Deep insight into secretome and transcriptome of Trichinella
spiralis and Trichinela pseudospiralis

p 2016

Deep insight into secretome and transcriptome of Trichinella spiralis and Trichinela pseudospiralis

ŠKORPÍKOVÁ, Lucie, Jana ILGOVÁ, David POTĚŠIL, Zbyněk ZDRÁHAL, Martin DEMKO et. al.

Basic information

Original name

Deep insight into secretome and transcriptome of Trichinella spiralis and Trichinela pseudospiralis

Name in Czech

Detailní pohled na sekretom a transkriptom Trichinella spiralis a Trichinela pseudospiralis

Authors

ŠKORPÍKOVÁ, Lucie (203 Czech Republic, belonging to the institution), Jana ILGOVÁ (703 Slovakia), David POTĚŠIL (203 Czech Republic), Zbyněk ZDRÁHAL (203 Czech Republic), Martin DEMKO (703 Slovakia), Jan OPPELT (203 Czech Republic), Milan GELNAR (203 Czech Republic) and Martin KAŠNÝ (203 Czech Republic)

Edition

EMOP XII – the 12th European Multicolloquium of Parasitology, 2016

Other information

Language

English

Type of outcome

Vyžádané přednášky

Field of Study

10600 1.6 Biological sciences

Country of publisher

Czech Republic

Confidentiality degree

není předmětem státního či obchodního tajemství

References:

URL

RIV identification code

RIV/00216224:14310/16:00090454

Organization unit

Faculty of Science

Keywords in English

Eudiplozoon; serpin

Abstract

V originále

By adoption of homology searches of RNA 158 753 271 bases/223 887 transcripts the 9757 contigs (>1 kb) were assembled and particular protein molecules in E. nipponicum transcriptome data were identified, e.g. peptidases/inhibitors; 29 contigs of cysteine peptidases (e.g. cathepsin L) and 7 contigs of their inhibitors (e.g. cystatins); 12 contigs of serine peptidases (e.g. cathepsin A) and 7 contigs of their inhibitors (e.g. serpin). Employing biochemical, proteomic and molecular tools, we found that cysteine peptidase activities prevailed in soluble protein extracts and excretory/secretory (E/S) products of E. nipponicum and the major part of activity was related to cathepsin L-like. Mass spectrometry revealed several tryptic peptides in E/S products matching to two translated sequences of cathepsin L genes. The dominance of cysteine peptidases of cathepsin L type in E. nipponicum resembles the situation in, e.g., fasciolid trematodes. The cathepsin L3 was cloned and expressed in both bacterial and yeasts expression systems. The recombinant enzyme was purified on Ni-NTA agarose column and the experiments focused on its molecular/biochemical properties were started.

Links

MUNI/A/1484/2014, interní kód MU

Name: Analýzy diverzity biologických systémů různých úrovní a na různých škálách terestrického a akvatického prostředí (Acronym: BIDA4)

Investor: Masaryk University, Category A

Citovat

ŠKORPÍKOVÁ, Lucie, Jana ILGOVÁ, David POTĚŠIL, Zbyněk ZDRÁHAL, Martin DEMKO, Jan OPPELT, Milan GELNAR and Martin KAŠNÝ. Deep insight into secretome and transcriptome of Trichinella spiralis and Trichinela pseudospiralis. In EMOP XII – the 12th European Multicolloquium of Parasitology. 2016.

@misc{1350531,
   author = {Škorpíková, Lucie and Ilgová, Jana and Potěšil, David and Zdráhal, Zbyněk and Demko, Martin and Oppelt, Jan and Gelnar, Milan and Kašný, Martin},
   booktitle = {EMOP XII – the 12th European Multicolloquium of Parasitology},
   keywords = {Eudiplozoon; serpin},
   language = {eng},
   title = {Deep insight into secretome and transcriptome of Trichinella spiralis and Trichinela pseudospiralis},
   url = {http://congress.utu.fi/emop2016/programme.php},
   year = {2016}
}

TY  - SLIDE
ID  - 1350531
AU  - Škorpíková, Lucie - Ilgová, Jana - Potěšil, David - Zdráhal, Zbyněk - Demko, Martin - Oppelt, Jan - Gelnar, Milan - Kašný, Martin
PY  - 2016
TI  - Deep insight into secretome and transcriptome of Trichinella spiralis and Trichinela pseudospiralis
KW  - Eudiplozoon
KW  - serpin
UR  - http://congress.utu.fi/emop2016/programme.php
N2  - By adoption of homology searches of RNA 158 753 271 bases/223 887 transcripts the 9757 contigs (>1 kb) were assembled and particular protein molecules in E. nipponicum transcriptome data were identified, e.g. peptidases/inhibitors; 29 contigs of cysteine peptidases (e.g. cathepsin L) and 7 contigs of their inhibitors (e.g. cystatins); 12 contigs of serine peptidases (e.g. cathepsin A) and 7 contigs of their inhibitors (e.g. serpin). Employing biochemical, proteomic and molecular tools, we found that cysteine peptidase activities prevailed in soluble protein extracts and excretory/secretory (E/S) products of E. nipponicum and the major part of activity was related to cathepsin L-like. Mass spectrometry revealed several tryptic peptides in E/S products matching to two translated sequences of cathepsin L genes. The dominance of cysteine peptidases of cathepsin L type in E. nipponicum resembles the situation in, e.g., fasciolid trematodes. The cathepsin L3 was cloned and expressed in both bacterial and yeasts expression systems. The recombinant enzyme was purified on Ni-NTA agarose column and the experiments focused on its molecular/biochemical properties were started.
ER  -

ŠKORPÍKOVÁ, Lucie, Jana ILGOVÁ, David POTĚŠIL, Zbyněk ZDRÁHAL, Martin DEMKO, Jan OPPELT, Milan GELNAR and Martin KAŠNÝ. Deep insight into secretome and transcriptome of Trichinella spiralis and Trichinela pseudospiralis. In \textit{EMOP XII – the 12th European Multicolloquium of Parasitology}. 2016.

Detailed Information on Publication Record