Mutation detail:
Mutation site | D144T |
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 | GQ149665.1 |
Drug/antibody/vaccine | - |
Transmissibility ![]() |
- |
Transmission mechanism | - |
Pathogenicity ![]() |
increase |
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 | 23637827 |
Clinical information | No |
Disease | - |
Published year | 2013 |
Journal | PLoS One |
Title | Glycosylation on Hemagglutinin Affects the Virulence and Pathogenicity of Pandemic H1N1/2009 Influenza A Virus in Mice |
Author | Yan Zhang,Jiping Zhu,Yongtao Li,Konrad C. Bradley |
Evidence | To add N-glycosylation sites to HA, nucleic acid mutations were performed to facilitate amino acid substitutions that created glycosylation motifs (Asn-X-Ser/Thr) at sites Asn142 (D144T) and Asn177 (K177N). Site-directed mutagenesis was performed using Pfu DNA polymerase |