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	D614G mutation in the SARS-CoV-2 spike protein enhances viral fitness by desensitizing it to temperature-dependent denaturation.
Journal, issue, pages	J Biol Chem, Vol. 297, Issue 4, Page 101238, Year 2021
Publish date	Sep 24, 2021
Authors	Tzu-Jing Yang / Pei-Yu Yu / Yuan-Chih Chang / Shang-Te Danny Hsu /
PubMed Abstract	The D614G mutation in the spike protein of SARS-CoV-2 alters the fitness of the virus, leading to the dominant form observed in the COVID-19 pandemic. However, the molecular basis of the mechanism by ...The D614G mutation in the spike protein of SARS-CoV-2 alters the fitness of the virus, leading to the dominant form observed in the COVID-19 pandemic. However, the molecular basis of the mechanism by which this mutation enhances fitness is not clear. Here we demonstrated by cryo-electron microscopy that the D614G mutation resulted in increased propensity of multiple receptor-binding domains (RBDs) in an upward conformation poised for host receptor binding. Multiple substates within the one RBD-up or two RBD-up conformational space were determined. According to negative staining electron microscopy, differential scanning calorimetry, and differential scanning fluorimetry, the most significant impact of the mutation lies in its ability to eliminate the unusual cold-induced unfolding characteristics and to significantly increase the thermal stability under physiological pH. The D614G spike variant also exhibited exceptional long-term stability when stored at 37 °C for up to 2 months. Our findings shed light on how the D614G mutation enhances the infectivity of SARS-CoV-2 through a stabilizing mutation and suggest an approach for better design of spike protein-based conjugates for vaccine development.
External links	J Biol Chem / PubMed:34563540 / PubMed Central
Methods	EM (single particle)
Resolution	3.4 - 3.6 Å
Structure data	31047 7eaz EMDB-31047, PDB-7eaz: Cryo-EM structure of SARS-CoV-2 Spike D614G variant, one RBD-up conformation 1 Method: EM (single particle) / Resolution: 3.5 Å 31048 7eb0 EMDB-31048, PDB-7eb0: Cryo-EM structure of SARS-CoV-2 Spike D614G variant, one RBD-up conformation 2 Method: EM (single particle) / Resolution: 3.6 Å 31050 7eb3 EMDB-31050, PDB-7eb3: Cryo-EM structure of SARS-CoV-2 Spike D614G variant, one RBD-up conformation 3 Method: EM (single particle) / Resolution: 3.6 Å 31051 7eb4 EMDB-31051, PDB-7eb4: Cryo-EM structure of SARS-CoV-2 Spike D614G variant, two RBD-up conformation 1 Method: EM (single particle) / Resolution: 3.5 Å 31052 7eb5 EMDB-31052, PDB-7eb5: Cryo-EM structure of SARS-CoV-2 Spike D614G variant, two RBD-up conformation 2 Method: EM (single particle) / Resolution: 3.4 Å
Chemicals	ChemComp-NAG: 2-acetamido-2-deoxy-beta-D-glucopyranose
Source	severe acute respiratory syndrome coronavirus 2
Keywords	VIRAL PROTEIN / SARS-CoV-2 / Spike protein