RE: S Protein Mutations12 Feb 2021 06:31
It was serendipity, but because one set of Thermos' primers to the S1 used the 69-70 as a binding site , they were able to follow progression of the B 1.1.7 (Kent) variant form early on.
There are variant in the other proteins including N (there is one in the N protein in B1.1.7). There are sites on S1 that have not changed and are the same as in Sars Cov so there is clearly very strong requirement for conservation at these sites .
The point is that the potential for mutation at all sites is not equal. It is a matter of choosing your binding sites wisely...
''In the case of SARS-CoV binding to hACE2, structural work identified 14 positions in RBD that are key for that binding: T402, R426,Y436,Y440, Y442, L472, N473, Y475, N479, Y484, T486, T487, G488 and Y491 Analysis of the 144 SARS-CoV-2 genome sequences, done by Walls and co-workers, revealed that 8 out of these 14 positions are strictly conserved, whereas the other 6; R426, Y442, L472, N479, Y484 and T487 (in SARS-CoV) are (semi)conservatively substituted with N439, L455, F486, Q493, Q498 and N501, respectively (in SARS-CoV-2) ''