Arginine aminopeptidase, an integral membrane protein of the Cryptosporidium parvum sporozoite

P. C. Okhuysen, H. L. DuPont, C. R. Sterling, C. L. Chappell

Research output: Contribution to journalComment/debate

27 Scopus citations

Abstract

Cryptosporidium parvum oocysts were studied for the expression of aminopeptidase by using amino acids bound to the synthetic fluorescent substrate 7-amino-4-trifluoromethyl coumarin. After 1 h of incubation, intact oocysts showed no activity; however, homogenization and solubilization with Triton X-114 followed by phase separation yielded a 22-fold increase in aminopeptidase activity in the detergent fraction. With arginyl-6-amino-2- styrylquinoline as a substrate, aminopeptidase activity was observed in permeabilized oocysts and freshly excysted sporozoites but not on intact oocysts or empty oocyst membranes after excystation. These results suggest that C. parvum expresses an arginine aminopeptidase that is an integral protein of the sporozoite membrane.

Original languageEnglish (US)
Pages (from-to)4667-4670
Number of pages4
JournalInfection and Immunity
Volume62
Issue number10
StatePublished - Oct 5 1994

ASJC Scopus subject areas

  • Parasitology
  • Microbiology
  • Immunology
  • Infectious Diseases

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