Mutation detail:
| Mutation site | V367F |
| Virus | SARS-CoV-2 |
Mutation level  |
Amino acid level |
| Gene/protein/region type | S |
| Gene ID | 43740568 |
| Country | Asia, Europe, North America, and Oceania |
| Mutation type |
nonsynonymous mutation |
| Genotype/subtype/clade | - |
| Sample |
Human |
| Variants | - |
| Viral reference sequence | NC_045512.2 |
| Drug/antibody/vaccine | - |
| Transmissibility |
promote |
| Transmission mechanism | V367F Mutation in SARS-CoV-2 Spike RBD Emerging during the Early Transmission Phase Enhances Viral Infectivity through Increased Human ACE2 Receptor Binding Affinity |
| 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 | 34105996 |
| Clinical information | No |
| Disease | - |
| Published year | 2021 |
| Journal | Journal Of Virology |
| Title | V367F Mutation in SARS-CoV-2 Spike RBD Emerging during the Early Transmission Phase Enhances Viral Infectivity through Increased Human ACE2 Receptor Binding Affinity |
| Author | Junxian Ou,Zhonghua Zhou,Ruixue Dai,Jing Zhang,Shan Zhao |
| Evidence | First, we performed experiments to assess the binding affinity in vitro with a receptor-ligand binding enzyme-linked immunosorbent assay (ELISA) using purified S proteins and human ACE2 protein. The result showed that the V367F mutation lowered the 50% effective dose (ED50) concentration (ED50 = 0.8-0.04μg/ml) compared to that of the prototype (ED50 = 1.7-0.14μg/ml) (Fig. 5A). This demonstrates that the V367F mutant has a higher affinity to human ACE2 than the prototype. Second, we performed surface plasmon resonance (SPR) experiments, which yielded the same conclusion: the prototype had a KD of 5.08 nM compared to the V367F mutant with a KD of 2.70 nM (Fig. 5B). Additionally, we performed a virus-cell interaction experiment to investigate the invasion efficiency of S proteins using an HIV backbone pseudovirus assay. ACE2-overexpressing Vero and Caco-2 cells were infected by the pseudoviruses bearing the mutant or wild-type RBD with the same multiplicity of infection (MOI). A higher infection efficiency is represented by the increased copy number of the integrated lentivirus genome. At 24 hpostinfection (h p.i.), the V367F pseudoviruses showed 6.08 higher copy numbers than the prototype in Caco-2 cells (P < 0.01). At 48 h p.i., the V367F pseudoviruses showed 6.61 and 9.16 higher copy numbers than the prototype in Vero (P < 0.0001) and Caco-2 cells (P < 0.0001), respectively (Fig. 5C). |