Mutation detail:
| Mutation site | V237M |
| 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 |
cell line |
| Variants | - |
| Viral reference sequence | FJ966082.1 |
| Drug/antibody/vaccine | MAb-CR9114 resistant |
| Transmissibility |
- |
| Transmission mechanism | - |
| Pathogenicity |
- |
| Pathogenicity mechanism | - |
| Immune escape mutation | Yes |
| 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 | 29097696 |
| Clinical information | No |
| Disease | - |
| Published year | 2017 |
| Journal | Sci Rep |
| Title | Natural and directed antigenic drift of the H1 influenza virus hemagglutinin stalk domain |
| Author | Christopher S Anderson,Sandra Ortega,Francisco A Chaves,Amelia M Clark,Hongmei Yang |
| Evidence | After passaging A/California/04/2009/E3 virus 16 times in MDCK cells in the presence of the different human sera and mAbs, mutations in the HA protein head and stalk domains were found, although at different passages (Table1). Specifically, serum from subject FAM195 selected a mutation in the head domain (V237M), in antigenic site Ca2; sera from subjects FAM196 and FAM297 selected a mutation in the head domain (A152S); sera from subject FAM298 selected a mutation in the stalk domain (V41I), and the mutation A152S; sera from subject FAM300 selected two mutations in the head domain (T89A, and S160G), in the described antigenic sites Cb, and Ca2, respectively50; and the two mAbs selected 3 mutations in the stalk domain (the CR9114 mAb selected mutations V466I, and R526G, and the 6F12 mAb selected the mutation A388V) (Table1 and Fig.4). As controls, the virus was passaged 16 times in the presence of two human sera (from patients FAM203 and FAM256) showing low HAI titers (<10, Supplementary Table3), in the presence of human and mouse IgG isotype controls, and in the presence of no sera/antibodies (Table1). None of the mutations selected under immune pressure were selected in these cases. We found no mutations in the stalk domain, and only two mutations in the head domain (Table8). |