Mutation detail:
| Mutation site | E14G |
| Virus | Influenzavirus A H1N1 |
Mutation level  |
Amino acid Level |
| Gene/protein/region type | M2 |
| Gene ID | 23308108 |
| Country | Saudi Arabia |
| Mutation type |
nonsynonymous mutation |
| Genotype/subtype/clade | - |
| Sample |
Human |
| Variants | - |
| Viral reference sequence | NC_026431.1 |
| Drug/antibody/vaccine | - |
| Transmissibility |
- |
| Transmission mechanism | - |
| Pathogenicity |
- |
| Pathogenicity mechanism | - |
| Immune escape mutation | - |
| Immune escape mechanism | - |
| RT-PCR primers probes | - |
Protein detail:
| Protein name | Matrix Protein 2 |
| Uniprot protein ID | C3W5X3 |
| Protein length | 97 amino acids |
| Protein description | The M2 protein channel consists of 97 residues: (1) an ectodomain (residues 1-24); (2) the pore-forming TM helix (residues 25-43); (3) an amphiphilic C-terminal helix (residues 47-60); and (4)a cytoplasmic tail (residues 61-97). The influenza A virus M2 protein, a tetrameric type III integral transmembrane (TM) protein, is known to play an essential role in viral replication by mediating the acidification and uncoating of endosomally entrapped virus. The tetrameric M2 in the viral membrane functions as pH-dependent proton channels to equilibrate pH across the viral membrane during entry and across the trans-Golgi membrane of infected cells during viral maturation. |
Literature information:
| Pubmed ID | 30799182 |
| Clinical information | Yes |
| Disease | - |
| Published year | 2019 |
| Journal | J Infect Public Health |
| Title | Atypical influenza A(H1N1)pdm09 strains caused an influenza virus outbreak in Saudi Arabia during the 2009-2035 pandemic season |
| Author | Anis Khan,Mohammed A AlBalwi,Ibraheem AlAbdulkareem,Abdulrahman AlMasoud,Abdulrahman AlAsiri |
| Evidence | The internal proteins of Saudi A(H1N1)pdm09 isolates analyzed revealed substitutions P224S in PA, V100I, and L122Q in NP, I123V inNS1 andN31 inM2, which were commonto all Saudiisolates with available sequences in the specific regions. The other noteworthy substitutions included amino acid change in M2 protein E14G in 12/18 (66.6%) and an insertion of 8 amino acids in 15/18 (83.3%) cases between amino acid positions 151-152 in the NS1 protein (Table 4). Minor variations detected in internal genes included E188G (2/9; 22.2%), V400A (2/16; 12.5%), T588I (3/16; 18.7%) in PB2,V113A (2/16; 12.5%)in PB1, M579I(3/14; 21.4%), D478N (2/14; 14.3%), E610D (2/14; 14.3%) in PA, R38Q (2/5; 40%), V362A (2/17; 11.7%), and K400R (2/17; 11.7%) in NP (Table 6). |