AVM v1, released 02-OCT-22

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

Mutation detail:


Mutation site L32I
Virus Influenzavirus A H1N1
Mutation level Amino acid Level
Gene/protein/region type HA
Gene ID 23308115
Country China
Mutation type nonsynonymous mutation
Genotype/subtype/clade -
Sample cell line
Variants -
Viral reference sequence GQ166223.1
Drug/antibody/vaccine -
Transmissibility -
Transmission mechanism -
Pathogenicity increase
Pathogenicity mechanism -
Immune escape mutation -
Immune escape mechanism -
RT-PCR primers probes -

Protein detail:


Protein name 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 21698272
Clinical information No
Disease -
Published year 2011
Journal PLoS One
Title Genomic Polymorphism of the Pandemic A (H1N1) Influenza Viruses Correlates with Viral Replication, Virulence, and Pathogenicity In Vitro and In Vivo
Author Lili Xu,Linlin Bao,Jianfang Zhou,Dayan Wang,Wei Deng
Evidence These mutations led to amino acid substitutions in HA (L32I), PA (A343T), PB1 (K353R and T566A), and PB2 (T471M), and may be critical molecular determinants for replication, virulence, and pathogenicity.