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; Jiří VOREL; Jana ILGOVÁ; Libor MIKEŠ; Lucie JEDLIČKOVÁ; John DALTON; Jan DVOŘÁK; Lubomír JANDA; Adam NOREK; Milan GELNAR a Martin KAŠNÝ
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
Označené pro přenos do RIV
Ano
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 |
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