Filovirus Glycoprotein Sequence, Structure and Virulence

TL;DR

This study links Ebola virus glycoprotein sequences and their hydropathic properties to differences in virulence and mortality rates, providing molecular insights into pathogenicity.

Contribution

It introduces a fractal hydropathic scaling approach to explain how specific amino acid features influence Ebola virulence.

Findings

Hydrophobic features correlate with mortality differences

Mucin-like domain hydropathic properties impact virulence

Sequence analysis explains mortality variability

Abstract

Leading Ebola subtypes exhibit a wide mortality range, here explained at the molecular level by using fractal hydropathic scaling of amino acid sequences based on protein self-organized criticality. Specific hydrophobic features in the hydrophilic mucin-like domain suffice to account for the wide mortality range. Significance statement: Ebola virus is spreading rapidly in Africa. The connection between protein amino acid sequence and mortality is identified here.