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	Structural basis for broad coronavirus neutralization.
Journal, issue, pages	Nat Struct Mol Biol, Vol. 28, Issue 6, Page 478-486, Year 2021
Publish date	May 12, 2021
Authors	Maximilian M Sauer / M Alejandra Tortorici / Young-Jun Park / Alexandra C Walls / Leah Homad / Oliver J Acton / John E Bowen / Chunyan Wang / Xiaoli Xiong / Willem de van der Schueren / Joel Quispe / Benjamin G Hoffstrom / Berend-Jan Bosch / Andrew T McGuire / David Veesler /
PubMed Abstract	Three highly pathogenic β-coronaviruses have crossed the animal-to-human species barrier in the past two decades: SARS-CoV, MERS-CoV and SARS-CoV-2. To evaluate the possibility of identifying ...Three highly pathogenic β-coronaviruses have crossed the animal-to-human species barrier in the past two decades: SARS-CoV, MERS-CoV and SARS-CoV-2. To evaluate the possibility of identifying antibodies with broad neutralizing activity, we isolated a monoclonal antibody, termed B6, that cross-reacts with eight β-coronavirus spike glycoproteins, including all five human-infecting β-coronaviruses. B6 broadly neutralizes entry of pseudotyped viruses from lineages A and C, but not from lineage B, and the latter includes SARS-CoV and SARS-CoV-2. Cryo-EM, X-ray crystallography and membrane fusion assays reveal that B6 binds to a conserved cryptic epitope located in the fusion machinery. The data indicate that antibody binding sterically interferes with the spike conformational changes leading to membrane fusion. Our data provide a structural framework explaining B6 cross-reactivity with β-coronaviruses from three lineages, along with a proof of concept for antibody-mediated broad coronavirus neutralization elicited through vaccination. This study unveils an unexpected target for next-generation structure-guided design of a pan-β-coronavirus vaccine.
External links	Nat Struct Mol Biol / PubMed:33981021
Methods	EM (single particle) / X-ray diffraction
Resolution	1.4 - 4.7 Å
Structure data	EMDB-23672: Structural basis for broad coronavirus neutralization Method: EM (single particle) / Resolution: 4.7 Å 23674 7m5e EMDB-23674, PDB-7m5e: MERS-CoV S bound to the broadly neutralizing B6 Fab fragment (C3 refinement) Method: EM (single particle) / Resolution: 2.5 Å PDB-7m51: B6 Fab fragment bound to the OC43 spike stem helix peptide Method: X-RAY DIFFRACTION / Resolution: 1.8 Å PDB-7m52: B6 Fab fragment bound to the HKU4 spike stem helix peptide Method: X-RAY DIFFRACTION / Resolution: 1.5 Å PDB-7m53: B6 Fab fragment bound to the SARS-CoV/SARS-CoV-2 spike stem helix peptide Method: X-RAY DIFFRACTION / Resolution: 1.4 Å PDB-7m55: B6 Fab fragment bound to the MERS-CoV spike stem helix peptide Method: X-RAY DIFFRACTION / Resolution: 1.4 Å
Chemicals	ChemComp-GOL: GLYCEROL ChemComp-HOH: WATER ChemComp-FOL: FOLIC ACID ChemComp-NAG: 2-acetamido-2-deoxy-beta-D-glucopyranose ChemComp-SIA: N-acetyl-alpha-neuraminic acid
Source	middle east respiratory syndrome-related coronavirus mus musculus (house mouse) human coronavirus oc43 bat coronavirus hku4 severe acute respiratory syndrome coronavirus 2
Keywords	ANTIVIRAL PROTEIN / IMMUNE SYSTEM / Broadly neutralizing antibody / Structural genomics / SSGCID / Seattle Structural Genomics Center for Infectious Disease / Center for Structural Genomics of Infectious Diseases / CSGID / VIRAL PROTEIN / MERS-CoV / coronaviruses / antibody