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A Calpain-Like Protein Is Involved in the Execution Phase of Programmed Cell Death of Entamoeba histolytica

Tania Domínguez-Fernández1, Mario Alberto Rodríguez1, Virginia Sánchez Monroy2

  • 1Departamento de Infectómica y Patogénesis Molecular, CINVESTAV, Ciudad de México, Mexico.

Frontiers in Cellular and Infection Microbiology
|October 16, 2018
PubMed

Insights

A calpain-like protein in Entamoeba histolytica is involved in programmed cell death (PCD). Inhibiting this protease reduces parasite cell death, suggesting its role in the PCD execution phase.

Area of Science:

  • Cell Biology
  • Parasitology
  • Biochemistry

Background:

  • Programmed cell death (PCD) in Entamoeba histolytica is induced by oxidative and chemical stress.
  • While caspases are absent, calpain, a calcium-activated cysteine protease, is implicated in E. histolytica PCD.

Purpose of the Study:

  • To investigate the role of a calpain-like protein in Entamoeba histolytica programmed cell death.
  • To validate the calpain-like protein as a potential executioner protease in E. histolytica PCD.

Main Methods:

  • Prediction of the 3D structure of the E. histolytica calpain-like protein.
  • Production of specific antibodies for protein detection and quantification.
  • Treatment with G418 to induce PCD and calpain-like protein expression analysis.
  • Utilizing small interfering RNA (siRNA) to assess the functional impact of the calpain-like protein on cell death.

Main Results:

  • The calpain-like protein was detected in the cytoplasm and near the nucleus of E. histolytica trophozoites.
  • Protein expression increased significantly after 9 hours of G418 treatment, correlating with PCD induction.
  • Specific calpain-like siRNA reduced the cell death rate by 65%, confirming its involvement in PCD.

Conclusions:

  • The calpain-like protein is a key protease in the execution phase of programmed cell death in Entamoeba histolytica.
  • The protein's interactome suggests it may regulate other PCD-related proteins, potentially those with calcium-binding domains.
Keywords:
Entamoeba histolyticacalcium binding sitescalpaincysteine proteasesprogrammed cell deathprotein overexpression

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