Peak protein from mutant strain B.1.525, also commonly known as the “UK and Nigeria variant”. It is a full-length protein, which is active in its native trimeric form, which is stabilized in LMNG detergent.
SARS-CoV-2 spike glycoprotein, UK / Nigeria variant B.1.525. Active trimeric form. UniProt acc. no. P0DTC2. Complete sequence aa 1 –1273. Mutations: del 69-70, del 144, Q52R, E484K, Q667H, F888L. Other mutations: RRAR furin cleavage site modified to GSAG, K986P, V987P. C-terminal label.
Ten emerging variants of SARS-CoV-2: B.1.1.298, B.1.1.7, B.1.351, P.1, P.2, B.1.429, B.1.525, B.1.526-1, B.1.526-2, B.1.1.318, and seven corresponding single amino acid mutations in the binding receptor Domains were examined using SARS-CoV-2 pseudovirus. The results indicate that the current SARS-CoV-2 variants do not increase infectivity between humans. Variants carrying K417N / T, N501Y, or E484K exhibited greater capacities to infect mouse cells that overexpress ACE2. Furin’s activities, TMPRSS2, and cathepsin L were increased against most of the variants.
RBD amino acid mutations comprising K417T / N, L452R, Y453F, S477N, E484K, and N501Y caused a significant immune escape of 11 of 13 monoclonal antibodies. However, resistance to neutralization by serum or convalescent serum vaccines was caused mainly by the E484K mutation, while the neutralization of the E484K carrier variants was reduced between 1.1 and 6.2 times. Convalescent serum from patients infected with B.1.1.7 and B.1.351 neutralized the variants themselves better than other SARS-CoV-2 variants.