Binding of SARS‐CoV‐2 to Cell Receptors: A Tale of Molecular Evolution

The magnified infectious power of the SARS‐CoV‐2 virus compared to its precursor SARS‐CoV is intimately linked to an enhanced ability in the mutated virus to find available hydrogen‐bond sites in the host cells. This characteristic is acquired during virus evolution because of the selective pressure exerted at the molecular level. We pinpoint the specific residue (in the virus) to residue (in the cell) contacts during the initial recognition and binding and show that the virus⋅⋅⋅cell interaction is mainly due to an extensive network of hydrogen bonds and to a large surface of noncovalent interactions. In addition to the formal quantum characterization of bonding interactions, computation of absorption spectra for the specific virus⋅⋅⋅cell interacting residues yields significant shifts of Δλmax=47 and 66 nm in the wavelength for maximum absorption in the complex with respect to the isolated host and virus, respectively. All together, now: Explicit virus cell interactions are seen between the spike protein and the proteins in the host cell. The collective action of a multitude of weak interactions stabilizes the initial virus cell contact. SARS‐COV to SARS‐COV‐2 mutations are driven by an evolution pressure that leads to enhanced hydrogen bonding.