Informace o publikaci
SERPIN, A KEY MOLECULE IN THE LIFE OF EUDIPLOZOON NIPPONICUM?!
| Autoři | |
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| Rok publikování | 2017 |
| Druh | Další prezentace na konferencích |
| Fakulta / Pracoviště MU | |
| Citace | |
| Popis | Eudiplozoon nipponicum (family Diplozoidae, Polyopisthocotylea) is hematophagous ectoparasite from the gills of common carp (Cyprinus carpio). The properties of proteins (e.g. functions) of the members from the family Monogenea are among the less investigated in whole phylum Platyhelminthes. During the previous experimental work of our colleagues, we obtained data concerning the important functional molecules produced by E. nipponicum (e.g. endopeptidases cathepsins L, B and D). Some of them occurred in excretory-secretory products, which indicates their possible participation in host-parasite interaction and some of them were proved to be part of feeding mechanisms. The main aim of our current work is to understand the regulation related to peptidase activity; the peptidase protein inhibitors, such as also serpins, could play a key role in this process. Serpins of vertebrates are known as important regulators of the coagulation cascade, complement, fibrinolysis, angiogenesis, inflammation etc. They possess typical conserved domains and a reactive central loop binding to the active site of peptidase. The inhibition, mediated by serpins, is typically irreversible, comprising conformational changes in serpin molecule leading to distortion of peptidase tertiary structure. Except the inhibition, some of them may have other functions like e.g. protein transporters or chaperones and they are relatively abundant also in secretions, body lysates and genomes/transcriptomes of helminths. We identified serpin gene/protein in transcriptome/proteome of E. nipponicum, subsequently it was prepared in recombinant form and in regard to reveal its functions molecular and biochemical characterization was performed (e.g. prediction of tertiary structure, antigenic properties evaluation, measurement of inhibitory effect). |
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