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Influenza virus contains two highly variable envelope glycoproteins,hemagglutinin (HA) and neuraminidase (NA). The structure and properties of HA,which is responsible for binding the virus to the cell that is being infected,change significantly when the virus is transmitted from avian or swine speciesto humans. Here we focus on much smaller human individual evolutionary aminoacid mutational changes in NA, which cleaves sialic acid groups and is requiredfor influenza virus replication. We show that very small amino acid changes canbe monitored very accurately across many Uniprot and NCBI strains usinghydropathicity scales to quantify the roughness of water film packages.Quantitative sequential analysis is most effective with the differentialhydropathicity scale based on protein self-organized criticality (SOC). NAexhibits punctuated evolution at the molecular scale, millions of times smallerthan the more familiar species scale, and thousands of times smaller than thegenomic scale. Our analysis shows that large-scale vaccination programs havebeen responsible for a very large convergent reduction in influenza severity inthe last century, a reduction which is hidden from short-term studies ofvaccine effectiveness. Hydropathic analysis is capable of interpreting and evenpredicting trends of functional changes in mutation prolific viruses.

Punctuated evolution of influenza virus neuraminidase (A/H1N1) under migration and vaccination pressures