| | | Protein: | Spike | | Coronavirus type: | Human SARS (2004) | | Mutation (as in paper): | S487T from series Y436H, S487T | | neutral AA: | Y, S | | neg. eff. AA: | H, T | | Effect: | Antigenic Drift | | Comment: | | Y436H/S487T mutants allows the mutant spike protein to escape neutralization from nAb Y112A. | | Literature reference | | (Mutation S487T from series Y436H, S487T in the paper is at an equivalent position of the mutation in your query) |
| | | Protein: | Spike | | Coronavirus type: | Human SARS (2004) | | Mutation (as in paper): | S487T from series Y436H, S487T | | neutral AA: | Y, S | | neg. eff. AA: | H, T | | Effect: | Host Change | | Comment: | | Y436H/S487T mutants exhibit increased binding activity to human ACE2 by about 4-fold compared with the wild-type and Y436H mutant. The mutant virus also showed increased in vivo growth in young micecompared to the wild type, indicating a higher binding affinity to mouse ACE2 as well, though the binding affinity to mouse ACE2 is still weak. | | Literature reference | | (Mutation S487T from series Y436H, S487T in the paper is at an equivalent position of the mutation in your query) |
| | | Protein: | Spike | | Coronavirus type: | Human SARS-CoV-2 (2019) | | Mutation (as in paper): | N501Y from series K417N, E484K, N501Y | | neutral AA: | K, E, N | | neg. eff. AA: | N, K, Y | | Effect: | Antigenic Drift | | Comment: | | 27percent of the samples (convalescent sera from 44 individuals previously infected with SARS-CoV-2) with K417N, E484K, N501Y lost all activity against the Receptor Binding Domain triple mutants, while only 23percent retained higher titres of neutralising antibodies. | | Literature reference | | (Mutation N501Y from series K417N, E484K, N501Y in the paper is at an equivalent position of the mutation in your query) |
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