Proteomic evaluation of adults of Rhyzopertha dominica resistant to phosphine

Byeoung Soo Park, Byung Ho Lee, Tae Wan Kim, Yong Lin Ren, Sung Eun Lee

Research output: Contribution to journalArticlepeer-review

20 Scopus citations

Abstract

A proteomic study using a PH3-susceptible (RD2) and -resistant strain (CRD343) of Rhyzopertha dominica was undertaken to validate the relation between change of proteins and PH3 resistance. Protein expression levels were compared using PD-Quest program after two-dimensional polyacrylamide gel-electrophoresis. Comparing the intensity of proteins, 15 proteins decreased and 6 proteins were newly expressed in CRD343. After MALDI-TOF and LC-MS/MS analyses, the decreased proteins were identified as arginine kinases, dihydrolipoamide dehydrogenase, Hsp60, reverse transcriptase, glyceraldehydes-3-phosphate dehydrogenase, triosephosphate isomerase and hypothetical proteins. Dihydrolipoamide dehydrogenase is involved in the Krebs cycle and glyceraldehydes-3-phosphate dehydrogenase and triosephosphate isomerase are involved in the glycolysis pathway. Among up-regulated proteins, sodium channel, glutamate racemase, enolase and vitellogenin were identified. Taken together, PH3 affected glycolysis as well as Krebs cycle and the induction of enolase might recover this dysfunction.

Original languageEnglish
Pages (from-to)121-126
Number of pages6
JournalEnvironmental Toxicology and Pharmacology
Volume25
Issue number1
DOIs
StatePublished - Jan 2008

Keywords

  • 2D-PAGE
  • Dihydrolipoamide dehydrogenase
  • Enolase
  • MALDI-TOF
  • Phosphine resistance
  • Rhyzopertha dominica

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