Mutation detail:
| Mutation site | G41V |
| Virus | Influenzavirus A H1N1 |
Mutation level  |
Amino acid Level |
| Gene/protein/region type | NA |
| Gene ID | 23308118 |
| Country | - |
| Mutation type |
nonsynonymous mutation |
| Genotype/subtype/clade | - |
| Sample |
Human |
| Variants | - |
| Viral reference sequence | NC_026434.1 |
| Drug/antibody/vaccine | - |
| Transmissibility |
- |
| Transmission mechanism | - |
| Pathogenicity |
- |
| Pathogenicity mechanism | - |
| Immune escape mutation | - |
| Immune escape mechanism | - |
| RT-PCR primers probes | - |
Protein detail:
| Protein name | Neuraminidase |
| Uniprot protein ID | C3W6G3 |
| Protein length | 469 amino acids |
| Protein description | The NA assembles as a tetramer of four identical polypeptides and, when embedded in the envelope of the virus, accounts for approximately 10-20% of the total glycoproteins on the virion surface, with about 40-50 NA spikes and 300-400 HA spikes on an average sized virion of 120 nm. The four monomers, each of approximately 470 amino acids, fold into four distinct structural domains: the cytoplasmic tail, the transmembrane region, the stalk, and the catalytic head. The NA catalyzes the removal of terminal sialic acid residues from viral and cellular glycoconjugates. Cleaves off the terminal sialic acids on the glycosylated HA during virus budding to facilitate virus release. Additionally helps virus spread through the circulation by further removing sialic acids from the cell surface. These cleavages prevent self-aggregation and ensure the efficient spread of the progeny virus from cell to cell. Otherwise, infection would be limited to one round of replication. Described as a receptor-destroying enzyme because it cleaves a terminal sialic acid from the cellular receptors. May facilitate viral invasion of the upper airways by cleaving the sialic acid moities on the mucin of the airway epithelial cells. |
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). |