AVM v1, released 02-OCT-22

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

Mutation detail:


Mutation site S31N
Virus Influenzavirus A H1N1
Mutation level Amino acid Level
Gene/protein/region type M2
Gene ID 23308108
Country -
Mutation type nonsynonymous mutation
Genotype/subtype/clade -
Sample cell line
Variants -
Viral reference sequence CY010790.1
Drug/antibody/vaccine amantadine resistant, rimantadine resistant
Transmissibility -
Transmission mechanism -
Pathogenicity -
Pathogenicity mechanism -
Immune escape mutation -
Immune escape mechanism -
RT-PCR primers probes -

Protein detail:


Protein name Matrix Protein 2
Uniprot protein ID C3W5X3
Protein length 97 amino acids
Protein description The M2 protein channel consists of 97 residues: (1) an ectodomain (residues 1-24); (2) the pore-forming TM helix (residues 25-43); (3) an amphiphilic C-terminal helix (residues 47-60); and (4)a cytoplasmic tail (residues 61-97). The influenza A virus M2 protein, a tetrameric type III integral transmembrane (TM) protein, is known to play an essential role in viral replication by mediating the acidification and uncoating of endosomally entrapped virus. The tetrameric M2 in the viral membrane functions as pH-dependent proton channels to equilibrate pH across the viral membrane during entry and across the trans-Golgi membrane of infected cells during viral maturation.

Literature information:


Pubmed ID 23437766
Clinical information No
Disease -
Published year 2013
Journal Journal of Medicinal Chemistry
Title Discovery of novel dual inhibitors of the wild-type and the most prevalent drug-resistant mutant, S31N, of the M2 proton channel from influenza A virus
Author Jizhou Wang,Chunlong Ma,Jun Wang,Hyunil Jo,Belgin Canturk,
Evidence Using a combination of structural information of M2 proton channel and medicinal chemistry approaches, we report the discovery of promising dual M2 inhibitors for S31N and WT M2 channels, demonstrating that M2 S31N is a druggable target.