Publication details

Inhibitory serinových peptidáz (SERPINY) parazitického organismu Eudiplozoon nipponicum (Monogenea)

Authors

ROUDNICKÝ Pavel VOREL Jiří ILGOVÁ Jana MIKEŠ Libor JEDLIČKOVÁ Lucie DVOŘÁK Jan GELNAR Milan KAŠNÝ Martin

Year of publication 2016
Type Appeared in Conference without Proceedings
MU Faculty or unit

Faculty of Science

Citation
Description Our experimental organisms Eudiplozoon nipponicum (family Diplozoidae, Polyopisthocotylea) is hematophagous ectoparasite from the gills of cyprinid fish (Cyprinus carpio). The properties of proteins (e.g. function) of the members from the family Monogenea are among the less investigated in whole phylum Platyhelminthes. During the previous experimental work, interesting results concerning the bioactive molecules of E. nipponicum (endopeptidases and their inhibitors) were recorded. Some of these molecules are probably presented in excretory-secretory products (secretome) of the parasite and thus potentially involved in parasite-host interactions. Therefore, we performed the complete mass spectrometry analysis of E. nipponicum secretome (LC MS/MS). Some of the identified protein molecules, such as e.g. serpins, were selected and further characterized. In general, serpins play a role in many physiological processes of higher organisms, such as complement cascade activation, blood clotting, fibrinolysis, inflammation and programmed apoptosis. The results of our experiments with serpin in recombinant form indicates that its function could be similar to other blood feeding worms. It was proved, that recombinant E. nipponicum serpin is e.g. able to inhibit the factor Xa which is the important member of blood coagulation cascade.
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