Journal
EXPERIMENTAL PARASITOLOGY
Volume 127, Issue 3, Pages 693-701Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.exppara.2010.11.005
Keywords
Cestode; Echinococcus multilocularis; Metacestode; Cathepsin B-like peptidase; Recombinant enzyme; Host proteins
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Funding
- Japan Society for the Promotion of Science (JSPS) [21256003]
- JSPS-Asia/Africa Science Platform Fund
- Ministry of Education, Japan
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Cysteine peptidases have potent activities in the pathogenesis of various parasitic infections, and are considered as targets for chemotherapy and antigens for vaccine. In this study, two cathepsin B-like cysteine peptidases (EmCBP1 and EmCBP2) from Echinococcus multilocularis metacestodes were identified and characterized. Immunoblot analyses demonstrated that EmCBP1 and EmCBP2 were present in excretory/secretory products and extracts of E. multilocularis metacestodes. By immunohistochemistry. EmCBP1 and EmCBP2 were shown to localize to the germinal layer, the brood capsule and the protoscolex. Recombinant EmCBP1 and EmCBP2 expressed in Pichia pastoris, at optimum pH 5.5, exhibited substrate preferences for Z-Phe-Arg-MCA. Z-Val-Val-Arg-MCA, and Z-Leu-Arg-MCA, and low levels of hydrolysis of Z-Arg-Arg-MCA. Furthermore, recombinant enzymes degraded IgG, albumin, type I and IV collagens, and fibronectin. These results suggested that EmCBP1 and EmCBP2 may play key roles in protein digestion for parasites' nutrition and in parasite-host interactions. (C) 2010 Elsevier Inc. All rights reserved.
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