AVM v1, released 02-OCT-22

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

Mutation detail:


Mutation site S160G
Virus Influenzavirus A H1N1
Mutation level Amino acid Level
Gene/protein/region type HA
Gene ID 23308115
Country Australia
Mutation type nonsynonymous mutation
Genotype/subtype/clade -
Sample Human
Variants -
Viral reference sequence NC_026434.1
Drug/antibody/vaccine -
Transmissibility -
Transmission mechanism -
Pathogenicity -
Pathogenicity mechanism -
Immune escape mutation -
Immune escape mechanism -
RT-PCR primers probes -

Protein detail:


Protein name Hemagglutinin
Uniprot protein ID C3W627
Protein length 566 amino acids
Protein description The HA protein is translated as an uncleaved HA0 precursor protein, folded as a trimer, and glycosylated and acylated. The HA protein binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell. This attachment induces virion internalization either through clathrin-dependent endocytosis or through clathrin- and caveolin-independent pathway. Plays a major role in the determination of host range restriction and virulence. Class I viral fusion protein. Responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. Low pH in endosomes induces an irreversible conformational change in HA2, releasing the fusion hydrophobic peptide. Several trimers are required to form a competent fusion pore.

Literature information:


Pubmed ID 22790606
Clinical information No
Disease -
Published year 2012
Journal Euro Surveill
Title Frequency of oseltamivir resistance in Sydney, during the Newcastle outbreak of community transmitted oseltamivir-resistant influenza A(H1N1)pdm09 virus, Australia, June to August 2018
Author B Wang,J Taylor,M Ratnamohan,K McPhie,A Kesson
Evidence the 2011 sequences showed five additional mutations (N44S, V62I, V241I, N369K and N386S) in NA and six additional amino acid substitutions (E130K, S160G, S202T, A214T, E391K and S468N) in HA (Figure 1). These were commonly present in most of the 2019 sequences and independent of their resistance profile.