Mutation detail:
Mutation site | S159N |
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 | CY064974.1 |
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 | 21784793 |
Clinical information | No |
Disease | - |
Published year | 2011 |
Journal | Bioinformatics |
Title | Structural analysis of the hot spots in the binding between H1N1 HA and the 2D1 antibody: do mutations of H1N1 from 1918 to 2010 affect much on this binding? |
Author | Qian Liu,Steven C H Hoi,Chinh T T Su,Zhenhua Li,Chee-Keong Kwoh |
Evidence | Using the Z-score method, three of the six mutations-T133N, S159N and N171D-are predicted as non-hot spot residues in both 1918HA1 and 2009HA1. Two mutations-V169I, and T242K-are believed to contribute, though slightly, to the antibody binding in 2009HA1 only after the mutations. They may be newly formed hot spots in the epitope of 2009HA1 after the mutations. The remaining one of the six mutations-E131D-is predicted to contribute to the binding free energy both before and after the mutation. |