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More virulent strains of influenza virus subtypes H1N1 appeared widely in2007 and H3N2 in 2011, and especially 2013-4, when the effectiveness of theH3N2 vaccine decreased nearly to zero. The amino acid differences ofneuraminidase from prior less virulent strains appear to be small (<1%) whentabulated through sequence alignments and counting site identities andsimilarities. Here we show how analyzing fractal hydropathic forces responsiblefor neuraminidase globular compaction and modularity quantifies the mutationalorigins of increased virulence. It also predicts vaccine escape and specifiesoptimized targets for the 2015 H3N2 vaccine different from the WHO target.Unlike some earlier methods based on measuring hemagglutinin antigenic driftand ferret sera, which take several years, cover only a few candidate strains,and are ambiguous, the new methods are timely and can be completed, using NCBIand GISAID amino acid sequences only, in a few days.

Vaccine escape in 2013-4 and the hydropathic evolution of glycoproteins of A/H3N2 viruses