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@proceedings{1381223,
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 = {23rd Helminthological Days},
keywords = {serpin; parasite; eudiplozoon; interaction host-parasite; inhibition},
language = {eng},
isbn = {978-80-968473-8-9},
title = {SERPIN, A KEY MOLECULE IN THE LIFE OF EUDIPLOZOON NIPPONICUM?!},
url = {http://pau.saske.sk/helminthdays2017/programme/},
year = {2017}
}
TY - CONF
ID - 1381223
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 - SERPIN, A KEY MOLECULE IN THE LIFE OF EUDIPLOZOON NIPPONICUM?!
SN - 9788096847389
KW - serpin
KW - parasite
KW - eudiplozoon
KW - interaction host-parasite
KW - inhibition
UR - http://pau.saske.sk/helminthdays2017/programme/
L2 - http://pau.saske.sk/helminthdays2017/programme/
N2 - 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).
ER -
ROUDNICKÝ, Pavel, Jiří VOREL, Jana ILGOVÁ, Libor MIKEŠ, Lucie JEDLIČKOVÁ, John DALTON, Jan DVOŘÁK, Lubomír JANDA, Adam NOREK, Milan GELNAR a Martin KAŠNÝ. SERPIN, A KEY MOLECULE IN THE LIFE OF EUDIPLOZOON NIPPONICUM?! In \textit{23rd Helminthological Days}. 2017. ISBN~978-80-968473-8-9.
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