Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Structures of Omicron spike complexes and implications for neutralizing antibody development.
Journal, issue, pages	Cell Rep, Vol. 39, Issue 5, Page 110770, Year 2022
Publish date	May 3, 2022
Authors	Hangtian Guo / Yan Gao / Tinghan Li / Tingting Li / Yuchi Lu / Le Zheng / Yue Liu / Tingting Yang / Feiyang Luo / Shuyi Song / Wei Wang / Xiuna Yang / Henry C Nguyen / Hongkai Zhang / Ailong Huang / Aishun Jin / Haitao Yang / Zihe Rao / Xiaoyun Ji /
PubMed Abstract	The emergence of the SARS-CoV-2 Omicron variant is dominant in many countries worldwide. The high number of spike mutations is responsible for the broad immune evasion from existing vaccines and ...The emergence of the SARS-CoV-2 Omicron variant is dominant in many countries worldwide. The high number of spike mutations is responsible for the broad immune evasion from existing vaccines and antibody drugs. To understand this, we first present the cryo-electron microscopy structure of ACE2-bound SARS-CoV-2 Omicron spike. Comparison to previous spike antibody structures explains how Omicron escapes these therapeutics. Secondly, we report structures of Omicron, Delta, and wild-type spikes bound to a patient-derived Fab antibody fragment (510A5), which provides direct evidence where antibody binding is greatly attenuated by the Omicron mutations, freeing spike to bind ACE2. Together with biochemical binding and 510A5 neutralization assays, our work establishes principles of binding required for neutralization and clearly illustrates how the mutations lead to antibody evasion yet retain strong ACE2 interactions. Structural information on spike with both bound and unbound antibodies collectively elucidates potential strategies for generation of therapeutic antibodies.
External links	Cell Rep / PubMed:35477022 / PubMed Central
Methods	EM (single particle)
Resolution	2.9 - 3.8 Å
Structure data	32739 7ws0 EMDB-32739, PDB-7ws0: Structures of Omicron Spike complexes illuminate broad-spectrum neutralizing antibody development Method: EM (single particle) / Resolution: 3.2 Å 32740 7ws1 EMDB-32740, PDB-7ws1: Structures of Omicron Spike complexes illuminate broad-spectrum neutralizing antibody development Method: EM (single particle) / Resolution: 3.4 Å 32741 7ws2 EMDB-32741, PDB-7ws2: Structures of Omicron Spike complexes illuminate broad-spectrum neutralizing antibody development Method: EM (single particle) / Resolution: 3.3 Å 32742 7ws3 EMDB-32742, PDB-7ws3: Structures of Omicron Spike complexes illuminate broad-spectrum neutralizing antibody development Method: EM (single particle) / Resolution: 3.6 Å 32743 7ws4 EMDB-32743, PDB-7ws4: Ultrapotent SARS-CoV-2 neutralizing antibodies with protective efficacy against newly emerged mutational variants Method: EM (single particle) / Resolution: 3.7 Å 32744 7ws5 EMDB-32744, PDB-7ws5: Structures of Omicron Spike complexes illuminate broad-spectrum neutralizing antibody development Method: EM (single particle) / Resolution: 3.7 Å 32748 7ws6 EMDB-32748, PDB-7ws6: Structures of Omicron Spike complexes illuminate broad-spectrum neutralizing antibody development Method: EM (single particle) / Resolution: 3.8 Å 32749 7ws7 EMDB-32749, PDB-7ws7: Structures of Omicron Spike complexes illuminate broad-spectrum neutralizing antibody development Method: EM (single particle) / Resolution: 3.4 Å 32750 7ws8 EMDB-32750, PDB-7ws8: Structures of Omicron Spike complexes illuminate broad-spectrum neutralizing antibody development Method: EM (single particle) / Resolution: 3.0 Å 32751 7ws9 EMDB-32751, PDB-7ws9: Structures of Omicron Spike complexes illuminate broad-spectrum neutralizing antibody development Method: EM (single particle) / Resolution: 2.9 Å 32752 7wsa EMDB-32752, PDB-7wsa: Structures of Omicron Spike complexes illuminate broad-spectrum neutralizing antibody development Method: EM (single particle) / Resolution: 3.0 Å
Chemicals	ChemComp-NAG: 2-acetamido-2-deoxy-beta-D-glucopyranose / N-Acetylglucosamine
Source	severe acute respiratory syndrome coronavirus 2 homo sapiens (human)
Keywords	VIRAL PROTEIN/IMMUNE SYSTEM / COVID-19 / spike glycoprotein / virus / VIRAL PROTEIN / antibody / VIRAL PROTEIN-IMMUNE SYSTEM complex / VIRAL PROTEIN/HYDROLASE / VIRAL PROTEIN-HYDROLASE complex