Transcriptomic and proteomic profiling of peptidase expression in Fasciola hepatica eggs developing at host's body temperature

Investor logo

Warning

This publication doesn't include Faculty of Economics and Administration. It includes Faculty of Science. Official publication website can be found on muni.cz.
Authors

ILGOVÁ Jana VOREL Jiří ROUDNICKÝ Pavel ŠKORPÍKOVÁ Lucie HORN Martin KAŠNÝ Martin

Year of publication 2022
Type Article in Periodical
Magazine / Source SCIENTIFIC REPORTS
MU Faculty or unit

Faculty of Science

Citation
Web https://doi.org/10.1038/s41598-022-14419-z
Doi http://dx.doi.org/10.1038/s41598-022-14419-z
Keywords Fasciola hepatica; eggs; embryonation; transcriptomics; proteomics; RNAseq; Mass spectrometry
Description Fasciola hepatica is a global parasite of livestock which also causes a neglected zoonosis in humans. The parasite's communication with the host during its complicated lifecycle is based on an ingenious enzymatic apparatus which includes a variety of peptidases. These enzymes are implicated in parasite migration, pathogenesis of the disease, and modification of host immune response. Although the dynamics of proteolytic machinery produced by intra-mammalian F. hepatica life stages has been previously investigated in great detail, peptidases of the eggs so far received little scientific attention. In this study, we performed a comparative RNA-seq analysis aimed at identification of peptidases expressed in F. hepatica eggs, cultured at 37 degrees C to represent gall bladder retained eggs, for different time periods and employed mass spectrometry in order to identify and quantify peptidases translated in F. hepatica egg lysates. We demonstrated that F. hepatica eggs undergo significant molecular changes when cultured at the physiological temperature of the definitive host. Egg transcriptome is subject to numerous subtle changes while their proteome is even more variable. The peptidase profile is considerably modified on both transcriptome and proteome level. Finally, we measured and classified proteolytic activities in extracts from F. hepatica eggs using a library of fluorogenic substrates and peptidase class-selective inhibitors. Activities of threonine peptidases were detected constantly, while the cysteine peptidases prevailing in freshly laid eggs are substituted by aspartic peptidase and metallopeptidase activities in the later stages of egg development.
Related projects:

You are running an old browser version. We recommend updating your browser to its latest version.