Carbohydrates that mimic schistosome surface coat components affect ERK and PKC signalling in Lymnaea stagnalis haemocytes

Plows, Louise D.; Cook, Richard T.; Davies, Angela J.; Walker, Anthony J.

doi:10.1016/j.ijpara.2004.11.012

Cited by 41 publications

(32 citation statements)

References 38 publications

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“…PKC is also capable of phosphorylating p47 phox at various sites, which are absolutely essential for activation and translocation of the protein [59]. PKC d has been successfully identified in insect hemocyte lysates [6,60] and as this study revealed the translocation of the insect 47 kDa protein from the cytosol to the membrane, it is not inconceivable that phosphorylation of this immunologically similar protein by PKC may occur upon stimulation of insect phagocytes.…”

Section: Discussionmentioning

confidence: 92%

Translocation of proteins homologous to human neutrophil p47phox and p67phox to the cell membrane in activated hemocytes of Galleria mellonella

Renwick

Reeves

Wientjes

et al. 2007

Developmental & Comparative Immunology

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Activation of the superoxide forming respiratory burst oxidase of human neutrophils, crucial in host defence, requires the cytosolic proteins p47 phox and p67 phox which translocate to the plasma membrane upon cell stimulation and activate flavocytochrome b 558 , the redox centre of this enzyme system. We have previously demonstrated the presence of proteins (67 and 47 kDa) in hemocytes of the insect Galleria mellonella homologous to proteins of the superoxide-forming NADPH oxidase complex of neutrophils. The work presented here illustrates for the first time translocation of homologous hemocyte proteins, 67 and 47 kDa from the cytosol to the plasma membrane upon phorbol 12-myristate 13 acetate (PMA) activation. In hemocytes, gliotoxin (GT), the fungal secondary metabolite significantly suppressed PMA-induced superoxide generation in a concentration dependent manner and reduced translocation to basel nonstimulated levels. Primarily these results correlate translocation of hemocyte 47 and 67 kDa proteins with PMA induced oxidase activity. Collectively results presented here, demonstrate further cellular and functional similarities between phagocytes of insects and mammals and further justify the use of insects in place of mammals for modelling the innate immune response to microbial pathogens. r

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Section: Discussionmentioning

confidence: 92%

Translocation of proteins homologous to human neutrophil p47phox and p67phox to the cell membrane in activated hemocytes of Galleria mellonella

Renwick

Reeves

Wientjes

et al. 2007

Developmental & Comparative Immunology

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“…Disruption of hemocyte signaling pathways, such as protein kinase C (PKC) and extracellular signal-regulated kinase (ERK) pathways, may also influence hemocyte activities (150)(151)(152). For example, carbohydrates known to be present on larval surfaces of T. szidati and T. regenti, such as D-galactose and L-fucose (153)(154)(155)(156), affected hemocyte PKC and ERK signaling in L. stagnalis, which suggests an immunosuppressive role (157,158). However, experiments investigating the direct effect of Trichobilharzia larvae on hemocyte signaling have not been performed.…”

Section: Molluscan and Avian Host Specificitymentioning

confidence: 99%

Avian Schistosomes and Outbreaks of Cercarial Dermatitis

et al. 2015

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SUMMARY Cercarial dermatitis (swimmer's itch) is a condition caused by infective larvae (cercariae) of a species-rich group of mammalian and avian schistosomes. Over the last decade, it has been reported in areas that previously had few or no cases of dermatitis and is thus considered an emerging disease. It is obvious that avian schistosomes are responsible for the majority of reported dermatitis outbreaks around the world, and thus they are the primary focus of this review. Although they infect humans, they do not mature and usually die in the skin. Experimental infections of avian schistosomes in mice show that in previously exposed hosts, there is a strong skin immune reaction that kills the schistosome. However, penetration of larvae into naive mice can result in temporary migration from the skin. This is of particular interest because the worms are able to migrate to different organs, for example, the lungs in the case of visceral schistosomes and the central nervous system in the case of nasal schistosomes. The risk of such migration and accompanying disorders needs to be clarified for humans and animals of interest (e.g., dogs). Herein we compiled the most comprehensive review of the diversity, immunology, and epidemiology of avian schistosomes causing cercarial dermatitis.

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“…In some experiments, the proteasome inhibitor Z-Leu-Leu-Leu-aldehyde (MG132; 50 μM; Merck Chemicals, Nottinghamshire, UK), the MEK1/2 inhibitor, 1,4-diamino-2,3-dicyano-1,4-bis[2-aminophenylthio]butadiene (U0126; 1-10 μM; Sigma), or vehicle control (0.1% (v/v) DMSO; Sigma) were added with or without ESPs. The inhibitor, U0126, has previously been used at these concentrations to block MEK1/2 activity in B. glabrata and Lymnaea stagnalis haemocytes, subsequently suppressing the phosphorylation (activation) of ERK (Plows et al 2004;Plows et al 2005;Wright et al 2006;Zahoor et al 2008Zahoor et al , 2009). The concentration chosen for MG132 was similar to that used by Kim et al (1999).…”

Section: Haemocytes and Haemocyte Treatmentsmentioning

confidence: 99%

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

Zahoor

Davies²,

Kirk³

et al. 2010

Cell Stress and Chaperones

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Synthesis of heat shock proteins (HSPs) following cellular stress is a response shared by many organisms. Amongst the HSP family, the ∼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.

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Carbohydrates that mimic schistosome surface coat components affect ERK and PKC signalling in Lymnaea stagnalis haemocytes

Cited by 41 publications

References 38 publications

Translocation of proteins homologous to human neutrophil p47phox and p67phox to the cell membrane in activated hemocytes of Galleria mellonella

Translocation of proteins homologous to human neutrophil p47phox and p67phox to the cell membrane in activated hemocytes of Galleria mellonella

Avian Schistosomes and Outbreaks of Cercarial Dermatitis

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

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