2021年6月24日
An infectivity-enhancing site on the SARS-CoV-2 spike protein targeted by antibodies
Cell
- 巻
- 184
- 号
- 13
- 開始ページ
- 3452
- 終了ページ
- 3.47E+21
- 記述言語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1016/j.cell.2021.05.032
Antibodies against the receptor-binding domain (RBD) of the SARS-CoV-2 spike protein prevent SARS-CoV-2 infection. However, the effects of antibodies against other spike protein domains are largely unknown. Here, we screened a series of anti-spike monoclonal antibodies from coronavirus disease 2019 (COVID-19) patients and found that some of antibodies against the N-terminal domain (NTD) induced the open conformation of RBD and thus enhanced the binding capacity of the spike protein to ACE2 and infectivity of SARS-CoV-2. Mutational analysis revealed that all of the infectivity-enhancing antibodies recognized a specific site on the NTD. Structural analysis demonstrated that all infectivity-enhancing antibodies bound to NTD in a similar manner. The antibodies against this infectivity-enhancing site were detected at high levels in severe patients. Moreover, we identified antibodies against the infectivity-enhancing site in uninfected donors, albeit at a lower frequency. These findings demonstrate that not only neutralizing antibodies but also enhancing antibodies are produced during SARS-CoV-2 infection.
- リンク情報
-
- DOI
- https://doi.org/10.1016/j.cell.2021.05.032
- PubMed
- https://www.ncbi.nlm.nih.gov/pubmed/34139176
- Scopus
- https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=85108345821&origin=inward 本文へのリンクあり
- Scopus Citedby
- https://www.scopus.com/inward/citedby.uri?partnerID=HzOxMe3b&scp=85108345821&origin=inward
- ID情報
-
- DOI : 10.1016/j.cell.2021.05.032
- ISSN : 0092-8674
- eISSN : 1097-4172
- PubMed ID : 34139176
- SCOPUS ID : 85108345821