An infectivity-enhancing site on the SARS-CoV-2 spike protein targeted by antibodies

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...

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Published in	Cell Vol. 184; no. 13; pp. 3452 - 3466.e18
Main Authors	Liu, Yafei, Soh, Wai Tuck, Kishikawa, Jun-ichi, Hirose, Mika, Nakayama, Emi E., Li, Songling, Sasai, Miwa, Suzuki, Tatsuya, Tada, Asa, Arakawa, Akemi, Matsuoka, Sumiko, Akamatsu, Kanako, Matsuda, Makoto, Ono, Chikako, Torii, Shiho, Kishida, Kazuki, Jin, Hui, Nakai, Wataru, Arase, Noriko, Nakagawa, Atsushi, Matsumoto, Maki, Nakazaki, Yukoh, Shindo, Yasuhiro, Kohyama, Masako, Tomii, Keisuke, Ohmura, Koichiro, Ohshima, Shiro, Okamoto, Toru, Yamamoto, Masahiro, Nakagami, Hironori, Matsuura, Yoshiharu, Kato, Takayuki, Okada, Masato, Standley, Daron M., Shioda, Tatsuo, Arase, Hisashi
Format	Journal Article
Language	English
Published	United States Elsevier Inc 24.06.2021
Subjects	ADE angiotensin converting enzyme 2 Animals Antibodies, Monoclonal - immunology Antibodies, Neutralizing - immunology Antibodies, Viral - immunology antibody-dependent enhancement Cell Line Chlorocebus aethiops COVID-19 - immunology COVID-19 infection cryo-electron microscopy cryo-EM docking model HEK293 Cells Humans mutational analysis pathogenicity Protein Binding - immunology Protein Domains - immunology SARS-CoV-2 - immunology Severe acute respiratory syndrome coronavirus 2 Spike Glycoprotein, Coronavirus - genetics Spike Glycoprotein, Coronavirus - immunology Vero Cells ADE docking model antibody-dependent enhancement angiotensin converting enzyme 2 cryo-EM cryo-electron microscopy
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Abstract	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. [Display omitted] •SARS-CoV-2 infectivity is enhanced by specific antibodies independent of the Fc receptor•The open RBD state is induced upon antibody binding to a specific site on the NTD•Divalent bridging of spikes is required to induce the RBD-up state•Infectivity-enhancing antibodies are detected in severe COVID-19 patients A subset of antibodies detected in patients with severe COVID-19 target a specific region of the N-terminal domain of the spike protein and enhance binding of the virus to the ACE2 receptor.
AbstractList	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. [Display omitted] •SARS-CoV-2 infectivity is enhanced by specific antibodies independent of the Fc receptor•The open RBD state is induced upon antibody binding to a specific site on the NTD•Divalent bridging of spikes is required to induce the RBD-up state•Infectivity-enhancing antibodies are detected in severe COVID-19 patients A subset of antibodies detected in patients with severe COVID-19 target a specific region of the N-terminal domain of the spike protein and enhance binding of the virus to the ACE2 receptor. 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. 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. A subset of antibodies detected in patients with severe COVID-19 target a specific region of the N-terminal domain of the spike protein and enhance binding of the virus to the ACE2 receptor. 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.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.
Author	Matsuoka, Sumiko Matsumoto, Maki Akamatsu, Kanako Nakayama, Emi E. Arakawa, Akemi Kishikawa, Jun-ichi Kishida, Kazuki Standley, Daron M. Sasai, Miwa Shioda, Tatsuo Soh, Wai Tuck Nakai, Wataru Li, Songling Matsuura, Yoshiharu Arase, Noriko Matsuda, Makoto Ohmura, Koichiro Tada, Asa Ohshima, Shiro Arase, Hisashi Suzuki, Tatsuya Hirose, Mika Nakagami, Hironori Nakazaki, Yukoh Yamamoto, Masahiro Jin, Hui Ono, Chikako Shindo, Yasuhiro Okamoto, Toru Okada, Masato Torii, Shiho Nakagawa, Atsushi Kohyama, Masako Kato, Takayuki Tomii, Keisuke Liu, Yafei
Author_xml	– sequence: 1 givenname: Yafei surname: Liu fullname: Liu, Yafei organization: Department of Immunochemistry, Research Institute for Microbial Diseases, Osaka University, Osaka 565-0871, Japan – sequence: 2 givenname: Wai Tuck surname: Soh fullname: Soh, Wai Tuck organization: Laboratory of Immunochemistry, World Premier International Immunology Frontier Research Centre, Osaka University, Osaka 565-0871, Japan – sequence: 3 givenname: Jun-ichi surname: Kishikawa fullname: Kishikawa, Jun-ichi organization: Laboratory for CryoEM Structural Biology, Institute for Protein Research, Osaka University, Osaka 565-0871, Japan – sequence: 4 givenname: Mika surname: Hirose fullname: Hirose, Mika organization: Laboratory for CryoEM Structural Biology, Institute for Protein Research, Osaka University, Osaka 565-0871, Japan – sequence: 5 givenname: Emi E. surname: Nakayama fullname: Nakayama, Emi E. organization: Department of Viral Infections, Research Institute for Microbial Diseases, Osaka University, Osaka 565-0871, Japan – sequence: 6 givenname: Songling surname: Li fullname: Li, Songling organization: Department of Genome Informatics, Research Institute for Microbial Diseases, Osaka University, Osaka 565-0871, Japan – sequence: 7 givenname: Miwa surname: Sasai fullname: Sasai, Miwa organization: Department of Immunoparasitology, Research Institute for Microbial Diseases, Osaka University, Osaka 565-0871, Japan – sequence: 8 givenname: Tatsuya surname: Suzuki fullname: Suzuki, Tatsuya organization: Institute for Advanced Co-Creation Studies, Research Institute for Microbial Diseases, Osaka University, Osaka 565-0871, Japan – sequence: 9 givenname: Asa surname: Tada fullname: Tada, Asa organization: Laboratory of Immunochemistry, World Premier International Immunology Frontier Research Centre, Osaka University, Osaka 565-0871, Japan – sequence: 10 givenname: Akemi surname: Arakawa fullname: Arakawa, Akemi organization: Laboratory of Immunochemistry, World Premier 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Virus Control, Research Institute for Microbial Diseases, Osaka University, Osaka 565-0871, Japan – sequence: 16 givenname: Kazuki surname: Kishida fullname: Kishida, Kazuki organization: Laboratory of Immunochemistry, World Premier International Immunology Frontier Research Centre, Osaka University, Osaka 565-0871, Japan – sequence: 17 givenname: Hui surname: Jin fullname: Jin, Hui organization: Department of Immunochemistry, Research Institute for Microbial Diseases, Osaka University, Osaka 565-0871, Japan – sequence: 18 givenname: Wataru surname: Nakai fullname: Nakai, Wataru organization: Department of Immunochemistry, Research Institute for Microbial Diseases, Osaka University, Osaka 565-0871, Japan – sequence: 19 givenname: Noriko surname: Arase fullname: Arase, Noriko organization: Department of Dermatology, Graduate school of Medicine, Osaka University, Osaka 565-0871, Japan – sequence: 20 givenname: Atsushi surname: Nakagawa fullname: Nakagawa, Atsushi organization: Department of Respiratory Medicine, Kobe City Medical Center General Hospital, Hyogo 650-0047, Japan – sequence: 21 givenname: Maki surname: Matsumoto fullname: Matsumoto, Maki organization: Drug Discovery Research Center, HuLA immune, Inc., Osaka 565-0871, Japan – sequence: 22 givenname: Yukoh surname: Nakazaki fullname: Nakazaki, Yukoh organization: Drug Discovery Research Center, HuLA immune, Inc., Osaka 565-0871, Japan – sequence: 23 givenname: Yasuhiro surname: Shindo fullname: Shindo, Yasuhiro organization: Drug Discovery Research Center, HuLA immune, Inc., Osaka 565-0871, Japan – sequence: 24 givenname: Masako surname: Kohyama fullname: Kohyama, Masako organization: Department of Immunochemistry, Research Institute for Microbial Diseases, Osaka University, Osaka 565-0871, Japan – sequence: 25 givenname: Keisuke surname: Tomii fullname: Tomii, Keisuke organization: Department of Respiratory Medicine, Kobe City Medical Center General Hospital, Hyogo 650-0047, Japan – sequence: 26 givenname: 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givenname: Yoshiharu surname: Matsuura fullname: Matsuura, Yoshiharu organization: Laboratory of Virus Control, Research Institute for Microbial Diseases, Osaka University, Osaka 565-0871, Japan – sequence: 32 givenname: Atsushi surname: Nakagawa fullname: Nakagawa, Atsushi organization: Laboratory for Supramolecular Crystallography, Institute for Protein Research, Osaka University, Osaka 565-0871, Japan – sequence: 33 givenname: Takayuki surname: Kato fullname: Kato, Takayuki organization: Laboratory for CryoEM Structural Biology, Institute for Protein Research, Osaka University, Osaka 565-0871, Japan – sequence: 34 givenname: Masato surname: Okada fullname: Okada, Masato organization: Department Oncogene Research, Research Institute for Microbial Diseases, Osaka University, Osaka 565-0871, Japan – sequence: 35 givenname: Daron M. surname: Standley fullname: Standley, Daron M. organization: Department of Genome Informatics, Research Institute for Microbial Diseases, Osaka University, 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BackLink	https://www.ncbi.nlm.nih.gov/pubmed/34139176$$D View this record in MEDLINE/PubMed
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Snippet	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...
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SubjectTerms	ADE angiotensin converting enzyme 2 Animals Antibodies, Monoclonal - immunology Antibodies, Neutralizing - immunology Antibodies, Viral - immunology antibody-dependent enhancement Cell Line Chlorocebus aethiops COVID-19 - immunology COVID-19 infection cryo-electron microscopy cryo-EM docking model HEK293 Cells Humans mutational analysis pathogenicity Protein Binding - immunology Protein Domains - immunology SARS-CoV-2 - immunology Severe acute respiratory syndrome coronavirus 2 Spike Glycoprotein, Coronavirus - genetics Spike Glycoprotein, Coronavirus - immunology Vero Cells
Title	An infectivity-enhancing site on the SARS-CoV-2 spike protein targeted by antibodies
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