Identification and characterization of a novel prolyl oligopeptidase in filarial parasite Setaria cervi

Biochem Biophys Res Commun. 2018 Jan 15;495(3):2235-2241. doi: 10.1016/j.bbrc.2017.12.093. Epub 2017 Dec 19.

Abstract

A 75 kDa serine protease having prolyl oligopeptidase activity has been purified from Setaria cervi, a bovine filarial parasite. The MALDI-MS/MS analysis of the purified protein revealed 6 peptides showing nearest match S9A (prolyl oligopeptidase) family protein from Plesiocystis pacifica. The ScPOP was found to be unique compared to mammalian POP with respect to its kinetic properties. To elucidate its role, filarial parasites were exposed to specific inhibitor of POP, Z-Pro-prolinal (ZPP) for 8 h. The inhibition of POP induced calcium signaling via phospholipase c stimulation which further triggered mitochondrial mediated apoptosis in filarial parasites.

Keywords: Apoptosis; Calcium; ER stress; Mitochondria; Parasite; Prolyl oligopeptidase.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Apoptosis / physiology*
  • Binding Sites
  • Calcium Signaling / physiology*
  • Enzyme Activation
  • Mitochondria / enzymology*
  • Peptide Hydrolases / chemistry*
  • Peptide Hydrolases / metabolism*
  • Protein Binding
  • Setaria Nematode / enzymology*
  • Setaria Nematode / growth & development*
  • Substrate Specificity

Substances

  • Peptide Hydrolases
  • oligopeptidase