Hydropathic evolution of hemagglutinin and neuraminidase glycoproteins of A(H1N1 and H3N2) viruses

TL;DR

This paper investigates how hydropathic force analysis reveals the mutational origins of increased virulence in H1N1 and H3N2 influenza viruses, providing insights beyond simple sequence comparisons.

Contribution

It introduces a fractal hydropathic analysis method to quantify virulence-related mutations and structural changes in influenza glycoproteins.

Findings

Hydropathic analysis correlates with increased virulence.

Mutational origins linked to changes in hydropathic forces.

Receptor sites and glycan attachment analyzed.

Abstract

More virulent strains of influenza virus subtypes H1N1 appeared in 2007 and H3N2 in 2011. The amino acid differences from prior less virulent strains appear to be small when tabulated through sequence alignments and counting site identities and similarities. Here we show how analyzing fractal hydropathic forces responsible for globular compaction and modularity quantifies the mutational origins of increased virulence, and also analyzes receptor sites and N-linked glycan accretion.