k 2017

SERPIN, A KEY MOLECULE IN THE LIFE OF EUDIPLOZOON NIPPONICUM?!

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

Základní údaje

Originální název

SERPIN, A KEY MOLECULE IN THE LIFE OF EUDIPLOZOON NIPPONICUM?!

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

23rd Helminthological Days, 2017

Další údaje

Jazyk

angličtina

Typ výsledku

Prezentace na konferencích

Obor

10600 1.6 Biological sciences

Stát vydavatele

Slovensko

Utajení

není předmětem státního či obchodního tajemství

Kód RIV

RIV/00216224:14310/17:00094753

Organizační jednotka

Přírodovědecká fakulta

ISBN

978-80-968473-8-9

Klíčová slova česky

serpin, parazit, eudiplozoon, interakce parazit-hostitel, inhibice

Klíčová slova anglicky

serpin; parasite; eudiplozoon; interaction host-parasite; inhibition
Změněno: 25. 8. 2017 09:47, Mgr. Pavel Roudnický, Ph.D.

Anotace

V originále

Eudiplozoon nipponicum (family Diplozoidae, Polyopisthocotylea) is hematophagous ectoparasite from the gills of common carp (Cyprinus carpio). The properties of proteins (e.g. functions) of the members from the family Monogenea are among the less investigated in whole phylum Platyhelminthes. During the previous experimental work of our colleagues, we obtained data concerning the important functional molecules produced by E. nipponicum (e.g. endopeptidases cathepsins L, B and D). Some of them occurred in excretory-secretory products, which indicates their possible participation in host-parasite interaction and some of them were proved to be part of feeding mechanisms. The main aim of our current work is to understand the regulation related to peptidase activity; the peptidase protein inhibitors, such as also serpins, could play a key role in this process. Serpins of vertebrates are known as important regulators of the coagulation cascade, complement, fibrinolysis, angiogenesis, inflammation etc. They possess typical conserved domains and a reactive central loop binding to the active site of peptidase. The inhibition, mediated by serpins, is typically irreversible, comprising conformational changes in serpin molecule leading to distortion of peptidase tertiary structure. Except the inhibition, some of them may have other functions like e.g. protein transporters or chaperones and they are relatively abundant also in secretions, body lysates and genomes/transcriptomes of helminths. We identified serpin gene/protein in transcriptome/proteome of E. nipponicum, subsequently it was prepared in recombinant form and in regard to reveal its functions molecular and biochemical characterization was performed (e.g. prediction of tertiary structure, antigenic properties evaluation, measurement of inhibitory effect).

Návaznosti

GBP505/12/G112, projekt VaV
Název: ECIP - Evropské centrum ichtyoparazitologie
Investor: Grantová agentura ČR, ECIP - Evropské centrum ichtyoparazitologie