Structural analysis of Dioclea lasiocarpa lectin: A C6 cells apoptosis-inducing protein

Int J Biochem Cell Biol. 2017 Nov:92:79-89. doi: 10.1016/j.biocel.2017.09.014. Epub 2017 Sep 20.

Abstract

Lectins are multidomain proteins that specifically recognize various carbohydrates. The structural characterization of these molecules is crucial in understanding their function and activity in systems and organisms. Most cancer cells exhibit changes in glycosylation patterns, and lectins may be able to recognize these changes. In this work, Dioclea lasiocarpa seed lectin (DLL) was structurally characterized. The lectin presented a high degree of similarity with other lectins isolated from legumes, presenting a jelly roll motif and a metal-binding site stabilizing the carbohydrate-recognition domain. DLL demonstrated differential interactions with carbohydrates, depending on type of glycosidic linkage present in ligands. As observed by the reduction of cell viability in C6 cells, DLL showed strong antiglioma activity by mechanisms involving activation of caspase 3.

Keywords: Crystal structure; DLL; Dioclea lasiocarpa lectin; Glioma; Molecular docking.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Antineoplastic Agents / chemistry*
  • Antineoplastic Agents / metabolism
  • Antineoplastic Agents / pharmacology*
  • Apoptosis / drug effects*
  • Carbohydrate Metabolism
  • Cell Line, Tumor
  • Cell Survival / drug effects
  • Dioclea / chemistry*
  • Glioma / pathology*
  • Molecular Docking Simulation
  • Plant Lectins / chemistry*
  • Plant Lectins / metabolism
  • Plant Lectins / pharmacology*
  • Protein Conformation
  • Rats
  • Seeds / chemistry

Substances

  • Antineoplastic Agents
  • Plant Lectins