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.

Základní údaje

Originální název

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

Název česky

Detailní pohled na sekretom a transkriptom Trichinella spiralis a Trichinela pseudospiralis

Autoři

ŠKORPÍKOVÁ, Lucie (203 Česká republika, domácí), Jana ILGOVÁ (703 Slovensko), David POTĚŠIL (203 Česká republika), Zbyněk ZDRÁHAL (203 Česká republika), Martin DEMKO (703 Slovensko), Jan OPPELT (203 Česká republika), Milan GELNAR (203 Česká republika) a Martin KAŠNÝ (203 Česká republika)

Vydání

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

Další údaje

Jazyk

angličtina

Typ výsledku

Vyžádané přednášky

Obor

10600 1.6 Biological sciences

Stát vydavatele

Česká republika

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Kód RIV

RIV/00216224:14310/16:00090454

Organizační jednotka

Přírodovědecká fakulta

Klíčová slova anglicky

Eudiplozoon; serpin

Příznaky

Mezinárodní význam

Změněno: 24. 3. 2017 22:32, RNDr. Martin Kašný, Ph.D.

Anotace

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.

Návaznosti

MUNI/A/1484/2014, interní kód MU

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

Investor: Masarykova univerzita, Analýzy diverzity biologických systémů různých úrovní a na různých škálách terestrického a akvatického prostředí, DO R. 2020_Kategorie A - Specifický výzkum - Studentské výzkumné projekty

Citovat

ŠKORPÍKOVÁ, Lucie, Jana ILGOVÁ, David POTĚŠIL, Zbyněk ZDRÁHAL, Martin DEMKO, Jan OPPELT, Milan GELNAR a 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 a 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.

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