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@article{1484114,
author = {Roudnický, Pavel and Vorel, Jiří and Ilgová, Jana and Benovics, Michal and Norek, Adam and Jedličková, Lucie and Mikeš, Libor and Potěšil, David and Zdráhal, Zbyněk and Dvořák, Jan and Gelnar, Milan and Kašný, Martin},
article_number = {DEC},
doi = {http://dx.doi.org/10.1051/parasite/2018062},
keywords = {Eudiplozoon nipponicum; fish parasite; monogenea; Platyhelminths; serpin; inhibitor},
language = {eng},
issn = {1252-607X},
journal = {Parasite},
title = {Identification and partial characterization of a novel serpin from Eudiplozoon nipponicum (Monogenea, Polyopisthocotylea)},
url = {https://www.parasite-journal.org/articles/parasite/abs/2018/01/parasite180126/parasite180126.html},
volume = {25},
year = {2018}
}
TY - JOUR
ID - 1484114
AU - Roudnický, Pavel - Vorel, Jiří - Ilgová, Jana - Benovics, Michal - Norek, Adam - Jedličková, Lucie - Mikeš, Libor - Potěšil, David - Zdráhal, Zbyněk - Dvořák, Jan - Gelnar, Milan - Kašný, Martin
PY - 2018
TI - Identification and partial characterization of a novel serpin from Eudiplozoon nipponicum (Monogenea, Polyopisthocotylea)
JF - Parasite
VL - 25
IS - DEC
SP - "61"
EP - "61"
SN - 1252607X
KW - Eudiplozoon nipponicum
KW - fish parasite
KW - monogenea
KW - Platyhelminths
KW - serpin
KW - inhibitor
UR - https://www.parasite-journal.org/articles/parasite/abs/2018/01/parasite180126/parasite180126.html
L2 - https://www.parasite-journal.org/articles/parasite/abs/2018/01/parasite180126/parasite180126.html
N2 - Background: Serpins are a superfamily of serine peptidase inhibitors that participate in the regulation of many physiological and cell peptidase-mediated processes in all organisms (e.g. in blood clotting, complement activation, fibrinolysis, inflammation, and programmed cell death). It was postulated that in the blood-feeding members of the monogenean family Diplozoidae, serpins could play an important role in the prevention of thrombus formation, activation of complement, inflammation in the host, and/or in the endogenous regulation of protein degradation. Results: In silico analysis showed that the DNA and primary protein structures of serpin from Eudiplozoon nipponicum (EnSerp1) are similar to other members of the serpin superfamily. The inhibitory potential of EnSerp1 on four physiologically-relevant serine peptidases (trypsin, factor Xa, kallikrein, and plasmin) was demonstrated and its presence in the worm’s excretory-secretory products (ESPs) was confirmed. Conclusion: EnSerp1 influences the activity of peptidases that play a role in blood coagulation, fibrinolysis, and complement activation. This inhibitory potential, together with the serpin’s presence in ESPs, suggests that it is likely involved in host-parasite interactions and could be one of the molecules involved in the control of feeding and prevention of inflammatory responses.
ER -
ROUDNICKÝ, Pavel, Jiří VOREL, Jana ILGOVÁ, Michal BENOVICS, Adam NOREK, Lucie JEDLIČKOVÁ, Libor MIKEŠ, David POTĚŠIL, Zbyněk ZDRÁHAL, Jan DVOŘÁK, Milan GELNAR and Martin KAŠNÝ. Identification and partial characterization of a novel serpin from Eudiplozoon nipponicum (Monogenea, Polyopisthocotylea). \textit{Parasite}. 2018, vol.~25, DEC, p.~''61'', 13 pp. ISSN~1252-607X. Available from: https://dx.doi.org/10.1051/parasite/2018062.
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