Major acid endopeptidases of the blood-feeding monogenean Eudiplozoon nipponicum (Heteronchoinea: Diplozoidae)

Investor logo
Investor logo
Investor logo

Warning

This publication doesn't include Faculty of Education. It includes Central European Institute of Technology. Official publication website can be found on muni.cz.
Authors

JEDLIČKOVÁ Lucie DVOŘÁKOVÁ Hana KAŠNÝ Martin ILGOVÁ Jana POTĚŠIL David ZDRÁHAL Zbyněk MIKEŠ Libor

Year of publication 2016
Type Article in Periodical
Magazine / Source Parasitology
MU Faculty or unit

Central European Institute of Technology

Citation
Web http://journals.cambridge.org/action/displayAbstract?fromPage=online&aid=10245366&fileId=S0031182015001808
Doi http://dx.doi.org/10.1017/S0031182015001808
Field Zoology
Keywords cysteine peptidase; aspartic peptidase; protease; haematophagous monogenea; cathepsin L; cathepsin B; cathepsin D; fish parasite; common carp
Description In parasitic flatworms, acid endopeptidases are involved in crucial processes, including digestion, invasion, interactions with the host immune system, etc. In haematophagous monogeneans, however, no solid information has been available about the occurrence of these enzymes. Here we aimed to identify major cysteine and aspartic endopeptidase activities in Eudiplozoon nipponicum, an invasive haematophagous parasite of common carp. Employing biochemical, proteomic and molecular tools, we found that cysteine peptidase activities prevailed in soluble protein extracts and excretory/secretory products (ESP) of E. nipponicum; the major part was cathepsin L-like in nature supplemented with cathepsin B-like activity. Significant activity of the aspartic cathepsin D also occurred in soluble protein extracts. The degradation of haemoglobin in the presence of ESP and worm protein extracts was completely inhibited by a combination of cysteine and aspartic peptidase inhibitors, and diminished by particular cathepsin L, B and D inhibitors. Mass spectrometry revealed several tryptic peptides in ESP matching to two translated sequences of cathepsin L genes, which were amplified from cDNA of E. nipponicum and bioinformatically annotated. The dominance of cysteine peptidases of cathepsin L type in E. nipponicum resembles the situation in, e.g. fasciolid trematodes.
Related projects:

You are running an old browser version. We recommend updating your browser to its latest version.