Publication details

A novel type I cystatin of parasite origin with atypical legumain-binding domain

Authors

ILGOVÁ Jana JEDLICKOVA Lucie DVORAKOVA Hana BENOVICS Michal MIKEŠ Libor JANDA Lubomír VOREL Jiří ROUDNICKÝ Pavel POTĚŠIL David ZDRÁHAL Zbyněk GELNAR Milan KAŠNÝ Martin

Year of publication 2017
Type Article in Periodical
Magazine / Source Scientific Reports
MU Faculty or unit

Faculty of Science

Citation
Web https://www.nature.com/articles/s41598-017-17598-2
Doi http://dx.doi.org/10.1038/s41598-017-17598-2
Field Zoology
Keywords cystatin; inhibitor; Eudiplozoon nippponicum; Monogenea; legumain; papain; inhibition
Description 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.
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