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.
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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
Original language English
Type of outcome Requested lectures
Field of Study 10600 1.6 Biological sciences
Country of publisher Czech Republic
Confidentiality degree is not subject to a state or trade secret
WWW URL
RIV identification code RIV/00216224:14310/16:00090454
Organization unit Faculty of Science
Keywords in English Eudiplozoon; serpin
Tags International impact
Changed by Changed by: RNDr. Martin Kašný, Ph.D., učo 11259. Changed: 24/3/2017 22:32.
Abstract
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 MUName: Analýzy diverzity biologických systémů různých úrovní a na různých škálách terestrického a akvatického prostředí (Acronym: BIDA4)
Investor: Masaryk University, Category A
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