Molecular and biochemical characterization of hemoglobinase, a cysteine proteinase, in Paragonimus westermani.
10.3347/kjp.2006.44.3.187
- Author:
Joon Hyuck CHOI
1
;
Jae Hyuk LEE
;
Hak Sun YU
;
Hae Jin JEONG
;
Jin KIM
;
Yeon Chul HONG
;
Hyun Hee KONG
;
Dong Il CHUNG
Author Information
1. Department of Parasitology, Kyungpook National University School of Medicine, Daegu 700-422, Korea. hhkong@knu.ac.kr
- Publication Type:Original Article ; Research Support, Non-U.S. Gov't
- Keywords:
Paragonimus westermani;
lung fluke;
cysteine proteinase;
hemoglobinase
- MeSH:
Sequence Alignment;
Recombinant Proteins/biosynthesis/genetics;
Phylogeny;
Paragonimus westermani/*enzymology/genetics;
Molecular Sequence Data;
Hemoglobins/metabolism;
Escherichia coli/enzymology/genetics;
DNA, Complementary/genetics;
Cysteine Endopeptidases/*genetics/immunology/*metabolism;
Astacoidea/parasitology;
Antigens, Helminth/genetics/immunology/metabolism;
Animals;
Amino Acid Sequence
- From:The Korean Journal of Parasitology
2006;44(3):187-196
- CountryRepublic of Korea
- Language:English
-
Abstract:
The mammalian trematode Paragonimus westermani is a typical digenetic parasite, which can cause paragonimiasis in humans. Host tissues and blood cells are important sources of nutrients for development, growth and reproduction of P. westermani. In this study, a cDNA clone encoding a 47 kDa hemoglobinase of P. westermani was characterized by sequencing analysis, and its localization was investigated immunohistochemically. The phylogenetic tree prepared based on the hemoglobinase gene showed high homology with hemoglobinases of Fasciola hepatica and Schistosoma spp. Moreover, recombinant P. westermani hemoglobinase degradaded human hemoglobin at acidic pH (from 3.0 to 5.5) and its activity was almost completely inhibited by E-64, a cysteine proteinase inhibitor. Immunohistochemical studies showed that P. westermani hemoglobinase was localized in the epithelium of the adult worm intestine implying that the protein has a specific function. These observations suggest that hemoglobinase may act as a digestive enzyme for acquisition of nutrients from host hemoglobin. Further investigations may provide insights into hemoglobin catabolism in P. westermani.
