Human influenza virus rapidly accumulates mutations in its major surface protein hemagglutinin (HA). The evolutionary success of influenza virus lineages depends on how these mutations affect HA’s functionality and antigenicity. Seasonal H3N2 influenza virus evolves rapidly, fixing 3 to 4 amino acid mutations per year in its hemagglutinin (HA) surface protein. Many of these mutations contribute to the rapid antigenic drift that necessitates frequent updates to the annual influenza vaccine. This evolution is further characterized by competition and turnover among groups of strains called clades bearing different complements of mutations. Clades vary widely in their evolutionary success, with some dying out soon after emergence and others going on to take over the virus population. Several lines of evidence indicate that successful clades have higher fitness than clades that remain at low frequency. A key goal in the study of H3N2 evolution is to identify the features that enable certain clades to succeed as others die out. Here you can see a recent crystal structure of the Hemagglutinin from H3N2 influenza virus determined to 2.2 Amgstrom resolution and showing a heavy glycosylation pattern (PDB code: 7QA4)
#molecularart ... #immolecular ... #influenza ... #virus ... #hemagglutinin ... #xray
Hemagglutinin structure rendered with @proteinimaging and depicted with @corelphotopaint
#molecularart ... #immolecular ... #influenza ... #virus ... #hemagglutinin ... #xray
Hemagglutinin structure rendered with @proteinimaging and depicted with @corelphotopaint
