Protein kinase C signalling during miracidium to mother sporocyst development in the helminth parasite, Schistosoma mansoni

Ludtmann, Marthe H.R., Rollinson, David, Emery, Aidan M. and Walker, Anthony J. (2009) Protein kinase C signalling during miracidium to mother sporocyst development in the helminth parasite, Schistosoma mansoni. International Journal for Parasitology, 39(11), pp. 1223-1233. ISSN (print) 0020-7519

Full text not available from this archive.


For schistosomes, development of the miracidium to mother sporocyst within a compatible molluscan host requires considerable physiological and morphological changes by the parasite. The molecular mechanisms controlling such development have not been explored extensively. To begin to elucidate the importance of kinase-mediated signal transduction to this process, the phosphorylation (activation) of protein kinase C (PKC) in larval stages of Schistosoma mansoni undergoing in vitro transformation was explored. Mining of the S. mansoni genomic database revealed two S. mansoni PKC proteins with high homology to human PKCbeta and containing the conserved autophosphorylation (activation) site represented by serine 660 of human PKCbeta(II). Western blotting with anti-phosphospecific antibodies directed to this site demonstrated that miracidia freshly-hatched from eggs possessed PKC (78kDa) which was phosphorylated (activated) when miracidia were exposed to phorbol ester, and dephosphorylated (inhibited) following exposure to the PKC inhibitor GF109203X. Miracidia treated with the phospholipase C (PLC) inhibitor U73122 also displayed decreased PKC phosphorylation. S. mansoni PKC was phosphorylated during the initial 24h development of miracidia into mother sporocysts; after 31h and 48h development, phosphorylation was reduced by 72% and 86%, respectively. Confocal microscopy of miracidia revealed phosphorylated PKC associated with the neural mass, excretory vesicle, tegument, ciliated plates, terebratorium and germinal cells; in larvae undergoing transformation for 31h, phosphorylated PKC was only occasionally detected, being present in regions likely corresponding to the ridge cyton. Inhibition of PKC in miracidia by GF109230X resulted in accelerated transformation, particularly to the postmiracidium stage; ciliated plates were also shed from developing larvae more rapidly. These results highlight the dynamic nature of PKC signalling during S. mansoni postembryonic development and support a role for active PKC in restricting transformation of S. mansoni miracidia into mother sporocysts.

Item Type: Article
Research Area: Biological sciences
Faculty, School or Research Centre: Faculty of Science (until 2011) > School of Life Sciences
Faculty of Science (until 2011)
Related URLs:
Depositing User: Automatic Import Agent
Date Deposited: 08 Feb 2010 09:45
Last Modified: 30 Sep 2010 12:28

Actions (Repository Editors)

Item Control Page Item Control Page