Mutation detail:
| Mutation site | S494Y |
| Virus | SARS-CoV-2 |
Mutation level  |
Amino acid level |
| Gene/protein/region type | S |
| Gene ID | 43740568 |
| Country | - |
| Mutation type |
nonsynonymous mutation |
| Genotype/subtype/clade | - |
| Sample |
cell line |
| Variants | - |
| Viral reference sequence | QHD43416.1 |
| Drug/antibody/vaccine | VHH E_NAb-resistant |
| Transmissibility |
- |
| Transmission mechanism | - |
| Pathogenicity |
- |
| Pathogenicity mechanism | - |
| Immune escape mutation | Yes |
| Immune escape mechanism | - |
| RT-PCR primers probes | - |
Protein detail:
| Protein name | Spike glycoprotein |
| Uniprot protein ID | P0DTC2 |
| Protein length | 1273 amino acids |
| Protein description | Spike protein is one of the structural proteins of SARS-CoV-2. The monomeric protein consists of one large ectodomain, a single-pass transmembrane anchor, and a short intracellular tail at C-terminus. It encompasses 22 glycosylation sites. S protein cleaves into two subunits namely S1 and S2 following receptor recognition. Receptor Binding Domain (RBD) in S1 subunit plays a major role in ACE2 receptor binding. |
Literature information:
| Pubmed ID | 33436526 |
| Clinical information | No |
| Disease | - |
| Published year | 2021 |
| Journal | Science |
| Title | Structure-guided multivalent nanobodies block SARS-CoV-2 infection and suppress mutational escape |
| Author | Paul-Albert Koenig, Hrishikesh Das, Hejun Liu, Beate M. Kummerer, Florian N. Gohr |
| Evidence | Particularly prominent were escape mutations F490S or S494P in the VHH E interface, as well as S371P and K378Q in the UVW interface, which are expected to compromise the structurally defined VHH-RBD interface (see extended results in the supplementary materials). We identified further mutations in interfaces E (G447S, Y449H/D/N, L452R, F490S, S494P/S, G496S, and Y508H) and UVW (Y369H, S371P, F374I/V, T376I, F377L, and K378Q/N) in this and a separate evolution experiment (tables S5 to S8) |