Identification and partial characterization of a novel serpin from Eudiplozoon nipponicum (Monogenea, Polyopisthocotylea)

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Authors

ROUDNICKÝ Pavel VOREL Jiří ILGOVÁ Jana BENOVICS Michal NOREK Adam JEDLIČKOVÁ Lucie MIKEŠ Libor POTĚŠIL David ZDRÁHAL Zbyněk DVOŘÁK Jan GELNAR Milan KAŠNÝ Martin

Year of publication 2018
Type Article in Periodical
Magazine / Source Parasite
MU Faculty or unit

Faculty of Science

Citation
Web https://www.parasite-journal.org/articles/parasite/abs/2018/01/parasite180126/parasite180126.html
Doi http://dx.doi.org/10.1051/parasite/2018062
Keywords Eudiplozoon nipponicum; fish parasite; monogenea; Platyhelminths; serpin; inhibitor
Description Background: Serpins are a superfamily of serine peptidase inhibitors that participate in the regulation of many physiological and cell peptidase-mediated processes in all organisms (e.g. in blood clotting, complement activation, fibrinolysis, inflammation, and programmed cell death). It was postulated that in the blood-feeding members of the monogenean family Diplozoidae, serpins could play an important role in the prevention of thrombus formation, activation of complement, inflammation in the host, and/or in the endogenous regulation of protein degradation. Results: In silico analysis showed that the DNA and primary protein structures of serpin from Eudiplozoon nipponicum (EnSerp1) are similar to other members of the serpin superfamily. The inhibitory potential of EnSerp1 on four physiologically-relevant serine peptidases (trypsin, factor Xa, kallikrein, and plasmin) was demonstrated and its presence in the worm’s excretory-secretory products (ESPs) was confirmed. Conclusion: EnSerp1 influences the activity of peptidases that play a role in blood coagulation, fibrinolysis, and complement activation. This inhibitory potential, together with the serpin’s presence in ESPs, suggests that it is likely involved in host-parasite interactions and could be one of the molecules involved in the control of feeding and prevention of inflammatory responses.
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