Mutation detail:
| Mutation site | V683T/A684S |
| Virus | Influenzavirus A H1N1 |
Mutation level  |
Amino acid Level |
| Gene/protein/region type | PB2 |
| Gene ID | 23308131 |
| Country | - |
| Mutation type |
nonsynonymous mutation |
| Genotype/subtype/clade | - |
| Sample |
cell line |
| Variants | - |
| Viral reference sequence | NC_026438.1 |
| Drug/antibody/vaccine | - |
| Transmissibility |
promote |
| Transmission mechanism | - |
| Pathogenicity |
- |
| Pathogenicity mechanism | - |
| Immune escape mutation | - |
| Immune escape mechanism | - |
| RT-PCR primers probes | - |
Protein detail:
| Protein name | Polymerase PB2 |
| Uniprot protein ID | C3W5X5 |
| Protein length | 759 amino acids |
| Protein description | PB2 plays an essential role in transcription initiation and cap-stealing mechanism, in which cellular capped pre-mRNAs are used to generate primers for viral transcription. Recognizes and binds the 7-methylguanosine-containing cap of the target pre-RNA which is subsequently cleaved after 10-13 nucleotides by the viral protein PA. Plays a role in the initiation of the viral genome replication and modulates the activity of the ribonucleoprotein (RNP) complex. |
Literature information:
| Pubmed ID | 26018156 |
| Clinical information | No |
| Disease | - |
| Published year | 2015 |
| Journal | JOURNAL OF VIROLOGY |
| Title | Identification of Influenza A Virus PB2 Residues Involved in Enhanced Polymerase Activity and Virus Growth in Mammalian Cells at Low Temperatures |
| Author | Tsuyoshi Hayashi,Saintedym Wills,Kendra A. Bussey,Toru Takimoto |
| Evidence | Using a reporter gene assay, we identified novel mutations, PB2 V661A and V683T/A684S, which are involved in enhanced Cal polymerase activity at low temperature.The PB2 T271A mutation, which we previously reported, also contributed to enhanced activity. |