Journal
ORGANIC & BIOMOLECULAR CHEMISTRY
Volume 7, Issue 15, Pages 3040-3048Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/b901735f
Keywords
-
Categories
Funding
- Royal Society URF (NJW)
- PHS [AI054961]
- Wellcome Trust (MS/MS instrumentation)
- NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES [R01AI054961, R56AI054961] Funding Source: NIH RePORTER
Ask authors/readers for more resources
Conoidin A (1) is an inhibitor of host cell invasion by the protozoan parasite Toxoplasma gondii. In the course of studies aimed at identifying potential targets of this compound, we determined that it binds to the T. gondii enzyme peroxiredoxin II (TgPrxII). Peroxiredoxins are a widely conserved family of enzymes that function in antioxidant defense and signal transduction, and changes in PrxII expression are associated with a variety of human diseases, including cancer. Disruption of the TgPrxII gene by homologous recombination had no effect on the sensitivity of the parasites to 1, suggesting that TgPrxII is not the invasion-relevant target of 1. However, we showed that 1 binds covalently to the peroxidatic cysteine of TgPrxII, inhibiting its enzymatic activity in vitro. Studies with human epithelial cells showed that 1 also inhibits hyperoxidation of human PrxII. These data identify Conoidin A as a novel inhibitor of this important class of antioxidant and redox signaling enzymes.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available