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-Structure paper
Title | Structural and functional analysis of an inter-Spike bivalent neutralizing antibody against SARS-CoV-2 variants. |
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Journal, issue, pages | iScience, Vol. 25, Issue 6, Page 104431, Year 2022 |
Publish date | Jun 17, 2022 |
Authors | Yaning Li / Qing Fan / Bing Zhou / Yaping Shen / Yuanyuan Zhang / Lin Cheng / Furong Qi / Shuo Song / Yingying Guo / Renhong Yan / Bin Ju / Zheng Zhang / |
PubMed Abstract | The different variants of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) have attracted most public concern because they caused "wave and wave" COVID-19 pandemic. The initial step of ...The different variants of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) have attracted most public concern because they caused "wave and wave" COVID-19 pandemic. The initial step of viral infection is mediated by the SARS-CoV-2 Spike (S) protein, which mediates the receptor recognition and membrane fusion between virus and host cells. Neutralizing antibodies (nAbs) targeting the S protein of SARS-CoV-2 have become promising candidates for clinical intervention strategy, while multiple studies have shown that different variants have enhanced infectivity and antibody resistance. Here, we explore the structure and function of STS165, a broadly inter-Spike bivalent nAb against SARS-CoV-2 variants and even SARS-CoV, contributing to further understanding of the working mechanism of nAbs. |
External links | iScience / PubMed:35607524 / PubMed Central |
Methods | EM (single particle) |
Resolution | 3.3 - 3.8 Å |
Structure data | EMDB-33202, PDB-7xic: EMDB-33203, PDB-7xid: EMDB-33204: S-ECD (Omicron) in complex with PD of ACE2 focused on RBD_PD sub-complex |
Chemicals | ChemComp-NAG: |
Source |
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Keywords | VIRAL PROTEIN/IMMUNE SYSTEM / SARS-Cov-2 / VIRAL PROTEIN / VIRAL PROTEIN-IMMUNE SYSTEM complex / VIRAL PROTEIN/HYDROLASE / VIRAL PROTEIN-HYDROLASE complex |