Mar 31, 2020

Re-insights into origin and adaptation of SARS-CoV-2

BioRxiv : the Preprint Server for Biology
Sebastian MatuszewskiCarla N Mavian


Understanding the molecular features that made SARS-CoV-2 a highly infectious virus is crucial for the development of targeted therapies and an effective vaccine. Following the recent report of a furin-like cleavage site1, unique to SARS-CoV-2, we characterized several additional residues positioned within the crown of the S glycoprotein under positive/diversifying selection along the ancestral lineage of current pandemic strains. Residue V483 in near proximity to the ACE2 binding domain, which may indeed affect the enhanced ability of currently circulating strains to infect host cells. Molecular dynamic simulations revealed long-range covariant movements with furin cleavage, correlated with pre-fusion conformation of SARS-CoV-2 S glycoprotein monomer. Residue T333 is hinge of this movement that gives further advantage to bind cell receptors facilitating fusion and entry. Evolutionary analysis revealed that current lineage is likely to have emerged from the reservoir after a recombination event between bat and pangolin ancestors. Recombination impacted residues located in the binding receptor region of S glycoprotein that are identical to pangolin ancestor. Interestingly, several recombination hotspots were detected throughout ...Continue Reading

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Sample Fixation
Anatomical Space Structure
Standing Position

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