AVM v1, released 02-OCT-22

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

Mutation detail:


Mutation site K177N
Virus Influenzavirus A H1N1
Mutation level Amino acid Level
Gene/protein/region type HA
Gene ID 23308115
Country -
Mutation type nonsynonymous mutation
Genotype/subtype/clade -
Sample cell line
Variants -
Viral reference sequence GQ149665.1
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 23637827
Clinical information No
Disease -
Published year 2013
Journal PLoS One
Title Glycosylation on Hemagglutinin Affects the Virulence and Pathogenicity of Pandemic H1N1/2010 Influenza A Virus in Mice
Author Yan Zhang,Jiping Zhu,Yongtao Li,Konrad C. Bradley
Evidence To add N-glycosylation sites to HA, nucleic acid mutations were performed to facilitate amino acid substitutions that created glycosylation motifs (Asn-X-Ser/Thr) at sites Asn142 (D144T) and Asn177 (K177N). Site-directed mutagenesis was performed using Pfu DNA polymerase