Detailed Information on Publication Record
2017
A novel type I cystatin of parasite origin with atypical legumain-binding domain
ILGOVÁ, Jana, Lucie JEDLICKOVA, Hana DVORAKOVA, Michal BENOVICS, Libor MIKEŠ et. al.Basic information
Original name
A novel type I cystatin of parasite origin with atypical legumain-binding domain
Authors
ILGOVÁ, Jana (703 Slovakia, guarantor, belonging to the institution), Lucie JEDLICKOVA (203 Czech Republic), Hana DVORAKOVA (203 Czech Republic), Michal BENOVICS (703 Slovakia, belonging to the institution), Libor MIKEŠ (203 Czech Republic), Lubomír JANDA (203 Czech Republic, belonging to the institution), Jiří VOREL (203 Czech Republic, belonging to the institution), Pavel ROUDNICKÝ (203 Czech Republic, belonging to the institution), David POTĚŠIL (203 Czech Republic, belonging to the institution), Zbyněk ZDRÁHAL (203 Czech Republic, belonging to the institution), Milan GELNAR (203 Czech Republic, belonging to the institution) and Martin KAŠNÝ (203 Czech Republic, belonging to the institution)
Edition
Scientific Reports, LONDON, NATURE PUBLISHING GROUP, 2017, 2045-2322
Other information
Language
English
Type of outcome
Článek v odborném periodiku
Field of Study
10600 1.6 Biological sciences
Country of publisher
United Kingdom of Great Britain and Northern Ireland
Confidentiality degree
není předmětem státního či obchodního tajemství
References:
Impact factor
Impact factor: 4.122
RIV identification code
RIV/00216224:14310/17:00095334
Organization unit
Faculty of Science
UT WoS
000417796000046
Keywords (in Czech)
cystatin; inhibitor; Eudiplozoon nippponicum; Monogenea; legumain; papain; inhibice
Keywords in English
cystatin; inhibitor; Eudiplozoon nippponicum; Monogenea; legumain; papain; inhibition
Tags
International impact, Reviewed
Změněno: 20/4/2020 11:21, Mgr. Michal Benovics, Ph.D.
Abstract
V originále
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.
Links
| GAP506/12/1258, research and development project |
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| GBP505/12/G112, research and development project |
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| LM2015043, research and development project |
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| LM2015085, research and development project |
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| LQ1601, research and development project |
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| MUNI/A/1362/2016, interní kód MU |
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