ArticleNature communications2021
Cross-neutralizing antibodies bind a SARS-CoV-2 cryptic site and resist circulating variants.
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Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.
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52citing papers in PubMed
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52 citing papers in PubMed.
- Targeting of conserved spike epitopes enables broad antibody neutralisation of diverse bat sarbecoviruses.PLoS biology · 2026Article
- A novel monoclonal antibody targeting the hemagglutinin-neuraminidase of peste des petits ruminants virus maintains neutralizing activity by blocking viral adsorption and receptor interaction.Journal of virology · 2026Article
- Nanobody-based combination vaccine using licensed protein nanoparticles protects animals against respiratory and viral infections.Nature biomedical engineering · 2026Article
- AI-aided design of multi-epitope peptide vaccine elicits cellular and humoral immunity to broad Omicron subvariants.Zoological research · 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
- Identification of a novel monoclonal antibody derived from the lumpy skin disease virus ORF123 that confers cross-binding and cross-neutralizing activity against Capripoxvirus members.Veterinary research · 2026Article
- A computational pipeline to discover potential cross-reactive antibodies: a case study on coronavirus.Frontiers in cellular and infection microbiology · 2026Article
- Engineering a multivalent antibody nanoparticle to overcome SARS-CoV-2 Omicron immune evasion.PLoS pathogens · 2025Article
- Review
- Flow Cytometry Multiplex Bead Array Technology and Its Immunological Clinical Applications in Covid-19 Era.Balkan journal of medical genetics : BJMG · 2025Article
- Discovery of Synergistic Broadly Neutralizing Antibodies Targeting Non-Dominant Epitopes on SARS-CoV-2 RBD and NTD.Vaccines · 2025Article
- Early 2022 breakthrough infection sera from India target the conserved cryptic class 5 epitope to counteract immune escape by SARS-CoV-2 variants.Journal of virology · 2025Article
- A single residue switch mediates the broad neutralization of Rotaviruses.Nature communications · 2025Article
- Affinity maturation endows potent activity onto class 6 SARS-CoV-2 broadly neutralizing antibodies.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Computational electrostatic engineering of nanobodies for enhanced SARS-CoV-2 receptor binding domain recognition.Frontiers in molecular biosciences · 2025Article
- Structural Immunology of SARS-CoV-2.Immunological reviews · 2025Review
- Combination of spatial transcriptomics analysis and retrospective study reveals liver infection of SARS-COV-2 is associated with clinical outcomes of COVID-19.EBioMedicine · 2025Article
- Structural insight into broadening SARS-CoV-2 neutralization by an antibody cocktail harbouring both NTD and RBD potent antibodies.Emerging microbes & infections · 2024Article
- Structural characterization of human monoclonal antibodies targeting uncommon antigenic sites on spike glycoprotein of SARS-CoV.The Journal of clinical investigation · 2024Article
- A cryptic site in class 5 epitope of SARS-CoV-2 RBD maintains highly conservation across natural isolates.iScience · 2024Article
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Authors and funding
31 authors.
Tingting Li *State Key Laboratory of Molecular Vaccinology and Molecular Diagnostics, School of Life Sciences, School of Public Health, Xiamen University, 361102, Xiamen, Fujian, China.ORCID 0000-0002-9917-7804
Wenhui Xue *State Key Laboratory of Molecular Vaccinology and Molecular Diagnostics, School of Life Sciences, School of Public Health, Xiamen University, 361102, Xiamen, Fujian, China.
Qingbing Zheng *State Key Laboratory of Molecular Vaccinology and Molecular Diagnostics, School of Life Sciences, School of Public Health, Xiamen University, 361102, Xiamen, Fujian, China.ORCID 0000-0002-7516-9965
Shuo Song *Institute for Hepatology, National Clinical Research Center for Infectious Disease, Shenzhen Third People's Hospital, 518112, Shenzhen, Guangdong, China.ORCID 0000-0002-0289-2941
Chuanlai Yang *State Key Laboratory of Molecular Vaccinology and Molecular Diagnostics, School of Life Sciences, School of Public Health, Xiamen University, 361102, Xiamen, Fujian, China.
Hualong Xiong *State Key Laboratory of Molecular Vaccinology and Molecular Diagnostics, School of Life Sciences, School of Public Health, Xiamen University, 361102, Xiamen, Fujian, China.
Sibo ZhangState Key Laboratory of Molecular Vaccinology and Molecular Diagnostics, School of Life Sciences, School of Public Health, Xiamen University, 361102, Xiamen, Fujian, China.
Minqing HongState Key Laboratory of Molecular Vaccinology and Molecular Diagnostics, School of Life Sciences, School of Public Health, Xiamen University, 361102, Xiamen, Fujian, China.
Yali ZhangState Key Laboratory of Molecular Vaccinology and Molecular Diagnostics, School of Life Sciences, School of Public Health, Xiamen University, 361102, Xiamen, Fujian, China.
Hai YuState Key Laboratory of Molecular Vaccinology and Molecular Diagnostics, School of Life Sciences, School of Public Health, Xiamen University, 361102, Xiamen, Fujian, China.
Yuyun ZhangState Key Laboratory of Molecular Vaccinology and Molecular Diagnostics, School of Life Sciences, School of Public Health, Xiamen University, 361102, Xiamen, Fujian, China.
Hui SunState Key Laboratory of Molecular Vaccinology and Molecular Diagnostics, School of Life Sciences, School of Public Health, Xiamen University, 361102, Xiamen, Fujian, China.
Yang HuangState Key Laboratory of Molecular Vaccinology and Molecular Diagnostics, School of Life Sciences, School of Public Health, Xiamen University, 361102, Xiamen, Fujian, China.
Tingting DengState Key Laboratory of Molecular Vaccinology and Molecular Diagnostics, School of Life Sciences, School of Public Health, Xiamen University, 361102, Xiamen, Fujian, China.
Xin ChiState Key Laboratory of Molecular Vaccinology and Molecular Diagnostics, School of Life Sciences, School of Public Health, Xiamen University, 361102, Xiamen, Fujian, China.
Jinjin LiState Key Laboratory of Molecular Vaccinology and Molecular Diagnostics, School of Life Sciences, School of Public Health, Xiamen University, 361102, Xiamen, Fujian, China.
Shaojuan WangState Key Laboratory of Molecular Vaccinology and Molecular Diagnostics, School of Life Sciences, School of Public Health, Xiamen University, 361102, Xiamen, Fujian, China.
Lizhi ZhouState Key Laboratory of Molecular Vaccinology and Molecular Diagnostics, School of Life Sciences, School of Public Health, Xiamen University, 361102, Xiamen, Fujian, China.
Tingting ChenState Key Laboratory of Molecular Vaccinology and Molecular Diagnostics, School of Life Sciences, School of Public Health, Xiamen University, 361102, Xiamen, Fujian, China.
Yingbin WangState Key Laboratory of Molecular Vaccinology and Molecular Diagnostics, School of Life Sciences, School of Public Health, Xiamen University, 361102, Xiamen, Fujian, China.
Tong ChengState Key Laboratory of Molecular Vaccinology and Molecular Diagnostics, School of Life Sciences, School of Public Health, Xiamen University, 361102, Xiamen, Fujian, China.ORCID 0000-0002-1638-6214
Tianying ZhangState Key Laboratory of Molecular Vaccinology and Molecular Diagnostics, School of Life Sciences, School of Public Health, Xiamen University, 361102, Xiamen, Fujian, China.ORCID 0000-0002-2477-329X
Quan YuanState Key Laboratory of Molecular Vaccinology and Molecular Diagnostics, School of Life Sciences, School of Public Health, Xiamen University, 361102, Xiamen, Fujian, China.ORCID 0000-0001-5487-561X
Qinjian ZhaoState Key Laboratory of Molecular Vaccinology and Molecular Diagnostics, School of Life Sciences, School of Public Health, Xiamen University, 361102, Xiamen, Fujian, China.
Jun ZhangState Key Laboratory of Molecular Vaccinology and Molecular Diagnostics, School of Life Sciences, School of Public Health, Xiamen University, 361102, Xiamen, Fujian, China.
Jason S McLellanDepartment of Molecular Biosciences, The University of Texas at Austin, Austin, 78712, TX, USA.ORCID 0000-0003-3991-542X
Z Hong ZhouCalifornia NanoSystems Institute (CNSI), UCLA, Los Angeles, 90095, CA, USA. hong.zhou@ucla.edu.ORCID 0000-0002-8373-4717
Zheng ZhangInstitute for Hepatology, National Clinical Research Center for Infectious Disease, Shenzhen Third People's Hospital, 518112, Shenzhen, Guangdong, China. zhangzheng1975@aliyun.com.ORCID 0000-0002-3544-1389
Shaowei LiState Key Laboratory of Molecular Vaccinology and Molecular Diagnostics, School of Life Sciences, School of Public Health, Xiamen University, 361102, Xiamen, Fujian, China. shaowei@xmu.edu.cn.ORCID 0000-0002-3374-1038
Ying GuState Key Laboratory of Molecular Vaccinology and Molecular Diagnostics, School of Life Sciences, School of Public Health, Xiamen University, 361102, Xiamen, Fujian, China. guying@xmu.edu.cn.ORCID 0000-0002-2870-2800
Ningshao XiaState Key Laboratory of Molecular Vaccinology and Molecular Diagnostics, School of Life Sciences, School of Public Health, Xiamen University, 361102, Xiamen, Fujian, China. nsxia@xmu.edu.cn.ORCID 0000-0003-0179-5266
Funding
National Natural Science Foundation of China (National Science Foundation of China) 81991491National Natural Science Foundation of China (National Science Foundation of China) 82001756National Natural Science Foundation of China (National Science Foundation of China) U1705283
Abstract
The emergence of numerous variants of SARS-CoV-2, the causative agent of COVID-19, has presented new challenges to the global efforts to control the COVID-19 pandemic. Here, we obtain two cross-neutralizing antibodies (7D6 and 6D6) that target Sarbecoviruses' receptor-binding domain (RBD) with sub-picomolar affinities and potently neutralize authentic SARS-CoV-2. Crystal structures show that both antibodies bind a cryptic site different from that recognized by existing antibodies and highly conserved across Sarbecovirus isolates. Binding of these two antibodies to the RBD clashes with the adjacent N-terminal domain and disrupts the viral spike. Both antibodies confer good resistance to mutations in the currently circulating SARS-CoV-2 variants. Thus, our results have direct relevance to public health as options for passive antibody therapeutics and even active prophylactics. They can also inform the design of pan-sarbecovirus vaccines.
Indexed as
AnimalsAntibodies, MonoclonalAntibodies, ViralBinding SitesBroadly Neutralizing AntibodiesChlorocebus aethiopsCHO CellsCOVID-19CricetulusEpitopesHEK293 CellsHumansImmunization, PassiveMiceMiddle East Respiratory Syndrome CoronavirusNeutralization TestsAntibodies, MonoclonalAntibodies, ViralBroadly Neutralizing AntibodiesEpitopesReceptors, VirusSpike Glycoprotein, Coronavirusspike glycoprotein, SARS-CoVspike protein, SARS-CoV-2
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