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7QDG

SARS-CoV-2 S protein S:A222V + S:D614G mutant 1-up

Summary for 7QDG
Entry DOI10.2210/pdb7qdg/pdb
EMDB information13916
DescriptorSpike glycoprotein,Fibritin, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-alpha-D-glucopyranose, ... (4 entities in total)
Functional Keywordssars-cov-2, s protein, s:a222v + s:d614g mutant, viral protein
Biological sourceSevere acute respiratory syndrome coronavirus 2
More
Total number of polymer chains3
Total formula weight426990.81
Authors
Primary citationGinex, T.,Marco-Marin, C.,Wieczor, M.,Mata, C.P.,Krieger, J.,Ruiz-Rodriguez, P.,Lopez-Redondo, M.L.,Frances-Gomez, C.,Melero, R.,Sanchez-Sorzano, C.O.,Martinez, M.,Gougeard, N.,Forcada-Nadal, A.,Zamora-Caballero, S.,Gozalbo-Rovira, R.,Sanz-Frasquet, C.,Arranz, R.,Bravo, J.,Rubio, V.,Marina, A.,Geller, R.,Comas, I.,Gil, C.,Coscolla, M.,Orozco, M.,Llacer, J.L.,Carazo, J.M.
The structural role of SARS-CoV-2 genetic background in the emergence and success of spike mutations: The case of the spike A222V mutation.
Plos Pathog., 18:e1010631-e1010631, 2022
Cited by
PubMed Abstract: The S:A222V point mutation, within the G clade, was characteristic of the 20E (EU1) SARS-CoV-2 variant identified in Spain in early summer 2020. This mutation has since reappeared in the Delta subvariant AY.4.2, raising questions about its specific effect on viral infection. We report combined serological, functional, structural and computational studies characterizing the impact of this mutation. Our results reveal that S:A222V promotes an increased RBD opening and slightly increases ACE2 binding as compared to the parent S:D614G clade. Finally, S:A222V does not reduce sera neutralization capacity, suggesting it does not affect vaccine effectiveness.
PubMed: 35816514
DOI: 10.1371/journal.ppat.1010631
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.4 Å)
Structure validation

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