Serpin from Eudiplozoon nipponicum

a 2017

Serpin from Eudiplozoon nipponicum

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

Basic information

Original name

Serpin from 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

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:

ECIP - European Centre of IchthyoParasitology

RIV identification code

RIV/00216224:14310/17:00094922

Organization unit

Faculty of Science

ISBN

978-80-210-8666-1

Keywords in English

serpin; parasite; eudiplozoon; interaction host-parasite; inhibition

Změněno: 11/9/2017 15:48, Mgr. Pavel Roudnický, Ph.D.

Abstract

V originále

The properties of proteins (e.g. functions) of the members from the family Monogenea are among the less investigated in whole phylum Platyhelminthes. We chose Eudiplozoon nipponicum as our experimental organism to address this issue and complete the mosaic of its functional proteins equipment. E. nipponicum (family 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 peptidase activity related to many 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. 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 of E. nipponicum and investigated properties of its recombinant form – molecular and biochemical characterization was performed. The tertiary structure was predicted, antigenic properties evaluated and inhibitory effect measured.

Links

GBP505/12/G112, research and development project

Name: ECIP - Evropské centrum ichtyoparazitologie

Investor: Czech Science Foundation

Citovat

ROUDNICKÝ, Pavel, Jiří VOREL, Jana ILGOVÁ, Libor MIKEŠ, Lucie JEDLIČKOVÁ, John DALTON, Jan DVOŘÁK, Lubomír JANDA, Adam NOREK, Milan GELNAR and Martin KAŠNÝ. Serpin from Eudiplozoon nipponicum. In 8th International Symposium on Monogenea. 2017. ISBN 978-80-210-8666-1.

@proceedings{1389088,
   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 = {8th International Symposium on Monogenea},
   keywords = {serpin; parasite; eudiplozoon; interaction host-parasite; inhibition},
   language = {eng},
   isbn = {978-80-210-8666-1},
   title = {Serpin from Eudiplozoon nipponicum},
   url = {http://ecip.cz/news/4},
   year = {2017}
}

TY  - CONF
ID  - 1389088
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 from Eudiplozoon nipponicum
SN  - 9788021086661
KW  - serpin
KW  - parasite
KW  - eudiplozoon
KW  - interaction host-parasite
KW  - inhibition
UR  - http://ecip.cz/news/4
L2  - http://ecip.cz/news/4
N2  - The properties of proteins (e.g. functions) of the members from the family Monogenea are among the less investigated in whole phylum Platyhelminthes. We chose Eudiplozoon nipponicum as our experimental organism to address this issue and complete the mosaic of its functional proteins equipment. E. nipponicum (family 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 peptidase activity related to many 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. 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 of E. nipponicum and investigated properties of its recombinant form – molecular and biochemical characterization was performed. The tertiary structure was predicted, antigenic properties evaluated and inhibitory effect measured.
ER  -

ROUDNICKÝ, Pavel, Jiří VOREL, Jana ILGOVÁ, Libor MIKEŠ, Lucie JEDLIČKOVÁ, John DALTON, Jan DVOŘÁK, Lubomír JANDA, Adam NOREK, Milan GELNAR and Martin KAŠNÝ. Serpin from Eudiplozoon nipponicum. In \textit{8th International Symposium on Monogenea}. 2017. ISBN~978-80-210-8666-1.

Detailed Information on Publication Record