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TitlePotent neutralizing broad-spectrum antibody against SARS-CoV-2 generated from dual-antigen-specific B cells from convalescents.
Journal, issue, pagesiScience, Vol. 26, Issue 6, Page 106955, Year 2023
Publish dateJun 16, 2023
AuthorsMasaru Takeshita / Hidehiro Fukuyama / Katsuhiko Kamada / Takehisa Matsumoto / Chieko Makino-Okamura / Qingshun Lin / Machie Sakuma / Eiki Kawahara / Isato Yamazaki / Tomomi Uchikubo-Kamo / Yuri Tomabechi / Kazuharu Hanada / Tamao Hisano / Saya Moriyama / Yoshimasa Takahashi / Mutsumi Ito / Masaki Imai / Tadashi Maemura / Yuri Furusawa / Seiya Yamayoshi / Yoshihiro Kawaoka / Mikako Shirouzu / Makoto Ishii / Hideyuki Saya / Yasushi Kondo / Yuko Kaneko / Katsuya Suzuki / Koichi Fukunaga / Tsutomu Takeuchi / /
PubMed AbstractSeveral 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 ...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.
External linksiScience / PubMed:37288342 / PubMed Central
MethodsEM (single particle)
Resolution3.3 - 4.4 Å
Structure data

33065

7x93

EMDB-33065, PDB-7x93:
The SARS-CoV-2 receptor binding domain bound with the Fab fragment of a human neutralizing antibody Ab765
Method: EM (single particle) / Resolution: 3.3 Å

33066

7x94

EMDB-33066, PDB-7x94:
The SARS-CoV-2 receptor binding domain bound with the Fab fragment of a human neutralizing antibody Ab712
Method: EM (single particle) / Resolution: 4.0 Å

33067

7x95

EMDB-33067, PDB-7x95:
The SARS-CoV-2 receptor binding domain bound with the Fab fragment of a human neutralizing antibody Ab709
Method: EM (single particle) / Resolution: 3.9 Å

33068

7x96

EMDB-33068, PDB-7x96:
The SARS-CoV-2 receptor binding domain bound with the Fab fragment of a human neutralizing antibody Ab847
Method: EM (single particle) / Resolution: 3.4 Å

33643

7y6l

EMDB-33643, PDB-7y6l:
The SARS-CoV-2 receptor binding domain bound with the Fab fragment of a human neutralizing antibody Ab816
Method: EM (single particle) / Resolution: 3.5 Å

33644

7y6n

EMDB-33644, PDB-7y6n:
The SARS-CoV-2 receptor binding domain bound with the Fab fragment of a human neutralizing antibody Ab803
Method: EM (single particle) / Resolution: 4.4 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose / N-Acetylglucosamine

Source
  • homo sapiens (human)
  • severe acute respiratory syndrome coronavirus 2
KeywordsVIRAL PROTEIN / severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2) spike trimer / COVID-19 / human neutralizing antibody / RBD

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