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TitleStructural insights in cell-type specific evolution of intra-host diversity by SARS-CoV-2.
Journal, issue, pagesNat Commun, Vol. 13, Issue 1, Page 222, Year 2022
Publish dateJan 11, 2022
AuthorsKapil Gupta / Christine Toelzer / Maia Kavanagh Williamson / Deborah K Shoemark / A Sofia F Oliveira / David A Matthews / Abdulaziz Almuqrin / Oskar Staufer / Sathish K N Yadav / Ufuk Borucu / Frederic Garzoni / Daniel Fitzgerald / Joachim Spatz / Adrian J Mulholland / Andrew D Davidson / Christiane Schaffitzel / Imre Berger /
PubMed AbstractAs the global burden of SARS-CoV-2 infections escalates, so does the evolution of viral variants with increased transmissibility and pathology. In addition to this entrenched diversity, RNA viruses ...As the global burden of SARS-CoV-2 infections escalates, so does the evolution of viral variants with increased transmissibility and pathology. In addition to this entrenched diversity, RNA viruses can also display genetic diversity within single infected hosts with co-existing viral variants evolving differently in distinct cell types. The BriSΔ variant, originally identified as a viral subpopulation from SARS-CoV-2 isolate hCoV-19/England/02/2020, comprises in the spike an eight amino-acid deletion encompassing a furin recognition motif and S1/S2 cleavage site. We elucidate the structure, function and molecular dynamics of this spike providing mechanistic insight into how the deletion correlates to viral cell tropism, ACE2 receptor binding and infectivity of this SARS-CoV-2 variant. Our results reveal long-range allosteric communication between functional domains that differ in the wild-type and the deletion variant and support a view of SARS-CoV-2 probing multiple evolutionary trajectories in distinct cell types within the same infected host.
External linksNat Commun / PubMed:35017512 / PubMed Central
MethodsEM (single particle)
Resolution2.8 - 3.03 Å
Structure data

12818

7od3

EMDB-12818, PDB-7od3:
SARS CoV-2 Spike protein, Bristol UK Deletion variant, Closed conformation, C3 symmetry
Method: EM (single particle) / Resolution: 2.8 Å

12842

7odl

EMDB-12842, PDB-7odl:
SARS CoV-2 Spike protein, Bristol UK Deletion variant, Closed conformation, C1 symmetry
Method: EM (single particle) / Resolution: 3.03 Å

Chemicals

ChemComp-EIC:
LINOLEIC ACID / Linoleic acid

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose / N-Acetylglucosamine

Source
  • severe acute respiratory syndrome coronavirus 2
KeywordsVIRAL PROTEIN / SARS-Cov2 / COVID / Linoleic Acid / Spike

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