| ILGOVÁ, Jana, Lucie JEDLICKOVA, Hana DVORAKOVA, Michal BENOVICS, Libor MIKEŠ, Lubomír JANDA, Jiří VOREL, Pavel ROUDNICKÝ, David POTĚŠIL, Zbyněk ZDRÁHAL, Milan GELNAR a Martin KAŠNÝ. A novel type I cystatin of parasite origin with atypical legumain-binding domain. Scientific Reports. LONDON: NATURE PUBLISHING GROUP, 2017, roč. 7, December, s. nestránkováno, 12 s. ISSN 2045-2322. Dostupné z: https://dx.doi.org/10.1038/s41598-017-17598-2. |
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@article{1401828,
author = {Ilgová, Jana and Jedlickova, Lucie and Dvorakova, Hana and Benovics, Michal and Mikeš, Libor and Janda, Lubomír and Vorel, Jiří and Roudnický, Pavel and Potěšil, David and Zdráhal, Zbyněk and Gelnar, Milan and Kašný, Martin},
article_location = {LONDON},
article_number = {December},
doi = {http://dx.doi.org/10.1038/s41598-017-17598-2},
keywords = {cystatin; inhibitor; Eudiplozoon nippponicum; Monogenea; legumain; papain; inhibition},
language = {eng},
issn = {2045-2322},
journal = {Scientific Reports},
title = {A novel type I cystatin of parasite origin with atypical legumain-binding domain},
url = {https://www.nature.com/articles/s41598-017-17598-2},
volume = {7},
year = {2017}
}
TY - JOUR
ID - 1401828
AU - Ilgová, Jana - Jedlickova, Lucie - Dvorakova, Hana - Benovics, Michal - Mikeš, Libor - Janda, Lubomír - Vorel, Jiří - Roudnický, Pavel - Potěšil, David - Zdráhal, Zbyněk - Gelnar, Milan - Kašný, Martin
PY - 2017
TI - A novel type I cystatin of parasite origin with atypical legumain-binding domain
JF - Scientific Reports
VL - 7
IS - December
SP - nestránkováno
EP - nestránkováno
PB - NATURE PUBLISHING GROUP
SN - 20452322
KW - cystatin
KW - inhibitor
KW - Eudiplozoon nippponicum
KW - Monogenea
KW - legumain
KW - papain
KW - inhibition
UR - https://www.nature.com/articles/s41598-017-17598-2
L2 - https://www.nature.com/articles/s41598-017-17598-2
N2 - Parasite inhibitors of cysteine peptidases are known to influence a vast range of processes linked to a degradation of either the parasites' own proteins or proteins native to their hosts. We characterise a novel type I cystatin (stefin) found in a sanguinivorous fish parasite Eudiplozoon nipponicum (Platyhelminthes: Monogenea). We have identified a transcript of its coding gene in the transcriptome of adult worms. Its amino acid sequence is similar to other stefins except for containing a legumain-binding domain, which is in this type of cystatins rather unusual. As expected, the recombinant form of E. nipponicum stefin (rEnStef) produced in Escherichia coli inhibits clan CA peptidases - cathepsins L and B of the worm - via the standard papain-binding domain. It also blocks haemoglobinolysis by cysteine peptidases in the worm's excretory-secretory products and soluble extracts. Furthermore, we had confirmed its ability to inhibit clan CD asparaginyl endopeptidase (legumain). The presence of a native EnStef in the excretory-secretory products of adult worms, detected by mass spectrometry, suggests that this protein has an important biological function at the host-parasite interface. We discuss the inhibitor's possible role in the regulation of blood digestion, modulation of antigen presentation, and in the regeneration of host tissues.
ER -
ILGOVÁ, Jana, Lucie JEDLICKOVA, Hana DVORAKOVA, Michal BENOVICS, Libor MIKEŠ, Lubomír JANDA, Jiří VOREL, Pavel ROUDNICKÝ, David POTĚŠIL, Zbyněk ZDRÁHAL, Milan GELNAR a Martin KAŠNÝ. A novel type I cystatin of parasite origin with atypical legumain-binding domain. \textit{Scientific Reports}. LONDON: NATURE PUBLISHING GROUP, 2017, roč.~7, December, s.~nestránkováno, 12 s. ISSN~2045-2322. Dostupné z: https://dx.doi.org/10.1038/s41598-017-17598-2.
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