AVM v1, released 02-OCT-22

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

Mutation detail:


Mutation site E23K
Virus Influenzavirus A H1N1
Mutation level Amino acid Level
Gene/protein/region type PA
Gene ID 23308128
Country US
Mutation type nonsynonymous mutation
Genotype/subtype/clade -
Sample cell line
Variants -
Viral reference sequence NC_026437.1
Drug/antibody/vaccine -
Transmissibility -
Transmission mechanism -
Pathogenicity -
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 32253432
Clinical information No
Disease -
Published year 2010
Journal The Journal of Infectious Diseases
Title Treatment-Emergent Influenza Virus Polymerase Acidic Substitutions Independent of Those at I38 Associated With Reduced Baloxavir Susceptibility and Virus Rebound in Trials of Baloxavir Marboxil
Author William L Ince,Fraser B Smith,Julian J O.Rear,Michael Thomson
Evidence US regulatory review of registrational trial data also identified treatment-emergent PA substitutions E23K in A/H1N1 viruses and E23G/K, A37T, and E199G in A/H3N2 viruses, which conferred reduced susceptibility to baloxavir, although to a lesser degree than I38F/M/N/T substitutions, and were associated with virus rebound.