Plasmodium spp. membrane glutathione S-transferases: detoxification units and drug targets.
Identifieur interne : 000688 ( Main/Exploration ); précédent : 000687; suivant : 000689Plasmodium spp. membrane glutathione S-transferases: detoxification units and drug targets.
Auteurs : Andreas M. Lisewski [États-Unis]Source :
- Microbial cell (Graz, Austria) [ 2311-2638 ] ; 2014.
Abstract
Membrane glutathione S-transferases from the class of membrane-associated proteins in eicosanoid and glutathione metabolism (MAPEG) form a superfamily of detoxification enzymes that catalyze the conjugation of reduced glutathione (GSH) to a broad spectrum of xenobiotics and hydrophobic electrophiles. Evolutionarily unrelated to the cytosolic glutathione S-transferases, they are found across bacterial and eukaryotic domains, for example in mammals, plants, fungi and bacteria in which significant levels of glutathione are maintained. Species of genus Plasmodium, the unicellular protozoa that are commonly known as malaria parasites, do actively support glutathione homeostasis and maintain its metabolism throughout their complex parasitic life cycle. In humans and in other mammals, the asexual intraerythrocytic stage of malaria, when the parasite feeds on hemoglobin, grows and eventually asexually replicates inside infected red blood cells (RBCs), is directly associated with host disease symptoms and during this critical stage GSH protects the host RBC and the parasite against oxidative stress from parasite-induced hemoglobin catabolism. In line with these observations, several GSH-dependent Plasmodium enzymes have been characterized including glutathione reductases, thioredoxins, glyoxalases, glutaredoxins and glutathione S-transferases (GSTs); furthermore, GSH itself have been found to associate spontaneously and to degrade free heme and its hydroxide, hematin, which are the main cytotoxic byproducts of hemoglobin catabolism. However, despite the apparent importance of glutathione metabolism for the parasite, no membrane associated glutathione S-transferases of genus Plasmodium have been previously described. We recently reported the first examples of MAPEG members among Plasmodium spp.
DOI: 10.15698/mic2014.11.177
PubMed: 28357217
PubMed Central: PMC5349128
Affiliations:
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Lisewski</name><affiliation wicri:level="2"><nlm:affiliation>Department of Molecular and Human Genetics, Computational and Integrative Biomedical Research Center, Baylor College of Medicine, Houston, TX 77030, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Molecular and Human Genetics, Computational and Integrative Biomedical Research Center, Baylor College of Medicine, Houston, TX 77030</wicri:regionArea><placeName><region type="state">Texas</region></placeName></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2014">2014</date><idno type="RBID">pubmed:28357217</idno><idno type="pmid">28357217</idno><idno type="doi">10.15698/mic2014.11.177</idno><idno type="pmc">PMC5349128</idno><idno type="wicri:Area/Main/Corpus">000590</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000590</idno><idno type="wicri:Area/Main/Curation">000590</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000590</idno><idno type="wicri:Area/Main/Exploration">000590</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en"><i>Plasmodium</i> spp. membrane glutathione S-transferases: detoxification units and drug targets.</title><author><name sortKey="Lisewski, Andreas M" sort="Lisewski, Andreas M" uniqKey="Lisewski A" first="Andreas M" last="Lisewski">Andreas M. Lisewski</name><affiliation wicri:level="2"><nlm:affiliation>Department of Molecular and Human Genetics, Computational and Integrative Biomedical Research Center, Baylor College of Medicine, Houston, TX 77030, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Molecular and Human Genetics, Computational and Integrative Biomedical Research Center, Baylor College of Medicine, Houston, TX 77030</wicri:regionArea><placeName><region type="state">Texas</region></placeName></affiliation></author></analytic><series><title level="j">Microbial cell (Graz, Austria)</title><idno type="ISSN">2311-2638</idno><imprint><date when="2014" type="published">2014</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Membrane glutathione S-transferases from the class of membrane-associated proteins in eicosanoid and glutathione metabolism (MAPEG) form a superfamily of detoxification enzymes that catalyze the conjugation of reduced glutathione (GSH) to a broad spectrum of xenobiotics and hydrophobic electrophiles. Evolutionarily unrelated to the cytosolic glutathione S-transferases, they are found across bacterial and eukaryotic domains, for example in mammals, plants, fungi and bacteria in which significant levels of glutathione are maintained. Species of genus <i>Plasmodium</i>, the unicellular protozoa that are commonly known as malaria parasites, do actively support glutathione homeostasis and maintain its metabolism throughout their complex parasitic life cycle. In humans and in other mammals, the asexual intraerythrocytic stage of malaria, when the parasite feeds on hemoglobin, grows and eventually asexually replicates inside infected red blood cells (RBCs), is directly associated with host disease symptoms and during this critical stage GSH protects the host RBC and the parasite against oxidative stress from parasite-induced hemoglobin catabolism. In line with these observations, several GSH-dependent <i>Plasmodium</i> enzymes have been characterized including glutathione reductases, thioredoxins, glyoxalases, glutaredoxins and glutathione S-transferases (GSTs); furthermore, GSH itself have been found to associate spontaneously and to degrade free heme and its hydroxide, hematin, which are the main cytotoxic byproducts of hemoglobin catabolism. However, despite the apparent importance of glutathione metabolism for the parasite, no membrane associated glutathione S-transferases of genus <i>Plasmodium</i> have been previously described. We recently reported the first examples of MAPEG members among <i>Plasmodium</i> spp.</div></front></TEI><pubmed><MedlineCitation Status="PubMed-not-MEDLINE" Owner="NLM"><PMID Version="1">28357217</PMID><DateRevised><Year>2020</Year><Month>10</Month><Day>01</Day></DateRevised><Article PubModel="Electronic"><Journal><ISSN IssnType="Print">2311-2638</ISSN><JournalIssue CitedMedium="Print"><Volume>1</Volume><Issue>11</Issue><PubDate><Year>2014</Year><Month>Oct</Month><Day>23</Day></PubDate></JournalIssue><Title>Microbial cell (Graz, Austria)</Title><ISOAbbreviation>Microb Cell</ISOAbbreviation></Journal><ArticleTitle><i>Plasmodium</i> spp. membrane glutathione S-transferases: detoxification units and drug targets.</ArticleTitle><Pagination><MedlinePgn>387-389</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.15698/mic2014.11.177</ELocationID><Abstract><AbstractText>Membrane glutathione S-transferases from the class of membrane-associated proteins in eicosanoid and glutathione metabolism (MAPEG) form a superfamily of detoxification enzymes that catalyze the conjugation of reduced glutathione (GSH) to a broad spectrum of xenobiotics and hydrophobic electrophiles. Evolutionarily unrelated to the cytosolic glutathione S-transferases, they are found across bacterial and eukaryotic domains, for example in mammals, plants, fungi and bacteria in which significant levels of glutathione are maintained. Species of genus <i>Plasmodium</i>, the unicellular protozoa that are commonly known as malaria parasites, do actively support glutathione homeostasis and maintain its metabolism throughout their complex parasitic life cycle. In humans and in other mammals, the asexual intraerythrocytic stage of malaria, when the parasite feeds on hemoglobin, grows and eventually asexually replicates inside infected red blood cells (RBCs), is directly associated with host disease symptoms and during this critical stage GSH protects the host RBC and the parasite against oxidative stress from parasite-induced hemoglobin catabolism. In line with these observations, several GSH-dependent <i>Plasmodium</i> enzymes have been characterized including glutathione reductases, thioredoxins, glyoxalases, glutaredoxins and glutathione S-transferases (GSTs); furthermore, GSH itself have been found to associate spontaneously and to degrade free heme and its hydroxide, hematin, which are the main cytotoxic byproducts of hemoglobin catabolism. However, despite the apparent importance of glutathione metabolism for the parasite, no membrane associated glutathione S-transferases of genus <i>Plasmodium</i> have been previously described. We recently reported the first examples of MAPEG members among <i>Plasmodium</i> spp.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Lisewski</LastName><ForeName>Andreas M</ForeName><Initials>AM</Initials><AffiliationInfo><Affiliation>Department of Molecular and Human Genetics, Computational and Integrative Biomedical Research Center, Baylor College of Medicine, Houston, TX 77030, USA.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D016420">Comment</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2014</Year><Month>10</Month><Day>23</Day></ArticleDate></Article><MedlineJournalInfo><Country>Austria</Country><MedlineTA>Microb Cell</MedlineTA><NlmUniqueID>101632887</NlmUniqueID><ISSNLinking>2311-2638</ISSNLinking></MedlineJournalInfo><CommentsCorrectionsList><CommentsCorrections RefType="CommentOn"><RefSource>Cell. 2014 Aug 14;158(4):916-28</RefSource><PMID Version="1">25126794</PMID></CommentsCorrections></CommentsCorrectionsList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Plasmodium</Keyword><Keyword MajorTopicYN="N">artemisinin</Keyword><Keyword MajorTopicYN="N">detoxification</Keyword><Keyword MajorTopicYN="N">glutathione</Keyword><Keyword MajorTopicYN="N">malaria</Keyword></KeywordList><CoiStatement>Conflict of interest: The author declares no conflict of interest.</CoiStatement></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2017</Year><Month>3</Month><Day>31</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2014</Year><Month>10</Month><Day>23</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2014</Year><Month>10</Month><Day>23</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate></History><PublicationStatus>epublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">28357217</ArticleId><ArticleId IdType="doi">10.15698/mic2014.11.177</ArticleId><ArticleId IdType="pii">MIC0174E185</ArticleId><ArticleId IdType="pmc">PMC5349128</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>États-Unis</li></country><region><li>Texas</li></region></list><tree><country name="États-Unis"><region name="Texas"><name sortKey="Lisewski, Andreas M" sort="Lisewski, Andreas M" uniqKey="Lisewski A" first="Andreas M" last="Lisewski">Andreas M. 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