Elucidating the Molecular Mechanism of 3D1 Antibody Binding to a Swine Enteric Coronavirus Antigen.Viruses · 2026Article
- Article
- Heterologous betacoronavirus spike immunization in nonhuman primates elicits cross-reactive antibodies that neutralize both sarbeco- and merbecoviruses.bioRxiv : the preprint server for biology · 2026Article
- Human antibody targeting of coronavirus spike S2 subunit is associated with protection mediated by Fc effector functions.Journal of virology · 2025Article
- Common cold embecovirus imprinting primes broadly neutralizing antibody responses to SARS-CoV-2 S2.The Journal of experimental medicine · 2025Article
- Effect of the S2' site cleavage on SARS-CoV-2 spike.Nature communications · 2025Article
- Unconventional linkers facilitate potent stabilized coronavirus stem antibody responses following nanoparticle vaccination.bioRxiv : the preprint server for biology · 2025Article
- Novel HIV-1 fusion peptide immunogens using glycan-engineered alphavirus-like particles.NPJ vaccines · 2025Article
80 more citing papers are in PubMed but not listed here.
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Authors and funding
23 authors at 2 institutions in 1 country.
Funding
Abstract
Broadly neutralizing antibodies (bnAbs) to coronaviruses (CoVs) are valuable in their own right as prophylactic and therapeutic reagents to treat diverse CoVs and as templates for rational pan-CoV vaccine design. We recently described a bnAb, CC40.8, from a CoV disease 2019 (COVID-19) convalescent donor that exhibits broad reactivity with human β-CoVs. Here, we showed that CC40.8 targets the conserved S2 stem helix region of the CoV spike fusion machinery. We determined a crystal structure of CC40.8 Fab with a SARS-CoV-2 S2 stem peptide at 1.6-Å resolution and found that the peptide adopted a mainly helical structure. Conserved residues in β-CoVs interacted with CC40.8 antibody, thereby providing a molecular basis for its broad reactivity. CC40.8 exhibited in vivo protective efficacy against SARS-CoV-2 challenge in two animal models. In both models, CC40.8-treated animals exhibited less weight loss and reduced lung viral titers compared to controls. Furthermore, we noted that CC40.8-like bnAbs are relatively rare in human COVID-19 infection, and therefore, their elicitation may require rational structure-based vaccine design strategies. Overall, our study describes a target on β-CoV spike proteins for protective antibodies that may facilitate the development of pan-β-CoV vaccines.
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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.