AVM v1, released 02-OCT-22

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

Mutation detail:


Mutation site I38T
Virus Influenzavirus A H1N1
Mutation level Amino acid Level
Gene/protein/region type PA
Gene ID 23308128
Country USA
Mutation type nonsynonymous mutation
Genotype/subtype/clade -
Sample cell line
Variants -
Viral reference sequence FJ966081.1
Drug/antibody/vaccine baloxavir resistant
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 33469660
Clinical information No
Disease -
Published year 2021
Journal Nucleic acids research
Title Structural insights into the substrate specificity of the endonuclease activity of the influenza virus cap-snatching mechanism
Author Gyanendra Kumar,Maxime Cuypers,Richard R Webby,Thomas R Webb,Stephen W White
Evidence To support this, we have failed to obtain RNA or DNA complex structures with PAN-I38T. While a number of mutations have been identified that have impacted the susceptibility of influenza viruses to baloxavir-like inhibitors, changes at position 38 are the most commonly observed clinically and the I38T mutation