Figure: 24 hours after infection, cells were harvested, and the expression of wild-type and mutant HA was measured by flow cytometry to evaluate the effect of the A388V mutation on the HA stalk epitopes.
Figure: A388V mutation, HA trimerization domain, and StrepTag II sequence are highlighted.
Figure: A significant conformational change to the HA stalk region induced by A388V mutation.
Figure: Amino acid sequences of (a) f
Discussion: Although our study suggests that V388 mutation would be substantially more resistant to multiple potent bNAbs, or to currently existing human serum antibodies in general, the neutralization efficacy of FI6V3 antibody was not affected by the A388V mutation.
Antigenicity of the 2015-2016 seasonal H1N1 human influenza virus HA and NA proteins.
Discussion: While not at exactly the same position, the E391K mutation in the circulating viruses is close to the A388V mutation we and other described after growing the virus in the presence of 6F12 mAb, and may be part of the same epitope.
IV mutation literature information.
PMID: 
2020
Nature medicine
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