The neuraminidase protein of the influenza A virus acts to cleave terminal sialic acid moieties from cell surface receptors, allowing the release of new virus copies from the host cell.  The flexibility of the 150 loop of the active site of the neuraminidase protein varies between different influenza strains and therefore affects the kinetics of the binding of the natural sialic acid moieties as well as neuraminidase inhibitors such as oseltamivir.  In particular, the electrostatics of the 150 loop residues may account for the differences in binding kinetics between strains.  By running Brownian Dynamics (BD) simulations of the association of oseltamivir with mutant and wild type neuraminidases from different strains of the influenza A virus, we were able to analyze the role of specific charged residues in the kinetics of binding in the active site.

Role of influenza A neuraminidase electrostatics in the binding of ligands

243rd National Meeting (2012)

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