학술논문

A human antibody reveals a conserved site on beta-coronavirus spike proteins and confers protection against SARS-CoV-2 infection
Document Type
article
Source
Science Translational Medicine. 14(637)
Subject
Medical Microbiology
Biomedical and Clinical Sciences
Immunology
Immunization
Biodefense
Vaccine Related
Prevention
Pneumonia & Influenza
Biotechnology
Emerging Infectious Diseases
Infectious Diseases
Lung
Pneumonia
Infection
Good Health and Well Being
Animals
Antibodies
Neutralizing
Antibodies
Viral
COVID-19
Humans
SARS-CoV-2
Spike Glycoprotein
Coronavirus
Biological Sciences
Medical and Health Sciences
Medical biotechnology
Biomedical engineering
Language
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.