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| COVID-19 coronavirus spike protein Credit: Alexandra C. Walls, Young-Jun Park, David Veesler Source: University of Washington Medicine News |
Followers of Creationism's putative intelligent [sic] designer must be awestruck by the sheer brilliance of its latest weapon of mass destruction - the modified coronavirus, SARS-CoV-2, that causes Covid-19. According to Johns Hopkins University, to date, this virus has infected 20,318,420 people world-wide and killed 742,048. In the USA, it has infected 5,141,879 and killed 164,545. The world-wide pandemic has caused economies to collapsed and major business to be ruined as governments impose lockdowns in a desperate battle to slow its spread.
Now, two research scientists from Northwestern University, Illinois, USA, have shown just how thorough this putative designer would have to have been to make the virus the 'success' it is. They have shown that the virus 'spike' proteins have a positively charged are just a few nanometers away from the actual binding site with which the virus binds to the protein ACE2, on the cell surface, fitting into it like a key into a lock. This forms a strong electrostatic bond with a negative area on the ACE2 protein, so helping the virus bind to the cell and prise open an entrance for it to inject its RNA contents into the cell.
They published their findings in the American Chemical Society's journal ACS Nano:
Polybasic Cleavage Sites Abstract
The receptor-binding domain (RBD) of the SARS-CoV-2 spike protein plays a crucial role in binding the human cell receptor ACE2 that is required for viral entry. Many studies have been conducted to target the structures of RBD–ACE2 binding and to design RBD-targeting vaccines and drugs. Nevertheless, mutations distal from the SARS-CoV-2 RBD also impact its transmissibility and antibody can target non-RBD regions, suggesting the incomplete role of the RBD region in the spike protein–ACE2 binding. Here, in order to elucidate distant binding mechanisms, we analyze complexes of ACE2 with the wild-type spike protein and with key mutants via large-scale all-atom explicit solvent molecular dynamics simulations. We find that though distributed approximately 10 nm away from the RBD, the SARS-CoV-2 polybasic cleavage sites enhance, via electrostatic interactions and hydration, the RBD–ACE2 binding affinity. A negatively charged tetrapeptide (GluGluLeuGlu) is then designed to neutralize the positively charged arginine on the polybasic cleavage sites. We find that the tetrapeptide GluGluLeuGlu binds to one of the three polybasic cleavage sites of the SARS-CoV-2 spike protein lessening by 34% the RBD–ACE2 binding strength. This significant binding energy reduction demonstrates the feasibility to neutralize RBD–ACE2 binding by targeting this specific polybasic cleavage site. Our work enhances understanding of the binding mechanism of SARS-CoV-2 to ACE2, which may aid the design of therapeutics for COVID-19 infection.
This is like a supply ship docking with the International Space Station by being drawn into position by powerful magnets that line the two up perfectly before opening the adjoining hatch.
Of course, this would have been such an advantage to any evolving virus that its evolution by natural selection is simple to understand, ad we have seen already how the unique immune system that bats have makes them ideal environments in which this evolutionary process is bound to take place. However, that explanation is dogmatically unavailable to ID proponents who are just left with malevolent intent as the reason their putative designer designed SARS-CoV-2.
This and many such problems for Creationists will be highlighted and discussed in my forthcoming book, "The Malevolent Designer: Why Nature's God is not Good".
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