Detailed Information on Publication Record
2017
Inhibition of proteolysis by the hematophagous Eudiplozoon nipponicum
ILGOVÁ, Jana, Lucie JEDLIČKOVÁ, Hana DVOŘÁKOVÁ, Libor MIKEŠ, Michal BENOVICS et. al.Basic information
Original name
Inhibition of proteolysis by the hematophagous Eudiplozoon nipponicum
Authors
ILGOVÁ, Jana (703 Slovakia, belonging to the institution), Lucie JEDLIČKOVÁ (203 Czech Republic), Hana DVOŘÁKOVÁ (203 Czech Republic), Libor MIKEŠ (203 Czech Republic), Michal BENOVICS (703 Slovakia, belonging to the institution), Pavel ROUDNICKÝ (203 Czech Republic, belonging to the institution), Jiří VOREL (203 Czech Republic, belonging to the institution), Libor VOJTEK (203 Czech Republic, belonging to the institution), Pavel HYRŠL (203 Czech Republic, belonging to the institution), Jiří SALÁT (203 Czech Republic, belonging to the institution), Milan GELNAR (203 Czech Republic, belonging to the institution) and Martin KAŠNÝ (203 Czech Republic, belonging to the institution)
Edition
8th International Symposium on Monogenea, 2017
Other information
Language
English
Type of outcome
Konferenční abstrakt
Field of Study
10600 1.6 Biological sciences
Country of publisher
Czech Republic
Confidentiality degree
není předmětem státního či obchodního tajemství
References:
RIV identification code
RIV/00216224:14310/17:00094966
Organization unit
Faculty of Science
ISBN
978-80-210-8666-1
Keywords in English
stefin; parasite; eudiplozoon; interaction host-parasite; inhibition;
Změněno: 24/9/2017 17:39, Mgr. Michal Benovics, Ph.D.
Abstract
V originále
Eudiplozoon nipponicum (Monogenea: Diplozoidae) is an obligatory hematophagous parasite of the common carp (Cyprinus carpio). The blood degradation by this species involves a cascade of cysteine and aspartic proteases hypothetically regulated by protease inhibitors (e.g. cystatins and stefins). These inhibitory molecules are also known to have impact on immunomodulation of the host and the repair of its tissue damaged by the parasite. Our study aims to reveal the biological function of the stefin of E. nipponicum which was detected in the transcriptome and excretory-secretory products of adult individuals. We prepared recombinant form of E. nipponicum stefin (rEnStef) in E. coli BL21 bacterial strain using pET19b expression plasmid vector. By adoption of fluorometric assay we observed efficient inhibition of cysteine peptidases (cathepsins L and B from E. nipponicum and mouse cathepsin L) via its conserved papain-binding domain. Surprisingly legumain (asparaginyl endopeptidase) inhibition was detected probably due to legumain-binding domain, untypical for stefins. rEnStef blocked proteolytic degradation of hemoglobin mediated by cysteine peptidases in the excretory-secretory products, soluble protein extracts from E. nipponicum and by recombinant cathepsins L3 and B of E. nipponicum, which manifests its role in blood digestion. rEnStef any effect on the activation of complement in carp’s plasma or oxidative burst in full blood studied using luminol-enhanced chemiluminescence. Significant downregulation of selected cytokines (IL-1beta, IL-8, TNF-alfa, IL-6 and IL-10) by LPS stimulated porcine alveolar macrophages and monocyte derived macrophages caused by rEnStef might indicate possible role of E. nipponicum stefin in immunomodulation of the host.
Links
GBP505/12/G112, research and development project |
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