Analytical and Bioanalytical Chemistry

, Volume 405, Issue 20, pp 6563–6572

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
Research Paper

DOI: 10.1007/s00216-013-7068-x

Cite this article as:
Swaminathan, K., Dyason, J.C., Maggioni, A. et al. Anal Bioanal Chem (2013) 405: 6563. doi:10.1007/s00216-013-7068-x

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.

Keywords

NeuraminidaseInhibitorInfluenzaAnthocyaninMass spectrometryMolecular docking

Copyright information

© Springer-Verlag Berlin Heidelberg 2013

Authors and Affiliations

  • Kavya Swaminathan
    • 1
  • Jeffrey C. Dyason
    • 2
  • Andrea Maggioni
    • 2
  • Mark von Itzstein
    • 2
  • Kevin M. Downard
    • 1
  1. 1.School of Molecular BioscienceUniversity of SydneySydneyAustralia
  2. 2.Institute for GlycomicsGriffith UniversityQueenslandAustralia