Molecular and biochemical mining of heat-shock and 14-3-3 proteins in drug-induced protoscolices of Echinococcus granulosus and the detection of a candidate gene for anthelmintic resistance

J Helminthol. 2011 Jun;85(2):196-203. doi: 10.1017/S0022149X10000477. Epub 2010 Aug 25.

Abstract

Cystic echinococcosis (CE) caused by the larval stage of Echinococcus granulosus is a disease that affects both humans and animals. In humans the disease is treated by surgery with a supplementary option of chemotherapy with a benzimidazole compound. During the present study heat-shock protein 60 (HSP 60) was identified as one of the most frequently expressed biomolecules by E. granulosus after albendazole treatment. Data were correlated with 14-3-3 protein signature, and overexpression of this molecule after albendazole induction was an indicator of cell survival and signal transduction during in vitro maintenance of E. granulosus for up to 72 h. This observation was further correlated with a uniform expression pattern of a housekeeping gene (actin II). Out of three β-tubulin gene isoforms of E. granulosus, β-tubulin gene isoform 2 showed a conserved point mutation indicative of benzimidazole resistance.

MeSH terms

  • 14-3-3 Proteins / biosynthesis
  • 14-3-3 Proteins / genetics*
  • Amino Acid Sequence
  • Animals
  • Anthelmintics / pharmacology*
  • Chaperonin 60 / biosynthesis
  • Chaperonin 60 / genetics*
  • Drug Resistance*
  • Echinococcus granulosus / drug effects*
  • Echinococcus granulosus / genetics*
  • Gene Expression Profiling
  • Gene Expression Regulation / drug effects
  • Molecular Sequence Data
  • Mutant Proteins / genetics
  • Point Mutation
  • Tubulin / genetics

Substances

  • 14-3-3 Proteins
  • Anthelmintics
  • Chaperonin 60
  • Mutant Proteins
  • Tubulin