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

ROUDNICKÝ, Pavel, Jiří VOREL, Jana ILGOVÁ, Libor MIKEŠ, Lucie JEDLIČKOVÁ, John DALTON, Jan DVOŘÁK, Lubomír JANDA, Adam NOREK, Milan GELNAR and Martin KAŠNÝ. SERPIN, A KEY MOLECULE IN THE LIFE OF EUDIPLOZOON NIPPONICUM?! In 23rd Helminthological Days. 2017. ISBN 978-80-968473-8-9.

Basic information

• Original name: SERPIN, A KEY MOLECULE IN THE LIFE OF EUDIPLOZOON NIPPONICUM?!
• Authors: ROUDNICKÝ, Pavel (203 Czech Republic, guarantor, belonging to the institution), Jiří VOREL (203 Czech Republic, belonging to the institution), Jana ILGOVÁ (703 Slovakia, belonging to the institution), Libor MIKEŠ (203 Czech Republic), Lucie JEDLIČKOVÁ (203 Czech Republic), John DALTON (372 Ireland), Jan DVOŘÁK (203 Czech Republic), Lubomír JANDA (203 Czech Republic), Adam NOREK (203 Czech Republic), Milan GELNAR (203 Czech Republic, belonging to the institution) and Martin KAŠNÝ (203 Czech Republic, belonging to the institution).
• Edition: 23rd Helminthological Days, 2017.

Other information

• Original language: English
• Type of outcome: Presentations at conferences
• Field of Study: 10600 1.6 Biological sciences
• Country of publisher: Slovakia
• Confidentiality degree: is not subject to a state or trade secret
• WWW: Programme & Abstracts
• RIV identification code: RIV/00216224:14310/17:00094753
• Organization unit: Faculty of Science
• ISBN: 978-80-968473-8-9
• Keywords (in Czech): serpin, parazit, eudiplozoon, interakce parazit-hostitel, inhibice
• Keywords in English: serpin; parasite; eudiplozoon; interaction host-parasite; inhibition

Abstract

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).

Links

• GBP505/12/G112, research and development project: Name: ECIP - Evropské centrum ichtyoparazitologie

Investor: Czech Science Foundation