Mutation detail:
| Mutation site | K449R |
| Virus | Norovirus |
Mutation level  |
Amino acid level |
| Gene/protein/region type | ORF2 |
| Gene ID | 1491972 |
| Country | Vietnam |
| Mutation type |
nonsynonymous mutation |
| Genotype/subtype/clade | GII.10 |
| Sample |
cell line |
| Variants | - |
| Viral reference sequence | AF504671.1 |
| Drug/antibody/vaccine | - |
| Transmissibility |
hinder |
| Transmission mechanism | However, the K449R mutant lost binding to all saliva samples (Fig. 3K), although both K and R are positive charged amino acids. This data indicate complex roles of the K449 in the binding function and as factor of binding specificity of GII.10 NoV. |
| Pathogenicity |
- |
| Pathogenicity mechanism | - |
| Immune escape mutation | - |
| Immune escape mechanism | - |
| RT-PCR primers probes | - |
Protein detail:
| Protein name | Capsid protein VP1 |
| Uniprot protein ID | Q83884 |
| Protein length | 530 amino acids |
| Protein description | The ORF2 encodes the major capsid protein, VP1, which consists of a shell (S) and two protruding (P) domains, P1 and P2. The S domain is responsible for assembly of VP1, and the P1 domain enhances the stability of virus particles.27,28 The P2 domain, the most exposed surface of the viral particle,27 is involved in interaction with both potential neutralizing antibody and histo-blood group antigens (HBGAs), which are the presumptive initial binding site in establishing human infection. |
Literature information:
| Pubmed ID | 25591173 |
| Clinical information | No |
| Disease | - |
| Published year | 2015 |
| Journal | Virology |
| Title | Strain-specific interaction of a GII.10 Norovirus with HBGAs |
| Author | Miao Jin, Ming Tan, Ming xia, chao wei, Pengwei Huang |
| Evidence | Table 2 |