Functions of novel serpin from Eudiplozoon nipponicum
(Monogenea).

a 2017

Functions of novel serpin from Eudiplozoon nipponicum (Monogenea).

ROUDNICKÝ, Pavel, Jiří VOREL, Jana ILGOVÁ, Libor MIKEŠ, Lucie JEDLIČKOVÁ et. al.

Základní údaje

Originální název

Functions of novel serpin from Eudiplozoon nipponicum (Monogenea).

Autoři

ROUDNICKÝ, Pavel (203 Česká republika, domácí), Jiří VOREL (203 Česká republika), Jana ILGOVÁ (703 Slovensko), Libor MIKEŠ (203 Česká republika), Lucie JEDLIČKOVÁ (203 Česká republika), John DALTON (372 Irsko), Jan DVOŘÁK (203 Česká republika), Lubomír JANDA (203 Česká republika), Adam NOREK (203 Česká republika), Milan GELNAR (203 Česká republika) a Martin KAŠNÝ (203 Česká republika)

Vydání

6th ECIP meeting, 2017

Další údaje

Jazyk

angličtina

Typ výsledku

Konferenční abstrakt

Obor

10600 1.6 Biological sciences

Stát vydavatele

Česká republika

Utajení

není předmětem státního či obchodního tajemství

Odkazy

ECIP - European Centre of IchthyoParasitology

Kód RIV

RIV/00216224:14310/17:00095268

Organizační jednotka

Přírodovědecká fakulta

ISBN

978-80-210-8799-6

Klíčová slova anglicky

diplozoon; monogenea; molecular interaction; serpin; haemocoagulation

Změněno: 15. 12. 2017 15:38, Mgr. Pavel Roudnický, Ph.D.

Anotace

V originále

The properties of functional proteins of the members from Monogenea are still poorly investigated. We chose Eudiplozoon nipponicum as our experimental organism to address this issue. E. nipponicum (Diplozoidae, Polyopisthocotylea) is hematophagous ectoparasite which lives on the gills of common carp (Cyprinus carpio). The main aim of our current work is to understand the regulation of host/parasite peptidase activity related to numerous physiological processes. Among the key regulatory factors could be included the peptidase inhibitors, such as serpins - serine peptidase inhibitors. These functional proteins are generally known as important regulators of the coagulation cascade, complement, fibrinolysis, angiogenesis, inflammation etc. In the transcriptome of E. nipponicum we identified serpin gene (EnS), prepared it in recombinant form (rEnS) and investigated its properties. We have been able to achieve approx. 70% of protein sample purity. Using western blot, the presence of purified rEnS in bacterial extracts and EnS in excretory-secretory products (ESP) was confirmed. These results were validated by mass spectrometry (MS). Fluorometric inhibition assays showed the rEnS ability to partially inhibit four serine peptidases (SP) playing a role in host-parasite interaction – digestion (trypsin), regulation of blood coagulation (factor Xa, plasmin) or tempering the inflammation (kallikrein). Due to properties mentioned above and presence of the serpin in ESP, we hypothesize that EnS might be one of the key factor of host-parasite interaction.

Návaznosti

GBP505/12/G112, projekt VaV

Název: ECIP - Evropské centrum ichtyoparazitologie

Investor: Grantová agentura ČR, ECIP - Evropské centrum ichtyoparazitologie

Citovat

ROUDNICKÝ, Pavel, Jiří VOREL, Jana ILGOVÁ, Libor MIKEŠ, Lucie JEDLIČKOVÁ, John DALTON, Jan DVOŘÁK, Lubomír JANDA, Adam NOREK, Milan GELNAR a Martin KAŠNÝ. Functions of novel serpin from Eudiplozoon nipponicum (Monogenea). In 6th ECIP meeting. 2017. ISBN 978-80-210-8799-6.

@proceedings{1399334,
   author = {Roudnický, Pavel and Vorel, Jiří and Ilgová, Jana and Mikeš, Libor and Jedličková, Lucie and Dalton, John and Dvořák, Jan and Janda, Lubomír and Norek, Adam and Gelnar, Milan and Kašný, Martin},
   booktitle = {6th ECIP meeting},
   keywords = {diplozoon; monogenea; molecular interaction; serpin; haemocoagulation},
   language = {eng},
   isbn = {978-80-210-8799-6},
   title = {Functions of novel serpin from Eudiplozoon nipponicum (Monogenea).},
   url = {http://ecip.cz/news/7},
   year = {2017}
}

TY  - CONF
ID  - 1399334
AU  - Roudnický, Pavel - Vorel, Jiří - Ilgová, Jana - Mikeš, Libor - Jedličková, Lucie - Dalton, John - Dvořák, Jan - Janda, Lubomír - Norek, Adam - Gelnar, Milan - Kašný, Martin
PY  - 2017
TI  - Functions of novel serpin from Eudiplozoon nipponicum (Monogenea).
SN  - 9788021087996
KW  - diplozoon
KW  - monogenea
KW  - molecular interaction
KW  - serpin
KW  - haemocoagulation
UR  - http://ecip.cz/news/7
L2  - http://ecip.cz/news/7
N2  - The properties of functional proteins of the members from Monogenea are still poorly investigated. We chose Eudiplozoon nipponicum as our experimental organism to address this issue. E. nipponicum (Diplozoidae, Polyopisthocotylea) is hematophagous ectoparasite which lives on the gills of common carp (Cyprinus carpio). The main aim of our current work is to understand the regulation of host/parasite peptidase activity related to numerous physiological processes. Among the key regulatory factors could be included the peptidase inhibitors, such as serpins - serine peptidase inhibitors. These functional proteins are generally known as important regulators of the coagulation cascade, complement, fibrinolysis, angiogenesis, inflammation etc. In the transcriptome of E. nipponicum we identified serpin gene (EnS), prepared it in recombinant form (rEnS) and investigated its properties. We have been able to achieve approx. 70% of protein sample purity. Using western blot, the presence of purified rEnS in bacterial extracts and EnS in excretory-secretory products (ESP) was confirmed. These results were validated by mass spectrometry (MS). Fluorometric inhibition assays showed the rEnS ability to partially inhibit four serine peptidases (SP) playing a role in host-parasite interaction – digestion (trypsin), regulation of blood coagulation (factor Xa, plasmin) or tempering the inflammation (kallikrein). Due to properties mentioned above and presence of the serpin in ESP, we hypothesize that EnS might be one of the key factor of host-parasite interaction.
ER  -

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