Staphylococcus aureus responds to allicin by global S-thioallylation - Role of the Brx/BSH/YpdA pathway and the disulfide reductase MerA to overcome allicin stress.
Identifieur interne : 000207 ( PubMed/Curation ); précédent : 000206; suivant : 000208Staphylococcus aureus responds to allicin by global S-thioallylation - Role of the Brx/BSH/YpdA pathway and the disulfide reductase MerA to overcome allicin stress.
Auteurs : Vu Van Loi [Allemagne] ; Nguyen Thi Thu Huyen [Allemagne] ; Tobias Busche [Allemagne] ; Quach Ngoc Tung [Allemagne] ; Martin Clemens Horst Gruhlke [Allemagne] ; Jörn Kalinowski [Allemagne] ; Jörg Bernhardt [Allemagne] ; Alan John Slusarenko [Allemagne] ; Haike Antelmann [Allemagne]Source :
- Free radical biology & medicine [ 1873-4596 ] ; 2019.
Abstract
The prevalence of methicillin-resitant Staphylococcus aureus (MRSA) in hospitals and the community poses an increasing health burden, which requires the discovery of alternative antimicrobials. Allicin (diallyl thiosulfinate) from garlic exhibits broad-spectrum antimicrobial activity against many multidrug resistant bacteria. The thiol-reactive mode of action of allicin involves its S-thioallylations of low molecular weight (LMW) thiols and protein thiols. To investigate the mode of action and stress response caused by allicin in S. aureus, we analyzed the transcriptome signature, the targets for S-thioallylation in the proteome and the changes in the bacillithiol (BSH) redox potential (EBSH) under allicin stress. Allicin caused a strong thiol-specific oxidative and sulfur stress response and protein damage as revealed by the induction of the PerR, HypR, QsrR, MhqR, CstR, CtsR, HrcA and CymR regulons in the RNA-seq transcriptome. Allicin also interfered with metal and cell wall homeostasis and caused induction of the Zur, CsoR and GraRS regulons. Brx-roGFP2 biosensor measurements revealed a strongly increased EBSH under allicin stress. In the proteome, 57 proteins were identified with S-thioallylations under allicin treatment, including translation factors (EF-Tu, EF-Ts), metabolic and redox enzymes (AldA, GuaB, Tpx, KatA, BrxA, MsrB) as well as redox-sensitive MarR/SarA-family regulators (MgrA, SarA, SarH1, SarS). Phenotype and biochemical analyses revealed that BSH and the HypR-controlled disulfide reductase MerA are involved in allicin detoxification in S. aureus. The reversal of protein S-thioallylation was catalyzed by the Brx/BSH/YpdA pathway. Finally, the BSSB reductase YpdA was shown to use S-allylmercaptobacillithiol (BSSA) as substrate to regenerate BSH in S. aureus. In conclusion, allicin results in an oxidative shift of EBSH and protein S-thioallylation, which can be reversed by YpdA and the Brx/BSH/YpdA electron pathways in S. aureus to regenerate thiol homeostasis.
DOI: 10.1016/j.freeradbiomed.2019.05.018
PubMed: 31121222
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Electronic address: haike.antelmann@fu-berlin.de.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Freie Universität Berlin, Institute for Biology-Microbiology, D-14195, Berlin</wicri:regionArea></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2019">2019</date><idno type="RBID">pubmed:31121222</idno><idno type="pmid">31121222</idno><idno type="doi">10.1016/j.freeradbiomed.2019.05.018</idno><idno type="wicri:Area/PubMed/Corpus">000207</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000207</idno><idno type="wicri:Area/PubMed/Curation">000207</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">000207</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Staphylococcus aureus responds to allicin by global S-thioallylation - Role of the Brx/BSH/YpdA pathway and the disulfide reductase MerA to overcome allicin stress.</title><author><name sortKey="Loi, Vu Van" sort="Loi, Vu Van" uniqKey="Loi V" first="Vu Van" last="Loi">Vu Van Loi</name><affiliation wicri:level="1"><nlm:affiliation>Freie Universität Berlin, Institute for Biology-Microbiology, D-14195, Berlin, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Freie Universität Berlin, Institute for Biology-Microbiology, D-14195, Berlin</wicri:regionArea></affiliation></author><author><name sortKey="Huyen, Nguyen Thi Thu" sort="Huyen, Nguyen Thi Thu" uniqKey="Huyen N" first="Nguyen Thi Thu" last="Huyen">Nguyen Thi Thu Huyen</name><affiliation wicri:level="1"><nlm:affiliation>Freie Universität Berlin, Institute for Biology-Microbiology, D-14195, Berlin, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Freie Universität Berlin, Institute for Biology-Microbiology, D-14195, Berlin</wicri:regionArea></affiliation></author><author><name sortKey="Busche, Tobias" sort="Busche, Tobias" uniqKey="Busche T" first="Tobias" last="Busche">Tobias Busche</name><affiliation wicri:level="1"><nlm:affiliation>Freie Universität Berlin, Institute for Biology-Microbiology, D-14195, Berlin, Germany; Center for Biotechnology, Bielefeld University, D-33594, Bielefeld, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Freie Universität Berlin, Institute for Biology-Microbiology, D-14195, Berlin, Germany; Center for Biotechnology, Bielefeld University, D-33594, Bielefeld</wicri:regionArea></affiliation></author><author><name sortKey="Tung, Quach Ngoc" sort="Tung, Quach Ngoc" uniqKey="Tung Q" first="Quach Ngoc" last="Tung">Quach Ngoc Tung</name><affiliation wicri:level="1"><nlm:affiliation>Freie Universität Berlin, Institute for Biology-Microbiology, D-14195, Berlin, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Freie Universität Berlin, Institute for Biology-Microbiology, D-14195, Berlin</wicri:regionArea></affiliation></author><author><name sortKey="Gruhlke, Martin Clemens Horst" sort="Gruhlke, Martin Clemens Horst" uniqKey="Gruhlke M" first="Martin Clemens Horst" last="Gruhlke">Martin Clemens Horst Gruhlke</name><affiliation wicri:level="1"><nlm:affiliation>Department of Plant Physiology, RWTH Aachen University, D-52056, Aachen, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Department of Plant Physiology, RWTH Aachen University, D-52056, Aachen</wicri:regionArea></affiliation></author><author><name sortKey="Kalinowski, Jorn" sort="Kalinowski, Jorn" uniqKey="Kalinowski J" first="Jörn" last="Kalinowski">Jörn Kalinowski</name><affiliation wicri:level="1"><nlm:affiliation>Center for Biotechnology, Bielefeld University, D-33594, Bielefeld, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Center for Biotechnology, Bielefeld University, D-33594, Bielefeld</wicri:regionArea></affiliation></author><author><name sortKey="Bernhardt, Jorg" sort="Bernhardt, Jorg" uniqKey="Bernhardt J" first="Jörg" last="Bernhardt">Jörg Bernhardt</name><affiliation wicri:level="1"><nlm:affiliation>Freie Universität Berlin, Institute for Biology-Microbiology, D-14195, Berlin, Germany; Institute for Microbiology, University of Greifswald, D-17489, Greifswald, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Freie Universität Berlin, Institute for Biology-Microbiology, D-14195, Berlin, Germany; Institute for Microbiology, University of Greifswald, D-17489, Greifswald</wicri:regionArea></affiliation></author><author><name sortKey="Slusarenko, Alan John" sort="Slusarenko, Alan John" uniqKey="Slusarenko A" first="Alan John" last="Slusarenko">Alan John Slusarenko</name><affiliation wicri:level="1"><nlm:affiliation>Department of Plant Physiology, RWTH Aachen University, D-52056, Aachen, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Department of Plant Physiology, RWTH Aachen University, D-52056, Aachen</wicri:regionArea></affiliation></author><author><name sortKey="Antelmann, Haike" sort="Antelmann, Haike" uniqKey="Antelmann H" first="Haike" last="Antelmann">Haike Antelmann</name><affiliation wicri:level="1"><nlm:affiliation>Freie Universität Berlin, Institute for Biology-Microbiology, D-14195, Berlin, Germany. Electronic address: haike.antelmann@fu-berlin.de.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Freie Universität Berlin, Institute for Biology-Microbiology, D-14195, Berlin</wicri:regionArea></affiliation></author></analytic><series><title level="j">Free radical biology & medicine</title><idno type="eISSN">1873-4596</idno><imprint><date when="2019" type="published">2019</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The prevalence of methicillin-resitant Staphylococcus aureus (MRSA) in hospitals and the community poses an increasing health burden, which requires the discovery of alternative antimicrobials. Allicin (diallyl thiosulfinate) from garlic exhibits broad-spectrum antimicrobial activity against many multidrug resistant bacteria. The thiol-reactive mode of action of allicin involves its S-thioallylations of low molecular weight (LMW) thiols and protein thiols. To investigate the mode of action and stress response caused by allicin in S. aureus, we analyzed the transcriptome signature, the targets for S-thioallylation in the proteome and the changes in the bacillithiol (BSH) redox potential (E<sub>BSH</sub>) under allicin stress. Allicin caused a strong thiol-specific oxidative and sulfur stress response and protein damage as revealed by the induction of the PerR, HypR, QsrR, MhqR, CstR, CtsR, HrcA and CymR regulons in the RNA-seq transcriptome. Allicin also interfered with metal and cell wall homeostasis and caused induction of the Zur, CsoR and GraRS regulons. Brx-roGFP2 biosensor measurements revealed a strongly increased E<sub>BSH</sub> under allicin stress. In the proteome, 57 proteins were identified with S-thioallylations under allicin treatment, including translation factors (EF-Tu, EF-Ts), metabolic and redox enzymes (AldA, GuaB, Tpx, KatA, BrxA, MsrB) as well as redox-sensitive MarR/SarA-family regulators (MgrA, SarA, SarH1, SarS). Phenotype and biochemical analyses revealed that BSH and the HypR-controlled disulfide reductase MerA are involved in allicin detoxification in S. aureus. The reversal of protein S-thioallylation was catalyzed by the Brx/BSH/YpdA pathway. Finally, the BSSB reductase YpdA was shown to use S-allylmercaptobacillithiol (BSSA) as substrate to regenerate BSH in S. aureus. In conclusion, allicin results in an oxidative shift of E<sub>BSH</sub> and protein S-thioallylation, which can be reversed by YpdA and the Brx/BSH/YpdA electron pathways in S. aureus to regenerate thiol homeostasis.</div></front></TEI><pubmed><MedlineCitation Status="In-Process" Owner="NLM"><PMID Version="1">31121222</PMID><DateRevised><Year>2020</Year><Month>03</Month><Day>30</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1873-4596</ISSN><JournalIssue CitedMedium="Internet"><Volume>139</Volume><PubDate><Year>2019</Year><Month>08</Month><Day>01</Day></PubDate></JournalIssue><Title>Free radical biology & medicine</Title><ISOAbbreviation>Free Radic. Biol. Med.</ISOAbbreviation></Journal><ArticleTitle>Staphylococcus aureus responds to allicin by global S-thioallylation - Role of the Brx/BSH/YpdA pathway and the disulfide reductase MerA to overcome allicin stress.</ArticleTitle><Pagination><MedlinePgn>55-69</MedlinePgn></Pagination><ELocationID EIdType="pii" ValidYN="Y">S0891-5849(19)30511-8</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.freeradbiomed.2019.05.018</ELocationID><Abstract><AbstractText>The prevalence of methicillin-resitant Staphylococcus aureus (MRSA) in hospitals and the community poses an increasing health burden, which requires the discovery of alternative antimicrobials. Allicin (diallyl thiosulfinate) from garlic exhibits broad-spectrum antimicrobial activity against many multidrug resistant bacteria. The thiol-reactive mode of action of allicin involves its S-thioallylations of low molecular weight (LMW) thiols and protein thiols. To investigate the mode of action and stress response caused by allicin in S. aureus, we analyzed the transcriptome signature, the targets for S-thioallylation in the proteome and the changes in the bacillithiol (BSH) redox potential (E<sub>BSH</sub>) under allicin stress. Allicin caused a strong thiol-specific oxidative and sulfur stress response and protein damage as revealed by the induction of the PerR, HypR, QsrR, MhqR, CstR, CtsR, HrcA and CymR regulons in the RNA-seq transcriptome. Allicin also interfered with metal and cell wall homeostasis and caused induction of the Zur, CsoR and GraRS regulons. Brx-roGFP2 biosensor measurements revealed a strongly increased E<sub>BSH</sub> under allicin stress. In the proteome, 57 proteins were identified with S-thioallylations under allicin treatment, including translation factors (EF-Tu, EF-Ts), metabolic and redox enzymes (AldA, GuaB, Tpx, KatA, BrxA, MsrB) as well as redox-sensitive MarR/SarA-family regulators (MgrA, SarA, SarH1, SarS). Phenotype and biochemical analyses revealed that BSH and the HypR-controlled disulfide reductase MerA are involved in allicin detoxification in S. aureus. The reversal of protein S-thioallylation was catalyzed by the Brx/BSH/YpdA pathway. Finally, the BSSB reductase YpdA was shown to use S-allylmercaptobacillithiol (BSSA) as substrate to regenerate BSH in S. aureus. In conclusion, allicin results in an oxidative shift of E<sub>BSH</sub> and protein S-thioallylation, which can be reversed by YpdA and the Brx/BSH/YpdA electron pathways in S. aureus to regenerate thiol homeostasis.</AbstractText><CopyrightInformation>Copyright © 2019 The Authors. Published by Elsevier Inc. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Loi</LastName><ForeName>Vu Van</ForeName><Initials>VV</Initials><AffiliationInfo><Affiliation>Freie Universität Berlin, Institute for Biology-Microbiology, D-14195, Berlin, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Huyen</LastName><ForeName>Nguyen Thi Thu</ForeName><Initials>NTT</Initials><AffiliationInfo><Affiliation>Freie Universität Berlin, Institute for Biology-Microbiology, D-14195, Berlin, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Busche</LastName><ForeName>Tobias</ForeName><Initials>T</Initials><AffiliationInfo><Affiliation>Freie Universität Berlin, Institute for Biology-Microbiology, D-14195, Berlin, Germany; Center for Biotechnology, Bielefeld University, D-33594, Bielefeld, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Tung</LastName><ForeName>Quach Ngoc</ForeName><Initials>QN</Initials><AffiliationInfo><Affiliation>Freie Universität Berlin, Institute for Biology-Microbiology, D-14195, Berlin, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Gruhlke</LastName><ForeName>Martin Clemens Horst</ForeName><Initials>MCH</Initials><AffiliationInfo><Affiliation>Department of Plant Physiology, RWTH Aachen University, D-52056, Aachen, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kalinowski</LastName><ForeName>Jörn</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Center for Biotechnology, Bielefeld University, D-33594, Bielefeld, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Bernhardt</LastName><ForeName>Jörg</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Freie Universität Berlin, Institute for Biology-Microbiology, D-14195, Berlin, Germany; Institute for Microbiology, University of Greifswald, D-17489, Greifswald, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Slusarenko</LastName><ForeName>Alan John</ForeName><Initials>AJ</Initials><AffiliationInfo><Affiliation>Department of Plant Physiology, RWTH Aachen University, D-52056, Aachen, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Antelmann</LastName><ForeName>Haike</ForeName><Initials>H</Initials><AffiliationInfo><Affiliation>Freie Universität Berlin, Institute for Biology-Microbiology, D-14195, Berlin, Germany. Electronic address: haike.antelmann@fu-berlin.de.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2019</Year><Month>05</Month><Day>20</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Free Radic Biol Med</MedlineTA><NlmUniqueID>8709159</NlmUniqueID><ISSNLinking>0891-5849</ISSNLinking></MedlineJournalInfo><CitationSubset>IM</CitationSubset><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">Allicin</Keyword><Keyword MajorTopicYN="Y">Bacillithiol</Keyword><Keyword MajorTopicYN="Y">BrxAB</Keyword><Keyword MajorTopicYN="Y">MerA</Keyword><Keyword MajorTopicYN="Y">S-thioallylation</Keyword><Keyword MajorTopicYN="Y">Staphylococcus aureus</Keyword><Keyword MajorTopicYN="Y">YpdA</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2019</Year><Month>03</Month><Day>27</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2019</Year><Month>05</Month><Day>08</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2019</Year><Month>05</Month><Day>15</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2019</Year><Month>5</Month><Day>24</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2019</Year><Month>5</Month><Day>24</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2019</Year><Month>5</Month><Day>24</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">31121222</ArticleId><ArticleId IdType="pii">S0891-5849(19)30511-8</ArticleId><ArticleId IdType="doi">10.1016/j.freeradbiomed.2019.05.018</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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