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@article{1324014,
author = {Jedličková, Lucie and Dvořáková, Hana and Kašný, Martin and Ilgová, Jana and Potěšil, David and Zdráhal, Zbyněk and Mikeš, Libor},
article_location = {NEW YORK},
article_number = {4},
doi = {http://dx.doi.org/10.1017/S0031182015001808},
keywords = {cysteine peptidase; aspartic peptidase; protease; haematophagous monogenea; cathepsin L; cathepsin B; cathepsin D; fish parasite; common carp},
language = {eng},
issn = {0031-1820},
journal = {Parasitology},
title = {Major acid endopeptidases of the blood-feeding monogenean Eudiplozoon nipponicum (Heteronchoinea: Diplozoidae)},
url = {http://journals.cambridge.org/action/displayAbstract?fromPage=online&aid=10245366&fileId=S0031182015001808},
volume = {143},
year = {2016}
}
TY - JOUR
ID - 1324014
AU - Jedličková, Lucie - Dvořáková, Hana - Kašný, Martin - Ilgová, Jana - Potěšil, David - Zdráhal, Zbyněk - Mikeš, Libor
PY - 2016
TI - Major acid endopeptidases of the blood-feeding monogenean Eudiplozoon nipponicum (Heteronchoinea: Diplozoidae)
JF - Parasitology
VL - 143
IS - 4
SP - 494-506
EP - 494-506
PB - CAMBRIDGE UNIV PRESS
SN - 00311820
KW - cysteine peptidase
KW - aspartic peptidase
KW - protease
KW - haematophagous monogenea
KW - cathepsin L
KW - cathepsin B
KW - cathepsin D
KW - fish parasite
KW - common carp
UR - http://journals.cambridge.org/action/displayAbstract?fromPage=online&aid=10245366&fileId=S0031182015001808
L2 - http://journals.cambridge.org/action/displayAbstract?fromPage=online&aid=10245366&fileId=S0031182015001808
N2 - 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.
ER -
JEDLIČKOVÁ, Lucie, Hana DVOŘÁKOVÁ, Martin KAŠNÝ, Jana ILGOVÁ, David POTĚŠIL, Zbyněk ZDRÁHAL and Libor MIKEŠ. Major acid endopeptidases of the blood-feeding monogenean Eudiplozoon nipponicum (Heteronchoinea: Diplozoidae). \textit{Parasitology}. NEW YORK: CAMBRIDGE UNIV PRESS, 2016, vol.~143, No~4, p.~494-506. ISSN~0031-1820. Available from: https://dx.doi.org/10.1017/S0031182015001808.
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