Cryptosporidium parvum metalloaminopeptidase inhibitors prevent in vitro excystation

Antimicrob Agents Chemother. 1996 Dec;40(12):2781-4. doi: 10.1128/AAC.40.12.2781.

Abstract

Cryptosporidium parvum arginine aminopeptidase (RAP) was studied during in vitro excystation. Specific RAP inhibitors were identified by using C. parvum extracts. Amastatin, a series of alpha-aminoboronic acids, and the chelating agents EDTA and 1,10-phenanthrolene, but not endoproteinase inhibitors, blocked enzymatic activity. RAP inhibitors found to be effective in soluble enzymatic assays were then studied for their effect on in vitro excystation. 1,10-Phenanthrolene, amastatin, and H-boronorleucine (pinacol) inhibited excystation by 84, 57, and 61%, respectively, compared with solvent-treated control oocysts. Sporozoites remained viable within the oocyst as determined by propidium iodide and fluorescein diacetate dye uptake, suggesting that alpha-aminoboronic acids were not directly lethal to the parasite.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Aminopeptidases / antagonists & inhibitors*
  • Animals
  • Anti-Bacterial Agents / pharmacology
  • Boronic Acids / analysis
  • Boronic Acids / pharmacology
  • Cryptosporidium parvum / drug effects*
  • Cryptosporidium parvum / enzymology
  • Cryptosporidium parvum / physiology
  • Edetic Acid / pharmacology
  • Peptides*
  • Phenanthrolines / pharmacology
  • Protease Inhibitors / pharmacology*
  • Spores / drug effects

Substances

  • Anti-Bacterial Agents
  • Boronic Acids
  • Peptides
  • Phenanthrolines
  • Protease Inhibitors
  • amastatin
  • Edetic Acid
  • Aminopeptidases
  • aminopeptidase B
  • 1,10-phenanthroline