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TitleStructural basis and mode of action for two broadly neutralizing antibodies against SARS-CoV-2 emerging variants of concern.
Journal, issue, pagesCell Rep, Vol. 38, Issue 2, Page 110210, Year 2022
Publish dateJan 11, 2022
AuthorsWenwei Li / Yaozong Chen / Jérémie Prévost / Irfan Ullah / Maolin Lu / Shang Yu Gong / Alexandra Tauzin / Romain Gasser / Dani Vézina / Sai Priya Anand / Guillaume Goyette / Debashree Chaterjee / Shilei Ding / William D Tolbert / Michael W Grunst / Yuxia Bo / Shijian Zhang / Jonathan Richard / Fei Zhou / Rick K Huang / Lothar Esser / Allison Zeher / Marceline Côté / Priti Kumar / Joseph Sodroski / Di Xia / Pradeep D Uchil / Marzena Pazgier / Andrés Finzi / Walther Mothes /
PubMed AbstractEmerging variants of concern for the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) can transmit more efficiently and partially evade protective immune responses, thus necessitating ...Emerging variants of concern for the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) can transmit more efficiently and partially evade protective immune responses, thus necessitating continued refinement of antibody therapies and immunogen design. Here, we elucidate the structural basis and mode of action for two potent SARS-CoV-2 spike (S)-neutralizing monoclonal antibodies, CV3-1 and CV3-25, which remain effective against emerging variants of concern in vitro and in vivo. CV3-1 binds to the (485-GFN-487) loop within the receptor-binding domain (RBD) in the "RBD-up" position and triggers potent shedding of the S1 subunit. In contrast, CV3-25 inhibits membrane fusion by binding to an epitope in the stem helix region of the S2 subunit that is highly conserved among β-coronaviruses. Thus, vaccine immunogen designs that incorporate the conserved regions in the RBD and stem helix region are candidates to elicit pan-coronavirus protective immune responses.
External linksCell Rep / PubMed:34971573 / PubMed Central
MethodsEM (single particle) / EM (subtomogram averaging) / X-ray diffraction
Resolution2.15 - 12.0 Å
Structure data

EMDB-25200: CryoEM structure of SARS-CoV-2 HexaPro spike in complex with S2-binding CV3-25
Method: EM (single particle) / Resolution: 3.49 Å

EMDB-25564:
Subtomogram averaging of SARS-CoV-2 Spike Protein bound to CV3-1
Method: EM (subtomogram averaging) / Resolution: 12.0 Å

EMDB-25565:
Subtomogram averaging of SARS-CoV-2 Spike Protein bound to Fab CV3-25
Method: EM (subtomogram averaging) / Resolution: 10.0 Å

EMDB-25566:
Subtomogram averaging of SARS-CoV-2 Spike Protein
Method: EM (subtomogram averaging) / Resolution: 10.0 Å

PDB-7nab:
Crystal structure of human neutralizing mAb CV3-25 binding to SARS-CoV-2 S MPER peptide 1140-1165
Method: X-RAY DIFFRACTION / Resolution: 2.15 Å

Chemicals

ChemComp-NA:
Unknown entry

ChemComp-CIT:
CITRIC ACID / Citric acid

ChemComp-HOH:
WATER / Water

Source
  • homo sapiens (human)
  • severe acute respiratory syndrome coronavirus 2
KeywordsVIRAL PROTEIN/IMMUNE SYSTEM / human neutralizing mAb / MPER-targeting / SARS-CoV-2 / spike / VIRAL PROTEIN-IMMUNE SYSTEM complex

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