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7X93

The SARS-CoV-2 receptor binding domain bound with the Fab fragment of a human neutralizing antibody Ab765

Summary for 7X93
Entry DOI10.2210/pdb7x93/pdb
EMDB information33065
DescriptorSpike glycoprotein, Ab765 heavy chain, Ab765 light chain, ... (6 entities in total)
Functional Keywordssevere acute respiratory syndrome coronavirus-2 (sars-cov-2) spike trimer, covid-19, human neutralizing antibody, rbd, viral protein
Biological sourceSevere acute respiratory syndrome coronavirus 2
More
Total number of polymer chains5
Total formula weight479799.98
Authors
Kamada, K.,Shirouzu, M. (deposition date: 2022-03-15, release date: 2023-03-22, Last modification date: 2024-10-23)
Primary citationTakeshita, M.,Fukuyama, H.,Kamada, K.,Matsumoto, T.,Makino-Okamura, C.,Lin, Q.,Sakuma, M.,Kawahara, E.,Yamazaki, I.,Uchikubo-Kamo, T.,Tomabechi, Y.,Hanada, K.,Hisano, T.,Moriyama, S.,Takahashi, Y.,Ito, M.,Imai, M.,Maemura, T.,Furusawa, Y.,Yamayoshi, S.,Kawaoka, Y.,Shirouzu, M.,Ishii, M.,Saya, H.,Kondo, Y.,Kaneko, Y.,Suzuki, K.,Fukunaga, K.,Takeuchi, T.
Potent neutralizing broad-spectrum antibody against SARS-CoV-2 generated from dual-antigen-specific B cells from convalescents.
Iscience, 26:106955-106955, 2023
Cited by
PubMed Abstract: Several antibody therapeutics have been developed against SARS-CoV-2; however, they have attenuated neutralizing ability against variants. In this study, we generated multiple broadly neutralizing antibodies from B cells of convalescents, by using two types of receptor-binding domains, Wuhan strain and the Gamma variant as bait. From 172 antibodies generated, six antibodies neutralized all strains prior to the Omicron variant, and the five antibodies were able to neutralize some of the Omicron sub-strains. Structural analysis showed that these antibodies have a variety of characteristic binding modes, such as ACE2 mimicry. We subjected a representative antibody to the hamster infection model after introduction of the N297A modification, and observed a dose-dependent reduction of the lung viral titer, even at a dose of 2 mg/kg. These results demonstrated that our antibodies have certain antiviral activity as therapeutics, and highlighted the importance of initial cell-screening strategy for the efficient development of therapeutic antibodies.
PubMed: 37288342
DOI: 10.1016/j.isci.2023.106955
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.3 Å)
Structure validation

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