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Now, in new research posted to the preprint server bioRxiv*, scientists use an experimental structure of the Spike RBD domain co-crystallized with part of the ACE2 receptor and several in silico methods to analyze the possible impacts of three amino acid replacements (Spike K417N, E484K, N501Y) concerning ACE2 binding.
Using more than 100,000 virus genome sequences uploaded in the GISAID database, researchers found around 9,000 mutations in the virus spike protein RBD.
A recent study by US researchers shows how the 501Y.V2 variant of the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), characterized by several mutations, is able to escape neutralization by present first-wave anti-SARS-CoV-2 antibodies and potentially re-infect COVID-19 convalescent individuals.
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One such strain is the South African 501.V2 and UK B1.1.7 strains, which have been isolated from many countries and seem to spread faster than the ancestral strain. A preprint that recently appeared on the bioRxiv server reports the computational structure of this strain and the possible effect of the mutations on infectivity and neutralization.
A recent study has found that extracellular vimentin can bind to SARS-CoV-2 spike protein in vitro, and antibodies against vimentin can decrease virus infectivity by up to 80%. This suggests vimentin could aid the virus’s binding to host cells and help in infection.