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

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

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
Type
Published Article
Journal
Parasite
Publisher
EDP Sciences
Publication Date
Dec 05, 2018
Volume
25
Identifiers
DOI: 10.1051/parasite/2018062
Source
EDP Sciences
Keywords
License
Green
External links

Abstract

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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