AVM v1, released 02-OCT-22

A manually curated database of aerosol-transmitted virus mutations, human diseases, and drugs

Mutation detail:


Mutation site L295P
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 CY041540.1
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 22809692
Clinical information No
Disease -
Published year 2012
Journal Virology
Title Both influenza hemagglutinin and polymerase acidic genes are important for delayed pandemic 2009 H1N1 virus clearance in the ferret model
Author Mariette F Ducatez,Natalia A Ilyushina,Thomas P Fabrizio,Jerold E Rehg,Nicolai V Bovin
Evidence In ferrets, H1N1 virus with HA K154Q and PA L295P mutations exhibited significantly higher titers in the upper respiratory tract compared to all other viruses 6 days post-infection.