A novel type I cystatin of parasite origin with atypical legumain-binding domain
| Autoři | |
|---|---|
| Rok publikování | 2017 |
| Druh | Článek v odborném periodiku |
| Časopis / Zdroj | Scientific Reports |
| Fakulta / Pracoviště MU | |
| Citace | |
| www | https://www.nature.com/articles/s41598-017-17598-2 |
| Doi | http://dx.doi.org/10.1038/s41598-017-17598-2 |
| Obor | Zoologie |
| Klíčová slova | cystatin; inhibitor; Eudiplozoon nippponicum; Monogenea; legumain; papain; inhibition |
| Popis | 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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