Analysis of sequence, structure of GAPDH of Leishmania donovani and its interactions

J Biomol Struct Dyn. 2013 Mar;31(3):258-75. doi: 10.1080/07391102.2012.698189. Epub 2012 Jul 25.

Abstract

Drug resistance acquired by Leishmania donovani (Ldv) is a major problem in the treatment and control of visceral leishmaniasis (VL). Glyceraldehyde-3-phosphate dehydrogenase (GAPDH), a major glycolytic enzyme has been targeted as is found in other protozoan which cause diseases like sleeping sickness. GAPDH gene of Ldv (AG83 strain) was amplified, sequenced, and modeled on the basis of crystal structure of Leishmania mexicana. The model of the Ldv GAPDH exhibited NAD-binding domain with Rossmann folding. Virtual screening of different experimentally proved compounds with the crystal and the modeled structures of GAPDH of Leishmania strains revealed diverse binding affinities of different compounds. Comparison of binding affinities (based on different programs) of compounds revealed that discovery studio v2.5 (Ligandfit) was able to predict the most hit compounds, the best hit compounds against GAPDH of Leishmania strains are hydrazine, vetrazine, and benzyl carbazate. It is predicted that patients suffering from both VL and cardiac disorders (atrial fibrillation) may benefit if they are treated with warfarin in conjunction with first-line antileishmanial therapies such as miltefosine and AmBisome.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Binding Sites
  • DNA Primers / metabolism
  • Glyceraldehyde-3-Phosphate Dehydrogenases / chemistry*
  • Glyceraldehyde-3-Phosphate Dehydrogenases / metabolism*
  • Leishmania donovani / drug effects
  • Leishmania donovani / enzymology*
  • Molecular Docking Simulation
  • Molecular Dynamics Simulation
  • Molecular Sequence Data
  • NAD / metabolism
  • Phylogeny
  • Protein Binding / drug effects
  • Protein Processing, Post-Translational / drug effects
  • Protein Subunits / chemistry
  • Protein Subunits / metabolism
  • RNA, Protozoan / isolation & purification
  • Reproducibility of Results
  • Sequence Analysis, Protein*
  • Thermodynamics
  • Triazoles / chemistry
  • Triazoles / pharmacology

Substances

  • DNA Primers
  • Protein Subunits
  • RNA, Protozoan
  • Triazoles
  • NAD
  • posaconazole
  • Glyceraldehyde-3-Phosphate Dehydrogenases