Identification and partial characterization of a novel serpin
from Eudiplozoon nipponicum (Monogenea, Polyopisthocotylea)

J 2018

Identification and partial characterization of a novel serpin from Eudiplozoon nipponicum (Monogenea, Polyopisthocotylea)

ROUDNICKÝ, Pavel; Jiří VOREL; Jana ILGOVÁ; Michal BENOVICS; Adam NOREK et. al.

Základní údaje

Originální název

Identification and partial characterization of a novel serpin from Eudiplozoon nipponicum (Monogenea, Polyopisthocotylea)

Autoři

ROUDNICKÝ, Pavel; Jiří VOREL; Jana ILGOVÁ; Michal BENOVICS; Adam NOREK; Lucie JEDLIČKOVÁ; Libor MIKEŠ; David POTĚŠIL; Zbyněk ZDRÁHAL; Jan DVOŘÁK; Milan GELNAR a Martin KAŠNÝ

Vydání

Parasite, 2018, 1252-607X

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10613 Zoology

Stát vydavatele

Francie

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 1.958

Kód RIV

RIV/00216224:14310/18:00101521

Organizační jednotka

Přírodovědecká fakulta

DOI

https://doi.org/10.1051/parasite/2018062

UT WoS

000452194000001

EID Scopus

2-s2.0-85058180856

Klíčová slova anglicky

Eudiplozoon nipponicum; fish parasite; monogenea; Platyhelminths; serpin; inhibitor

Štítky

CF PROT

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 26. 3. 2019 12:53, Mgr. Lucie Jarošová, DiS.

Anotace

V originále

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.

Návaznosti

GAP506/12/1258, projekt VaV

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

Investor: Grantová agentura ČR, Interakce hostitel-parazit u krevsajících diplozoidních monogeneí: Výzkum vysoce specializovaných adaptací k parazitismu

GBP505/12/G112, projekt VaV

Název: ECIP - Evropské centrum ichtyoparazitologie

Investor: Grantová agentura ČR, ECIP - Evropské centrum ichtyoparazitologie

LM2015043, projekt VaV

Název: Česká infrastruktura pro integrativní strukturní biologii (Akronym: CIISB)

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, Czech Infrastructure for Integrative Structural Biology

LM2015085, projekt VaV

Název: CERIT Scientific Cloud (Akronym: CERIT-SC)

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, CERIT Scientific Cloud

MUNI/A/1362/2016, interní kód MU

Název: Biologická diverzita – analýzy biologických systémů různých úrovní a na různých škálách prostředí

Investor: Masarykova univerzita, Biologická diverzita – analýzy biologických systémů různých úrovní a na různých škálách prostředí, DO R. 2020_Kategorie A - Specifický výzkum - Studentské výzkumné projekty

Citovat

ROUDNICKÝ, Pavel; Jiří VOREL; Jana ILGOVÁ; Michal BENOVICS; Adam NOREK; Lucie JEDLIČKOVÁ; Libor MIKEŠ; David POTĚŠIL; Zbyněk ZDRÁHAL; Jan DVOŘÁK; Milan GELNAR a Martin KAŠNÝ. Identification and partial characterization of a novel serpin from Eudiplozoon nipponicum (Monogenea, Polyopisthocotylea). Parasite. 2018, roč. 25, DEC, s. "61", 13 s. ISSN 1252-607X. Dostupné z: https://doi.org/10.1051/parasite/2018062.

@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 = {https://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 a Martin KAŠNÝ. Identification and partial characterization of a novel serpin from Eudiplozoon nipponicum (Monogenea, Polyopisthocotylea). \textit{Parasite}. 2018, roč.~25, DEC, s.~''61'', 13 s. ISSN~1252-607X. Dostupné z: https://doi.org/10.1051/parasite/2018062.

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