7Y6N
The SARS-CoV-2 receptor binding domain bound with the Fab fragment of a human neutralizing antibody Ab803
Summary for 7Y6N
Entry DOI | 10.2210/pdb7y6n/pdb |
EMDB information | 33644 |
Descriptor | Spike glycoprotein, Ab803 heavy chain, Ab803 light chain, ... (4 entities in total) |
Functional Keywords | severe acute respiratory syndrome coronavirus-2 (sars-cov-2) spike trimer, covid-19, human neutralizing antibody, rbd, viral protein |
Biological source | Severe acute respiratory syndrome coronavirus 2 More |
Total number of polymer chains | 3 |
Total formula weight | 196440.09 |
Authors | Uchikubo, T.,Shirouzu, M. (deposition date: 2022-06-21, release date: 2023-06-21, Last modification date: 2024-11-13) |
Primary citation | Takeshita, 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: 37288342DOI: 10.1016/j.isci.2023.106955 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (4.4 Å) |
Structure validation
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