Mutation detail:
| Mutation site | H655Y |
| Virus | SARS-CoV-2 |
Mutation level  |
Amino acid level |
| Gene/protein/region type | S |
| Gene ID | 43740568 |
| Country | USA |
| Mutation type |
nonsynonymous mutation |
| Genotype/subtype/clade | - |
| Sample |
cell line |
| Variants | Gamma/Omicron |
| Viral reference sequence | NC_045512.2 |
| Drug/antibody/vaccine | - |
| Transmissibility |
promote |
| Transmission mechanism | we provided evidence that some of these specific polymorphisms enhance viral growth, spike cleavage, and syncytia formation and therefore confer an advantage in viral transmission. |
| Pathogenicity |
- |
| Pathogenicity mechanism | - |
| Immune escape mutation | - |
| 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 | 35150638 |
| Clinical information | No |
| Disease | - |
| Published year | 2022 |
| Journal | Cell Host & Microbe |
| Title | Mutations in SARS-CoV-2 variants of concern link to increased spike cleavage and virus transmission |
| Author | Alba Escalera, Ana S Gonzalez-Reiche, Sadaf Aslam, Ignacio Mena, Manon Laporte |
| Evidence | The S:655Y substitution was transmitted more efficiently than its ancestor S:655H in the hamster infection model and was able to outcompete S:655H in the hamster model and in a human primary airway system. |