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8HGM

Structure of SARS-CoV-2 spike RBD in complex with neutralizing antibody NIV-11

Summary for 8HGM
Entry DOI10.2210/pdb8hgm/pdb
EMDB information34742
DescriptorSpike glycoprotein, NIV-11 Fab heavy chain, NIV-11 Fab light chain, ... (4 entities in total)
Functional Keywordscomplex, viral protein, viral protein-immune system complex, viral protein/immune system
Biological sourceSevere acute respiratory syndrome coronavirus 2 (2019-nCoV,SARS-CoV-2)
More
Total number of polymer chains3
Total formula weight190160.68
Authors
Primary citationMoriyama, S.,Anraku, Y.,Taminishi, S.,Adachi, Y.,Kuroda, D.,Kita, S.,Higuchi, Y.,Kirita, 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.
Structural delineation and computational design of SARS-CoV-2-neutralizing antibodies against Omicron subvariants.
Nat Commun, 14:4198-4198, 2023
Cited by
PubMed 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 high mutation-resilience under escape mutation screening. A computationally designed antibody based on one of the Y489-binding antibodies, NIV-10/FD03, was able to bind XBB with any 486 mutation and neutralized XBB.1.5. The structural basis for the mutation-resilience of this Y489-binding antibody group may provide important insights into the design of therapeutics resistant to viral escape.
PubMed: 37452031
DOI: 10.1038/s41467-023-39890-8
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.4 Å)
Structure validation

226707

數據於2024-10-30公開中

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