Mutation detail:
| Mutation site | R182M |
| Virus | Influenzavirus A H1N1 |
Mutation level  |
Amino acid Level |
| Gene/protein/region type | HA |
| Gene ID | 23308115 |
| Country | Saudi Arabia |
| Mutation type |
nonsynonymous mutation |
| Genotype/subtype/clade | - |
| Sample |
Human |
| Variants | - |
| Viral reference sequence | NC_026433.1 |
| Drug/antibody/vaccine | - |
| Transmissibility |
- |
| Transmission mechanism | - |
| Pathogenicity |
- |
| Pathogenicity mechanism | - |
| Immune escape mutation | - |
| Immune escape mechanism | - |
| RT-PCR primers probes | - |
Protein detail:
| Protein name | Hemagglutinin |
| Uniprot protein ID | C3W627 |
| Protein length | 566 amino acids |
| Protein description | The HA protein is translated as an uncleaved HA0 precursor protein, folded as a trimer, and glycosylated and acylated. The HA protein binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell. This attachment induces virion internalization either through clathrin-dependent endocytosis or through clathrin- and caveolin-independent pathway. Plays a major role in the determination of host range restriction and virulence. Class I viral fusion protein. Responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. Low pH in endosomes induces an irreversible conformational change in HA2, releasing the fusion hydrophobic peptide. Several trimers are required to form a competent fusion pore. |
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 2009-2017 pandemic season |
| Author | Anis Khan,Mohammed A AlBalwi,Ibraheem AlAbdulkareem,Abdulrahman AlMasoud,Abdulrahman AlAsiri |
| Evidence | According to the amino acid substitution pattern, sequences were classified into five groups. Group 1 had a signature amino acid change in HA2 subunit of unknown function V47I detected in 4/43 (9.3%) cases. Group 2 included sequences with variations in major glycosylation site of HA important in disease severity, that is, A285S present in 4/43 (9.3%) and I295V in one isolate (2.3%). A fickle substitution of unknown function was detected at residue 175 (V175S/C/G/L) in 8/43 (18.6%) isolate; out of which four sequences with V175G clustered in rather smaller group 3. Group 4 included 2/43 (4.6%) study sequences, two with double mutation S478N/R509M (S151N and R182M in HA3 subunit). |