Towards an understanding of the function of the phytochelatin synthase of Schistosoma mansoni.
Phytochelatin synthase (PCS) is a protease-like enzyme that catalyzes the production of metal chelating peptides, the phytochelatins, from glutathione (GSH). In plants, algae, and fungi phytochelatin production is important for metal tolerance and detoxification. PCS proteins also function in xenobi...
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ftdoajarticles:oai:doaj.org/article:fbdc1935f15443c386ccca847e74f0de 2023-05-15T15:09:25+02:00 Towards an understanding of the function of the phytochelatin synthase of Schistosoma mansoni. Coraline Rigouin Elyse Nylin Alexis A Cogswell Dirk Schaumlöffel Dirk Dobritzsch David L Williams 2013-01-01T00:00:00Z https://doi.org/10.1371/journal.pntd.0002037 https://doaj.org/article/fbdc1935f15443c386ccca847e74f0de EN eng Public Library of Science (PLoS) http://europepmc.org/articles/PMC3561135?pdf=render https://doaj.org/toc/1935-2727 https://doaj.org/toc/1935-2735 1935-2727 1935-2735 doi:10.1371/journal.pntd.0002037 https://doaj.org/article/fbdc1935f15443c386ccca847e74f0de PLoS Neglected Tropical Diseases, Vol 7, Iss 1, p e2037 (2013) Arctic medicine. Tropical medicine RC955-962 Public aspects of medicine RA1-1270 article 2013 ftdoajarticles https://doi.org/10.1371/journal.pntd.0002037 2022-12-31T03:54:49Z Phytochelatin synthase (PCS) is a protease-like enzyme that catalyzes the production of metal chelating peptides, the phytochelatins, from glutathione (GSH). In plants, algae, and fungi phytochelatin production is important for metal tolerance and detoxification. PCS proteins also function in xenobiotic metabolism by processing GSH S-conjugates. The aim of the present study is to elucidate the role of PCS in the parasitic worm Schistosoma mansoni. Recombinant S. mansoni PCS proteins expressed in bacteria could both synthesize phytochelatins and hydrolyze various GSH S-conjugates. We found that both the N-truncated protein and the N- and C-terminal truncated form of the enzyme (corresponding to only the catalytic domain) work through a thiol-dependant and, notably, metal-independent mechanism for both transpeptidase (phytochelatin synthesis) and peptidase (hydrolysis of GSH S-conjugates) activities. PCS transcript abundance was increased by metals and xenobiotics in cultured adult worms. In addition, these treatments were found to increase transcript abundance of other enzymes involved in GSH metabolism. Highest levels of PCS transcripts were identified in the esophageal gland of adult worms. Taken together, these results suggest that S. mansoni PCS participates in both metal homoeostasis and xenobiotic metabolism rather than metal detoxification as previously suggested and that the enzyme may be part of a global stress response in the worm. Because humans do not have PCS, this enzyme is of particular interest as a drug target for schistosomiasis. Article in Journal/Newspaper Arctic Directory of Open Access Journals: DOAJ Articles Arctic PLoS Neglected Tropical Diseases 7 1 e2037 |
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Open Polar |
collection |
Directory of Open Access Journals: DOAJ Articles |
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ftdoajarticles |
language |
English |
topic |
Arctic medicine. Tropical medicine RC955-962 Public aspects of medicine RA1-1270 |
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Arctic medicine. Tropical medicine RC955-962 Public aspects of medicine RA1-1270 Coraline Rigouin Elyse Nylin Alexis A Cogswell Dirk Schaumlöffel Dirk Dobritzsch David L Williams Towards an understanding of the function of the phytochelatin synthase of Schistosoma mansoni. |
topic_facet |
Arctic medicine. Tropical medicine RC955-962 Public aspects of medicine RA1-1270 |
description |
Phytochelatin synthase (PCS) is a protease-like enzyme that catalyzes the production of metal chelating peptides, the phytochelatins, from glutathione (GSH). In plants, algae, and fungi phytochelatin production is important for metal tolerance and detoxification. PCS proteins also function in xenobiotic metabolism by processing GSH S-conjugates. The aim of the present study is to elucidate the role of PCS in the parasitic worm Schistosoma mansoni. Recombinant S. mansoni PCS proteins expressed in bacteria could both synthesize phytochelatins and hydrolyze various GSH S-conjugates. We found that both the N-truncated protein and the N- and C-terminal truncated form of the enzyme (corresponding to only the catalytic domain) work through a thiol-dependant and, notably, metal-independent mechanism for both transpeptidase (phytochelatin synthesis) and peptidase (hydrolysis of GSH S-conjugates) activities. PCS transcript abundance was increased by metals and xenobiotics in cultured adult worms. In addition, these treatments were found to increase transcript abundance of other enzymes involved in GSH metabolism. Highest levels of PCS transcripts were identified in the esophageal gland of adult worms. Taken together, these results suggest that S. mansoni PCS participates in both metal homoeostasis and xenobiotic metabolism rather than metal detoxification as previously suggested and that the enzyme may be part of a global stress response in the worm. Because humans do not have PCS, this enzyme is of particular interest as a drug target for schistosomiasis. |
format |
Article in Journal/Newspaper |
author |
Coraline Rigouin Elyse Nylin Alexis A Cogswell Dirk Schaumlöffel Dirk Dobritzsch David L Williams |
author_facet |
Coraline Rigouin Elyse Nylin Alexis A Cogswell Dirk Schaumlöffel Dirk Dobritzsch David L Williams |
author_sort |
Coraline Rigouin |
title |
Towards an understanding of the function of the phytochelatin synthase of Schistosoma mansoni. |
title_short |
Towards an understanding of the function of the phytochelatin synthase of Schistosoma mansoni. |
title_full |
Towards an understanding of the function of the phytochelatin synthase of Schistosoma mansoni. |
title_fullStr |
Towards an understanding of the function of the phytochelatin synthase of Schistosoma mansoni. |
title_full_unstemmed |
Towards an understanding of the function of the phytochelatin synthase of Schistosoma mansoni. |
title_sort |
towards an understanding of the function of the phytochelatin synthase of schistosoma mansoni. |
publisher |
Public Library of Science (PLoS) |
publishDate |
2013 |
url |
https://doi.org/10.1371/journal.pntd.0002037 https://doaj.org/article/fbdc1935f15443c386ccca847e74f0de |
geographic |
Arctic |
geographic_facet |
Arctic |
genre |
Arctic |
genre_facet |
Arctic |
op_source |
PLoS Neglected Tropical Diseases, Vol 7, Iss 1, p e2037 (2013) |
op_relation |
http://europepmc.org/articles/PMC3561135?pdf=render https://doaj.org/toc/1935-2727 https://doaj.org/toc/1935-2735 1935-2727 1935-2735 doi:10.1371/journal.pntd.0002037 https://doaj.org/article/fbdc1935f15443c386ccca847e74f0de |
op_doi |
https://doi.org/10.1371/journal.pntd.0002037 |
container_title |
PLoS Neglected Tropical Diseases |
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7 |
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1 |
container_start_page |
e2037 |
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1766340612648337408 |