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

J 2016

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

JEDLIČKOVÁ, Lucie, Hana DVOŘÁKOVÁ, Martin KAŠNÝ, Jana ILGOVÁ, David POTĚŠIL et. al.

Basic information

Original name

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

Authors

JEDLIČKOVÁ, Lucie (203 Czech Republic), Hana DVOŘÁKOVÁ (203 Czech Republic), Martin KAŠNÝ (203 Czech Republic, guarantor, belonging to the institution), Jana ILGOVÁ (703 Slovakia, belonging to the institution), David POTĚŠIL (203 Czech Republic, belonging to the institution), Zbyněk ZDRÁHAL (203 Czech Republic, belonging to the institution) and Libor MIKEŠ (203 Czech Republic)

Edition

Parasitology, NEW YORK, CAMBRIDGE UNIV PRESS, 2016, 0031-1820

Other information

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

10600 1.6 Biological sciences

Country of publisher

United States of America

Confidentiality degree

není předmětem státního či obchodního tajemství

References:

URL

Impact factor

Impact factor: 2.620

RIV identification code

RIV/00216224:14740/16:00087768

Organization unit

Central European Institute of Technology

DOI

http://dx.doi.org/10.1017/S0031182015001808

UT WoS

000373393500010

Keywords in English

cysteine peptidase; aspartic peptidase; protease; haematophagous monogenea; cathepsin L; cathepsin B; cathepsin D; fish parasite; common carp

Abstract

V originále

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.

Links

ED1.1.00/02.0068, research and development project

Name: CEITEC - central european institute of technology

GAP506/12/1258, research and development project

Name: Interakce hostitel-parazit u krevsajících diplozoidních monogeneí: Výzkum vysoce specializovaných adaptací k parazitismu

Investor: Czech Science Foundation

GBP206/12/G151, research and development project

Name: Centrum nových přístupů k bioanalýze a molekulární diagnostice

MUNI/A/1484/2014, interní kód MU

Name: Analýzy diverzity biologických systémů různých úrovní a na různých škálách terestrického a akvatického prostředí (Acronym: BIDA4)

Investor: Masaryk University, Category A

Citovat

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). 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.

@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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