ArticleImmunity2021
A SARS-CoV-2 antibody broadly neutralizes SARS-related coronaviruses and variants by coordinated recognition of a virus-vulnerable site.
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Article in Immunity, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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39citing papers in PubMed
4.2field-weighted citation impact, top 5% of its field
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Who cites it
39 citing papers in PubMed, 75 citations in OpenAlex.
- Longitudinal analysis of immune responses to SARS-CoV-2 recombinant vaccine S-268019-b in phase 1/2 prime-boost study.Frontiers in immunology · 2025Trial
- Rapid immunization and antibody redesign platform discovers broadly neutralizing antibodies against non-immunized SARS-CoV-2 variant.Molecular therapy : the journal of the American Society of Gene Therapy · 2026Article
- Review
- Structural and virological identification of neutralizing antibody footprint provides insights into therapeutic antibody design against SARS-CoV-2 variants.Communications biology · 2025Article
- Allosteric Control and Glycan Shielding Adaptations in the SARS-CoV-2 Spike from Early to Peak Virulence.bioRxiv : the preprint server for biology · 2025Article
- Molecular convergence of neutralizing antibodies in human revealed by repeated rabies vaccination.NPJ vaccines · 2025Article
- Different Fc scaffolds enhance the breadth ofFrontiers in immunology · 2025Article
- Japan-Korea collaboration on biophysical techniques for drug discovery in infectious diseases: Toward future pandemic preparedness.Biophysics and physicobiology · 2025Article
- The lethal K18-hACE2 knock-in mouse model mimicking the severe pneumonia of COVID-19 is practicable for antiviral development.Emerging microbes & infections · 2024Article
- Developing a workflow for the isolation of hybridoma cells producing fully human antigen-specific antibodies using a surface IgG detection method.Scientific reports · 2024Article
- Overcoming antibody-resistant SARS-CoV-2 variants with bispecific antibodies constructed using non-neutralizing antibodies.iScience · 2024Article
- Antibodies from dengue patients with prior exposure to Japanese encephalitis virus are broadly neutralizing against Zika virus.Communications biology · 2024Article
- Inadequate structural constraint on Fab approach rather than paratope elicitation limits HIV-1 MPER vaccine utility.Nature communications · 2023Article
- IgG3 subclass antibodies recognize antigenically drifted influenza viruses and SARS-CoV-2 variants through efficient bivalent binding.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Structural basis for cross-group recognition of an influenza virus hemagglutinin antibody that targets postfusion stabilized epitope.PLoS pathogens · 2023Article
- Structural delineation and computational design of SARS-CoV-2-neutralizing antibodies against Omicron subvariants.Nature communications · 2023Article
- CD62L expression marks SARS-CoV-2 memory B cell subset with preference for neutralizing epitopes.Science advances · 2023Article
- Structural basis of spike RBM-specific human antibodies counteracting broad SARS-CoV-2 variants.Communications biology · 2023Article
- Heterologous SARS-CoV-2 spike protein booster elicits durable and broad antibody responses against the receptor-binding domain.Nature communications · 2023Article
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Authors and funding
35 authors at 6 institutions in 1 country.
Taishi OnoderaResearch Center for Drug and Vaccine Development, National Institute of Infectious Diseases, Tokyo 162-8640, Japan.
Shunsuke KitaLaboratory of Biomolecular Science, and Center for Research and Education on Drug Discovery, Faculty of Pharmaceutical Sciences, Hokkaido University, Sapporo 060-0812, Japan.
Yu AdachiResearch Center for Drug and Vaccine Development, National Institute of Infectious Diseases, Tokyo 162-8640, Japan.
Saya MoriyamaResearch Center for Drug and Vaccine Development, National Institute of Infectious Diseases, Tokyo 162-8640, Japan.
Akihiko SatoDivision of Molecular Pathobiology, Research Center for Zoonosis Control, Hokkaido University, Sapporo 001-0020, Japan; Drug Discovery & Disease Research Laboratory, Shionogi & Co., Ltd., Osaka 561-0825, Japan.
Takao NomuraLaboratory of Biomolecular Science, and Center for Research and Education on Drug Discovery, Faculty of Pharmaceutical Sciences, Hokkaido University, Sapporo 060-0812, Japan.
Shuhei SakakibaraLaboratory of Immune Regulation, WPI Immunology Frontier Research Center, Osaka University, Osaka 565-0871, Japan.
Takeshi InoueLaboratory of Lymphocyte Differentiation, WPI Immunology Frontier Research Center, Osaka University, Osaka 565-0871, Japan.
Takashi TadokoroLaboratory of Biomolecular Science, and Center for Research and Education on Drug Discovery, Faculty of Pharmaceutical Sciences, Hokkaido University, Sapporo 060-0812, Japan.
Yuki AnrakuLaboratory of Biomolecular Science, and Center for Research and Education on Drug Discovery, Faculty of Pharmaceutical Sciences, Hokkaido University, Sapporo 060-0812, Japan.
Kohei YumotoLaboratory of Biomolecular Science, and Center for Research and Education on Drug Discovery, Faculty of Pharmaceutical Sciences, Hokkaido University, Sapporo 060-0812, Japan.
Cong TianLaboratory of Biomolecular Science, and Center for Research and Education on Drug Discovery, Faculty of Pharmaceutical Sciences, Hokkaido University, Sapporo 060-0812, Japan.
Hideo FukuharaLaboratory of Biomolecular Science, and Center for Research and Education on Drug Discovery, Faculty of Pharmaceutical Sciences, Hokkaido University, Sapporo 060-0812, Japan; Global Station for Biosurfaces and Drug Discovery, Hokkaido University, Sapporo 060-0812, Japan.
Michihito SasakiDivision of Molecular Pathobiology, Research Center for Zoonosis Control, Hokkaido University, Sapporo 001-0020, Japan.
Yasuko OrbaDivision of Molecular Pathobiology, Research Center for Zoonosis Control, Hokkaido University, Sapporo 001-0020, Japan.
Nozomi ShiwaDepartment of Pathology, National Institute of Infectious Diseases, Tokyo 208-0011, Japan.
Naoko IwataDepartment of Pathology, National Institute of Infectious Diseases, Tokyo 208-0011, Japan.
Noriyo NagataDepartment of Pathology, National Institute of Infectious Diseases, Tokyo 208-0011, Japan.
Tateki SuzukiDepartment of Virology, Faculty of Medicine, Kyushu University, Fukuoka 812-8582, Japan.
Jiei SasakiDepartment of Virology, Faculty of Medicine, Kyushu University, Fukuoka 812-8582, Japan.
Tsuyoshi SekizukaPathogen Genomic Center, National Institute of Infectious Diseases, Tokyo 162-8640, Japan.
Keisuke TonouchiResearch Center for Drug and Vaccine Development, National Institute of Infectious Diseases, Tokyo 162-8640, Japan; Department of Life Science and Medical Bioscience, Waseda University, Tokyo 162-8480, Japan.
Lin SunResearch Center for Drug and Vaccine Development, National Institute of Infectious Diseases, Tokyo 162-8640, Japan.
Shuetsu FukushiDepartment of Virology I, National Institute of Infectious Diseases, Tokyo 162-8640, Japan.
Hiroyuki SatofukaChromosome Engineering Research Center, Tottori University, Tottori 683-8503, Japan.
Yasuhiro KazukiChromosome Engineering Research Center, Tottori University, Tottori 683-8503, Japan; Division of Genome and Cellular Functions, Department of Molecular and Cellular Biology, School of Life Science, Faculty of Medicine, Tottori University, Tottori 683-8503, Japan.
Mitsuo OshimuraTrans Chromosomics Inc., Tottori 683-8503, Japan.
Tomohiro KurosakiLaboratory of Lymphocyte Differentiation, WPI Immunology Frontier Research Center, Osaka University, Osaka 565-0871, Japan.
Makoto KurodaPathogen Genomic Center, National Institute of Infectious Diseases, Tokyo 162-8640, Japan.
Yoshiharu MatsuuraLaboratory of Virus Control, Center for Infectious Diseases Education and Research, Osaka University, Osaka 565-0871, Japan.
Tadaki SuzukiDepartment of Pathology, National Institute of Infectious Diseases, Tokyo 208-0011, Japan.
Hirofumi SawaDivision of Molecular Pathobiology, Research Center for Zoonosis Control, Hokkaido University, Sapporo 001-0020, Japan.
Takao HashiguchiDepartment of Virology, Faculty of Medicine, Kyushu University, Fukuoka 812-8582, Japan; Laboratory of Medical Virology, Institute for Frontier Life and Medical Sciences, Kyoto University, Kyoto 606-8507, Japan.
Katsumi MaenakaLaboratory of Biomolecular Science, and Center for Research and Education on Drug Discovery, Faculty of Pharmaceutical Sciences, Hokkaido University, Sapporo 060-0812, Japan; Global Station for Biosurfaces and Drug Discovery, Hokkaido University, Sapporo 060-0812, Japan. Electronic address: maenaka@pharm.hokudai.ac.jp.
Yoshimasa TakahashiResearch Center for Drug and Vaccine Development, National Institute of Infectious Diseases, Tokyo 162-8640, Japan. Electronic address: ytakahas@niid.go.jp.
Hokkaido University · JPNational Institute of Infectious Diseases · JPKyushu University · JPThe University of Osaka · JPTottori University · JPWaseda University · JP
Funding
No grant is acknowledged in the PubMed record.
Abstract
Potent neutralizing SARS-CoV-2 antibodies often target the spike protein receptor-binding site (RBS), but the variability of RBS epitopes hampers broad neutralization of multiple sarbecoviruses and drifted viruses. Here, using humanized mice, we identified an RBS antibody with a germline V
Indexed as
AnimalsBetacoronavirusBinding Sites, AntibodyBroadly Neutralizing AntibodiesCOVID-19CricetinaeCross ReactionsHumansImmunoglobulin Class SwitchingImmunoglobulin Fab FragmentsImmunoglobulin GMiceProtein DomainsSARS-CoV-2Spike Glycoprotein, CoronavirusBroadly Neutralizing AntibodiesImmunoglobulin Fab FragmentsImmunoglobulin GSpike Glycoprotein, Coronavirusspike protein, SARS-CoV-2IgG3neutralizing antibodyreceptor-binding domainSARS-CoVSARS-CoV-2variants of concernX-ray crystallography
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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.