Binding of a natural anthocyanin inhibitor to influenza neuraminidase by mass spectrometry.

Kavya Swaminathan, Jeffrey C Dyason, Andrea Maggioni, Mark von Itzstein, Kevin M Downard

Other Analytical and bioanalytical chemistry 2013 51 citations

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Study Design

Study Type: In Vitro
Population: Influenza neuraminidase enzyme (in vitro)

Intervention: Binding of a natural anthocyanin inhibitor to influenza neuraminidase by mass spectrometry. None
Comparator: None
Primary Outcome: Influenza neuraminidase inhibition
Effect Direction: Positive
Risk of Bias: Unclear

Abstract

The binding of a natural anthocyanin to influenza neuraminidase has been studied employing mass spectrometry and molecular docking. Derived from a black elderberry extract, cyanidin-3-sambubiocide has been found to be a potent inhibitor of sialidase activity. This study reveals the molecular basis for its activity for the first time. The anthocyanin is shown by parallel experimental and computational approaches to bind in the so-called 430-cavity in the vicinity of neuraminidase residues 356-364 and 395-432. Since this antiviral compound binds remote from Asp 151 and Glu 119, two residues known to regulate neuraminidase resistance, it provides the potential for the development of a new class of antivirals against the influenza virus without this susceptibility.

TL;DR

The anthocyanin is shown by parallel experimental and computational approaches to bind in the so-called 430-cavity in the vicinity of neuraminidase residues 356–364 and 395–432, providing the potential for the development of a new class of antivirals against the influenza virus without this susceptibility.

Used In Evidence Reviews

B Elderberry for Influenza

Binding of a natural anthocyanin inhibitor to influenza neuraminidase by mass spectrometry.

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Study Design

Abstract

TL;DR

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