Mutation detail:
| Mutation site | T157A |
| Virus | Influenzavirus A H1N1 |
Mutation level  |
Amino acid Level |
| Gene/protein/region type | PA |
| Gene ID | 23308128 |
| Country | - |
| Mutation type |
nonsynonymous mutation |
| Genotype/subtype/clade | - |
| Sample |
Human |
| Variants | - |
| Viral reference sequence | CY130059.1 |
| Drug/antibody/vaccine | - |
| Transmissibility |
promote |
| Transmission mechanism | - |
| Pathogenicity |
increase |
| Pathogenicity mechanism | - |
| Immune escape mutation | - |
| Immune escape mechanism | - |
| RT-PCR primers probes | - |
Protein detail:
| Protein name | Polymerase PA |
| Uniprot protein ID | C3W5X6 |
| Protein length | 716 amino acids |
| Protein description | PA Plays an essential role in viral RNA transcription and replication by forming the heterotrimeric polymerase complex together with PB1 and PB2 subunits. The complex transcribes viral mRNAs by using a unique mechanism called cap-snatching. It consists in the hijacking and cleavage of host capped pre-mRNAs. These short capped RNAs are then used as primers for viral mRNAs. The PB2 subunit is responsible for the binding of the 5' cap of cellular pre-mRNAs which are subsequently cleaved after 10-13 nucleotides by the PA subunit that carries the endonuclease activity. |
Literature information:
| Pubmed ID | 30733797 |
| Clinical information | No |
| Disease | - |
| Published year | 2018 |
| Journal | Journal of Genetic Engineering and Biotechnology |
| Title | In silico thermodynamic stability of mammalian adaptation and virulence determinants in polymerase complex proteins of H9N2 virus |
| Author | Zienab Mosaad,Abdelsatar Arafa,Hussein A Hussein,Mohamed A Shalaby |
| Evidence | It was reported that PA mutations in the Amino acids T157A and T162A weaken the proteolysis Function of PA [48] but some PA mutation enhances the polymerase replication activity at higher temperatures to that influence the virus adaptations |