The virus infects human lung cells through the binding of the SARS-CoV-2 S ‘spike’ protein to the trans-membrane receptor Angiotensin Converting Enzyme 2 (ACE2) expressed on the cells. SPR analysis (Biacore T200) was used to determine the affinity of the spike protein for human ACE2 receptor and to demonstrate partial blockade of the binding interaction by masking the spike protein with a non-membrane-bound form of ACE2.

fig 1.  Binding of recombinant SARS-CoV-2 S spike protein to biotinylated human ACE2 protein captured onto a streptavidin-coated sensor chip. The S protein was applied at 12.5 to 200 nM and gave a kinetic-derived affinity constant (Kd) of 35.6 nM.

fig 2. Binding of recombinant spike protein (20 nM) to surface-bound (streptavidin-captured) biotinylated ACE2 is attenuated by pre-incubation of the spike protein with a 10-fold excess of soluble, non-biotinylated ACE2 (200 nM).

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