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Identification and characterization of Paragonimus westermani leucine aminopeptidase.

Authors :
Song SM
Park JH
Kim J
Kim SI
Hong YC
Kong HH
Chung DI
Source :
Parasitology international [Parasitol Int] 2008 Sep; Vol. 57 (3), pp. 334-41. Date of Electronic Publication: 2008 Mar 04.
Publication Year :
2008

Abstract

Paragonimus westermani is a tissue-invading trematode parasite that causes inflammatory lung disease as well as systemic infections including cerebral invasion in carnivorous mammals. While aminopeptidases play important roles in trematodes in the catabolism of host hemoglobin, an essential source of nutrient for the parasite, little is known about aminopeptidase in Paragonimus. Presently, we isolated a cDNA encoding a 58 kDa P. westermani leucine aminopeptidase (PwLAP). Deduced amino acid sequence of PwLAP exhibited significant sequence homology with LAP from Schistosoma spp. and Fasciola hepatica. Biochemical analysis of the recombinant PwLAP protein demonstrated preferential substrate specificity for Leu-NHMec and inhibition by EDTA, 1,10-phenanthroline, and bestatin, which are conserved characteristics of the M17 family of leucine aminopeptidase. PwLAP exhibited relatively higher enzyme activity in the presence of Mn2+ compared to Schistosoma mansoni LAP. Based on the biochemical properties and immunohistochemical analysis, PwLAP is concluded to represent a leucine aminopeptidase. The enzyme is most likely responsible for the catabolism of host hemoglobin, and, hence, represents a potential target of Paragonimus chemotherapy.

Details

Language :
English
ISSN :
1383-5769
Volume :
57
Issue :
3
Database :
MEDLINE
Journal :
Parasitology international
Publication Type :
Academic Journal
Accession number :
18394951
Full Text :
https://doi.org/10.1016/j.parint.2008.02.004