The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Structural delineation of SARS-CoV-2 broadly neutralizing antibody to Omicron subvariants including BA.4/BA.5 and BA.2.75
Open accessPreprint — published as 10.1038/s41467-023-39890-8 · Paper page
Abstract
SARS-CoV-2 Omicron subvariants have evolved to evade receptor-binding site (RBS) antibodies that exist in diverse individuals as public antibody clones. We rationally selected RBS antibodies resilient to mutations in emerging Omicron subvariants. Y489 was identified as a site of virus vulnerability and a common footprint of broadly neutralizing antibodies against the subvariants. Multiple Y489-binding antibodies were encoded by public clonotypes and additionally recognized F486, potentially accounting for the emergence of Omicron subvariants harboring the F486V mutation. However, a subclass of antibodies broadly neutralized BA.4/BA.5 variants via hydrophobic binding sites of rare clonotypes along with extremely high mutation-resilience under escape mutation screening. The structural basis for mutation-resilience of this antibody group may inform the design of therapeutics resistant to viral escape.
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Highly accurate protein structure prediction with AlphaFold
Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., Tunyasuvunakool, K., Bates, R., Žídek, A., Potapenko, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03819-2 · Cited by 43,764
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Metadata
- Authors
- Moriyama, S., Anraku, Y., Taminishi, S., Adachi, Y., Kuroda, D., Kita, S., Higuchi, Y., Kotaki, R., Tonouchi, K., Yumoto, K., Suzuki, T., Someya, T., Fukuhara, H., Kuroda, Y., Yamamoto, T., Onodera, T., Fukushi, S., Maeda, K., Nakamura-Uchiyama, F., Hashiguchi, T., Hoshino, A., Maenaka, K., & Takahashi, Y.
- Affiliations
- National Institute of Infectious Diseases (JP)
- Hokkaido University (JP)
- Kyoto Prefectural University of Medicine (JP)
- Waseda University (JP)
- Kyoto University (JP)
- Tokyo Metropolitan Bokutoh Hospital
- Corresponding author
- Moriyama, Saya
- Takahashi, Yoshimasa
- ORCID
- Venue
- Nature Communications
- Published
- 2022-12-21
- Volume
- 14
- Issue
- 1
- Pages
- 4198-4198
- ISSN
- 2041-1723 (ISSN-L)
- PMC
- PMC10349087
- OpenAlex
- W4384298552
- Cited by
- 22
- References
- 1
- Citations by year
- 2026: 3 · 2025: 7 · 2024: 9 · 2023: 3
- FWCI
- 4.53
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- Nature Communications (publishedVersion, cc-by)
- Research Square (acceptedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DORA PSI (Paul Scherrer Institute) (submittedVersion, cc-by)
- RePEc: Research Papers in Economics (submittedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- Japan Agency for Medical Research and Development (JP22gm1810004, JP20fk0108534, JP223fa627009, JP19fk0108104, JP223fa627005, 20fk0108298h0001, 21fk0108465h0001, JP21fk0108534, JP20fk0108516, JP20fk0108104, JP22fk0108141, JP22wm0325047, JP22ama121037)
- Ministry of Education, Culture, Sports, Science and Technology (JP19H04202, JP20H05873, JPMJCR20H8, JP20H05773)
- Paul Scherrer Institut
- University of Tokyo
- Japan Society for the Promotion of Science (JP20H05873, JP19fk0108104, 19H04202, JP223fa627005, JP20H05773)
- Japan Science and Technology Agency (JP19fk0108104, JPMJCR20H8)
- Institute of Medical Science, University of Tokyo
- Core Research for Evolutional Science and Technology (JPMJCR20H8)
- Topics
- Health Sciences › Medicine › Infectious Diseases › SARS-CoV-2 and COVID-19 Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › vaccines and immunoinformatics approaches
- Life Sciences › Immunology and Microbiology › Immunology › Monoclonal and Polyclonal Antibodies Research
- Keywords
- SARS-CoV-2 Omicron subvariants, neutralizing antibodies, receptor binding sites, XBB.1.5, BA.4/BA.5, antibody escape mutations, antibody design, hydrophobic binding site
- MeSH terms
- Broadly Neutralizing Antibodies, COVID-19, SARS-CoV-2, Antibodies, Viral, Binding Sites, Humans, Antibodies, Neutralizing, Spike Glycoprotein, Coronavirus
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