Mutation detail:
| Mutation site | R221Q |
| 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 |
cell line |
| Variants | - |
| Viral reference sequence | FJ966081.1 |
| Drug/antibody/vaccine | - |
| Transmissibility |
- |
| Transmission mechanism | - |
| Pathogenicity |
increase |
| Pathogenicity mechanism | - |
| Immune escape mutation | - |
| Immune escape mechanism | - |
| RT-PCR primers probes | - |
Protein detail:
| Protein name | 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 | 30021892 |
| Clinical information | No |
| Disease | - |
| Published year | 2018 |
| Journal | JOURNAL OF VIROLOGY |
| Title | Functional Evolution of the 2009 Pandemic H1N1 Influenza Virus NS1 and PA in Humans |
| Author | Aitor Nogales,Luis Martinez-Sobrido,Kevin Chiem,David J. Topham,Marta L. DeDiego |
| Evidence | The amino acid sequences from the 9 human clinical isolates were identical and showed 4 amino acid changes (V100I, N204S, R221Q, and L229S) in the PA-X protein (Table 1) and 5 amino acid changes (V100I, P224S, N321K, I330V, and R362K) in the PA protein (Table 2), compared to the A/California/04/2009 pH1N1 strain, circulating at the origin of the pandemic. |