Partial purification and characterization of a cysteine protease Inhibitor from the plerocercoid of Spirometra erinacei

Young Bae Chung, Hyun Jong Yang

Research output: Contribution to journalArticlepeer-review

7 Scopus citations

Abstract

Helminthic cysteine proteases are well known to play critical roles in tissue invasion, nutrient uptake, and immune evasion of the parasites. In the same manner, the sparganum, the plerocercoid of Spirometra mansoni, is also known to secrete a large amount of cysteine proteases. However, cysteine protease inhibitors regulating the proteolytic activities of the cysteine protease are poorly illustrated. In this regard, we partially purified an endogenous cysteine protease inhibitor from spargana and characterized its biochemical properties. The cysteine protease inhibitor was purified by sequential chromatographies using Resource Q anion exchanger and Superdex 200 HR gel filtration from crude extracts of spargana. The molecular weight of the purified protein was estimated to be about 11 kD on SDS-PAGE. It was able to inhibit papain and 27 kDa cysteine protease of spargana with the ratio of 25.7% and 49.1%, respectively, while did not inhibit chymotrypsin. This finding suggests that the cysteine protease inhibitor of spargana may be involved in regulation of endogenous cysteine proteases of the parasite, rather than interact with cysteine proteases from their hosts.

Original languageEnglish
Pages (from-to)183-186
Number of pages4
JournalThe Korean journal of parasitology
Volume46
Issue number3
DOIs
StatePublished - 2008

Keywords

  • Cysteine protease
  • Inhibitor
  • Plerocercoid
  • Sparganum
  • Spirometra mansoni

Fingerprint

Dive into the research topics of 'Partial purification and characterization of a cysteine protease Inhibitor from the plerocercoid of Spirometra erinacei'. Together they form a unique fingerprint.

Cite this