Mutation detail:
Mutation site | G443A |
Virus | Norovirus |
Mutation level ![]() |
Amino acid level |
Gene/protein/region type | ORF2 |
Gene ID | 1491972 |
Country | - |
Mutation type ![]() |
nonsynonymous mutation |
Genotype/subtype/clade | GII.4 |
Sample ![]() |
Human |
Variants | - |
Viral reference sequence | GU325839.1 |
Drug/antibody/vaccine | - |
Transmissibility ![]() |
- |
Transmission mechanism | - |
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 | 31500340 |
Clinical information | No |
Disease | - |
Published year | 2019 |
Journal | Viruses |
Title | Human Norovirus Histo-Blood Group Antigen (HBGA) Binding Sites Mediate the Virus Specific Interactions with Lettuce Carbohydrates |
Author | Malak A Esseili, xiang Gao, Patricia Boley, Yixuan Hou , Linda J Saif |
Evidence | The VLPs of the two mutants D374A and G443A showed typical morphology and size (~40 nm in diameter) under TEM as those of the GII.4.HS194.2009 WT VLP (Figure 2A). Besides the 40 nm particles, the VLPs of the mutant D374A also formed particles with a 27 nm |