Larval excretory-secretory products from the parasite Schistosoma mansoni modulate HSP70 protein expression in defence cells of its snail host, Biomphalaria glabrata

Zahoor, Zahida, Davies, Angela J., Kirk, Ruth S., Rollinson, David and Walker, Anthony John (2010) Larval excretory-secretory products from the parasite Schistosoma mansoni modulate HSP70 protein expression in defence cells of its snail host, Biomphalaria glabrata. Cell Stress & Chaperones, 15(5), pp. 639-650. ISSN (print) 1355-8145

Full text not available from this archive.

Abstract

Synthesis of heat shock proteins (HSPs) following cellular stress is a response shared by many organisms. Amongst the HSP family, the approximately 70 kDa HSPs are the most evolutionarily conserved with intracellular chaperone and extracellular immunoregulatory functions. This study focused on the effects of larval excretory-secretory products (ESPs) from the parasite Schistosoma mansoni on HSP70 protein expression levels in haemocytes (defence cells) from its snail intermediate host Biomphalaria glabrata. S. mansoni larval stage ESPs are known to interfere with haemocyte physiology and behaviour. Haemocytes from two different B. glabrata strains, one which is susceptible to S. mansoni infection and one which is resistant, both showed reduced HSP70 protein levels following 1 h challenge with S. mansoni ESPs when compared to unchallenged controls; however, the reduction observed in the resistant strain was less marked. The decline in intracellular HSP70 protein persisted for at least 5 h in resistant snail haemocytes only. Furthermore, in schistosome-susceptible snails infected by S. mansoni for 35 days, haemocytes possessed approximately 70% less HSP70. The proteasome inhibitor, MG132, partially restored HSP70 protein levels in ESP-challenged haemocytes, demonstrating that the decrease in HSP70 was in part due to intracellular degradation. The extracellular signal-regulated kinase (ERK) signalling pathway appears to regulate HSP70 protein expression in these cells, as the mitogen-activated protein-ERK kinase 1/2 (MEK1/2) inhibitor, U0126, significantly reduced HSP70 protein levels. Disruption of intracellular HSP70 protein expression in B. glabrata haemocytes by S. mansoni ESPs may be a strategy employed by the parasite to manipulate the immune response of the intermediate snail host.

Item Type: Article
Uncontrolled Keywords: heat shock protein 70 (hsp70), excretory-secretory products (esps), extracellular signal-regulated kinase (erk), schistosomes, snail haemocytes, biomphalaria glabrata, heat-shock proteins, mussel mytilus-galloprovincialis, lymnaea-stagnalis hemocytes, gene-expression, transcriptional activation, superoxide production, echinostoma-caproni, signal-transduction, primary sporocysts, stress-response
Research Area: Biological sciences
Faculty, School or Research Centre: Faculty of Science (until 2011) > School of Life Sciences
Related URLs:
Depositing User: Automatic Import Agent
Date Deposited: 01 Jun 2010 11:04
Last Modified: 30 Sep 2010 12:44
URI: http://eprints.kingston.ac.uk/id/eprint/11951

Actions (Repository Editors)

Item Control Page Item Control Page