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Parasite. 2018;25:61. doi: 10.1051/parasite/2018062. Epub 2018 Dec 5.

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

Author information

1
Department of Botany and Zoology, Faculty of Science, Masaryk University, Kamenice 753/5, 62500 Brno, Czech Republic.
2
Veterinary Research Institute, Hudcova 296/70, 62100 Brno, Czech Republic.
3
Department of Parasitology, Faculty of Science, Charles University, Viničná 7, 12844 Prague 2, Czech Republic.
4
Central European Institute of Technology, Masaryk University, Kamenice 753/5, 62500 Brno, Czech Republic.
5
Central European Institute of Technology, Masaryk University, Kamenice 753/5, 62500 Brno, Czech Republic - National Centre for Biomolecular Research, Faculty of Science, Masaryk University, Kamenice 753/5, 62500 Brno, Czech Republic.
6
School of Biological Sciences, Medical Biology Centre, Queen's University Belfast, 97 Lisburn Road, Belfast BT9 7BL, United Kingdom - Department of Zoology and Fisheries, Faculty of Agrobiology, Food and Natural Resources, Czech University of Life Sciences in Prague, Kamýcká 129, 16521 Prague, Czech Republic.
7
Department of Botany and Zoology, Faculty of Science, Masaryk University, Kamenice 753/5, 62500 Brno, Czech Republic - Department of Parasitology, Faculty of Science, Charles University, Viničná 7, 12844 Prague 2, Czech Republic.

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.

PMID:
30516130
DOI:
10.1051/parasite/2018062
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