Mutation detail:
| Mutation site | A215V |
| Virus | Influenzavirus A H1N1 |
Mutation level  |
Amino acid Level |
| Gene/protein/region type | HA |
| Gene ID | 23308115 |
| Country | - |
| 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 | 33414352 |
| Clinical information | No |
| Disease | - |
| Published year | 2021 |
| Journal | Microbiology resource announcements |
| Title | Coding-Complete Genome Sequences of Six Influenza Type A Strains Circulating in Lithuania in the 2009-2010 Epidemic Season |
| Author | Lukasz Rabalski , Boguslaw Szewczyk , Kestutis Zagminas, Algirdas Griskevicius , Krzysztof Lepek |
| Evidence | All sequences were aligned, using MAFFT v7.388, against the A/California/07/2009 reference strain circulating among people at that time (9,-12). We observed a high degree of similarity (>99%) among all six strains as well as the reference strain (similarity levels are presented in Table 1). These analyses revealed several single-nucleotide polymorphisms that alter the amino acid sequences in two major surface glycoproteins, namely, hemagglutinin (HA) and neuraminidase (NA), i.e., V24I (isolate 1305), R45K (isolates 1319 and 1324), V47G (isolates 1319 and 1324), S74N (isolate 1167), P83S (all isolates), S203T (all isolates), A215V (isolate 1305), I321V (isolates 1167, 1172, 1241, and 1305), I321F (isolates 1319 and 1324), and E374K (all isolates except isolate 1167) in HA and G41V (isolate 1172), I46T (isolate 1167), V106I (all isolates), and N248D (all isolates) in NA. The S74N, P83S, S203T, and A215V substitutions are localized in epitope regions of HA or the immediate vicinity (13). The V47G and S74N substitutions were characterized earlier in our findings, in A(H1N1) isolates collected in Taiwan in 2010 to 2011 (14). None of the isolates harbored the NA drug resistance mutations in the NA gene (15). |