Molecular modeling, docking and dynamics simulations of GNA-related lectins for potential prevention of influenza virus (H1N1)

J Mol Model. 2012 Jan;18(1):27-37. doi: 10.1007/s00894-011-1022-7. Epub 2011 Mar 29.


The Galanthus nivalis agglutinin (GNA)-related lectin family exhibit significant anti-HIV and anti-HSV properties that are closely related to their carbohydrate-binding activities. However, there is still no conclusive evidence that GNA-related lectins possess anti-influenza properties. The hemagglutinin (HA) of influenza virus is a surface protein that is involved in binding host cell sialic acid during the early stages of infection. Herein, we studied the 3D-QSARs (three-dimensional quantitative structure-activity relationships) of lectin- and HA-sialic acid by molecular modeling. The affinities and stabilities of lectin- and HA-sialic acid complexes were also assessed by molecular docking and molecular dynamics simulations. Finally, anti-influenza GNA-related lectins that possess stable conformations and higher binding affinities for sialic acid than HAs of human influenza virus were screened, and a possible mechanism was proposed. Accordingly, our results indicate that some GNA-related lectins, such as Yucca filamentosa lectin and Polygonatum cyrtonema lectin, could act as drugs that prevent influenza virus infection via competitive binding. In conclusion, the GNA-related lectin family may be helpful in the design of novel candidate agents for preventing influenza A infection through the use of competitive combination against sialic acid specific viral infection.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Antiviral Agents / chemistry
  • Hydrogen Bonding
  • Influenza A Virus, H1N1 Subtype / drug effects*
  • Mannose-Binding Lectins / chemistry*
  • Models, Chemical
  • Models, Molecular*
  • Molecular Dynamics Simulation*
  • Molecular Sequence Data
  • Plant Lectins / chemistry*
  • Protein Structure, Secondary
  • Quantitative Structure-Activity Relationship
  • Sequence Alignment
  • Sequence Analysis, Protein


  • Antiviral Agents
  • Mannose-Binding Lectins
  • Plant Lectins
  • snowdrop lectin