Copper stress in Staphylococcus aureus leads to adaptive changes in central carbon metabolism.
Identifieur interne : 000565 ( Main/Exploration ); précédent : 000564; suivant : 000566Copper stress in Staphylococcus aureus leads to adaptive changes in central carbon metabolism.
Auteurs : Emma Tarrant [Royaume-Uni] ; Gustavo P Riboldi ; Matthew R. Mcilvin ; Jack Stevenson ; Anna Barwinska-Sendra ; Louisa J. Stewart ; Mak A. Saito ; Kevin J. WaldronSource :
- Metallomics : integrated biometal science [ 1756-591X ] ; 2019.
Descripteurs français
- KwdFr :
- Anti-infectieux (métabolisme), Carbone (métabolisme), Cuivre (métabolisme), Glyceraldehyde 3-phosphate dehydrogenases (métabolisme), Humains (MeSH), Infections à staphylocoques (microbiologie), Protéines bactériennes (métabolisme), Staphylococcus aureus (croissance et développement), Staphylococcus aureus (métabolisme), Stress oxydatif (MeSH), Stress physiologique (MeSH).
- MESH :
- croissance et développement : Staphylococcus aureus.
- microbiologie : Infections à staphylocoques.
- métabolisme : Anti-infectieux, Carbone, Cuivre, Glyceraldehyde 3-phosphate dehydrogenases, Protéines bactériennes, Staphylococcus aureus.
- Humains, Stress oxydatif, Stress physiologique.
English descriptors
- KwdEn :
- Anti-Infective Agents (metabolism), Bacterial Proteins (metabolism), Carbon (metabolism), Copper (metabolism), Glyceraldehyde-3-Phosphate Dehydrogenases (metabolism), Humans (MeSH), Oxidative Stress (MeSH), Staphylococcal Infections (microbiology), Staphylococcus aureus (growth & development), Staphylococcus aureus (metabolism), Stress, Physiological (MeSH).
- MESH :
- chemical , metabolism : Anti-Infective Agents, Bacterial Proteins, Carbon, Copper, Glyceraldehyde-3-Phosphate Dehydrogenases.
- growth & development : Staphylococcus aureus.
- metabolism : Staphylococcus aureus.
- microbiology : Staphylococcal Infections.
- Humans, Oxidative Stress, Stress, Physiological.
Abstract
Copper toxicity has been a long-term selection pressure on bacteria due to its presence in the environment and its use as an antimicrobial agent by grazing protozoa, by phagocytic cells of the immune system, and in man-made medical and commercial products. There is recent evidence that exposure to increased copper stress may have been a key driver in the evolution and spread of methicillin-resistant Staphylococcus aureus, a globally important pathogen that causes significant mortality and morbidity worldwide. Yet it is unclear how S. aureus physiology is affected by copper stress or how it adapts in order to be able to grow in the presence of excess copper. Here, we have determined quantitatively how S. aureus alters its proteome during growth under copper stress conditions, comparing this adaptive response in two different types of growth regime. We found that the adaptive response involves induction of the conserved copper detoxification system as well as induction of enzymes of central carbon metabolism, with only limited induction of proteins involved in the oxidative stress response. Further, we identified a protein that binds copper inside S. aureus cells when stressed by copper excess. This copper-binding enzyme, a glyceraldehyde-3-phosphate dehydrogenase essential for glycolysis, is inhibited by copper in vitro and inside S. aureus cells. Together, our data demonstrate that copper stress leads to the inhibition of glycolysis in S. aureus, and that the bacterium adapts to this stress by altering its central carbon utilisation pathways.
DOI: 10.1039/c8mt00239h
PubMed: 30443649
PubMed Central: PMC6350627
Affiliations:
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Waldron</name></author></analytic><series><title level="j">Metallomics : integrated biometal science</title><idno type="eISSN">1756-591X</idno><imprint><date when="2019" type="published">2019</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Anti-Infective Agents (metabolism)</term><term>Bacterial Proteins (metabolism)</term><term>Carbon (metabolism)</term><term>Copper (metabolism)</term><term>Glyceraldehyde-3-Phosphate Dehydrogenases (metabolism)</term><term>Humans (MeSH)</term><term>Oxidative Stress (MeSH)</term><term>Staphylococcal Infections (microbiology)</term><term>Staphylococcus aureus (growth & development)</term><term>Staphylococcus aureus (metabolism)</term><term>Stress, Physiological (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Anti-infectieux (métabolisme)</term><term>Carbone (métabolisme)</term><term>Cuivre (métabolisme)</term><term>Glyceraldehyde 3-phosphate dehydrogenases (métabolisme)</term><term>Humains (MeSH)</term><term>Infections à staphylocoques (microbiologie)</term><term>Protéines bactériennes (métabolisme)</term><term>Staphylococcus aureus (croissance et développement)</term><term>Staphylococcus aureus (métabolisme)</term><term>Stress oxydatif (MeSH)</term><term>Stress physiologique (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Anti-Infective Agents</term><term>Bacterial Proteins</term><term>Carbon</term><term>Copper</term><term>Glyceraldehyde-3-Phosphate Dehydrogenases</term></keywords><keywords scheme="MESH" qualifier="croissance et développement" xml:lang="fr"><term>Staphylococcus aureus</term></keywords><keywords scheme="MESH" qualifier="growth & development" xml:lang="en"><term>Staphylococcus aureus</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Staphylococcus aureus</term></keywords><keywords scheme="MESH" qualifier="microbiologie" xml:lang="fr"><term>Infections à staphylocoques</term></keywords><keywords scheme="MESH" qualifier="microbiology" xml:lang="en"><term>Staphylococcal Infections</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Anti-infectieux</term><term>Carbone</term><term>Cuivre</term><term>Glyceraldehyde 3-phosphate dehydrogenases</term><term>Protéines bactériennes</term><term>Staphylococcus aureus</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Humans</term><term>Oxidative Stress</term><term>Stress, Physiological</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Humains</term><term>Stress oxydatif</term><term>Stress physiologique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Copper toxicity has been a long-term selection pressure on bacteria due to its presence in the environment and its use as an antimicrobial agent by grazing protozoa, by phagocytic cells of the immune system, and in man-made medical and commercial products. There is recent evidence that exposure to increased copper stress may have been a key driver in the evolution and spread of methicillin-resistant Staphylococcus aureus, a globally important pathogen that causes significant mortality and morbidity worldwide. Yet it is unclear how S. aureus physiology is affected by copper stress or how it adapts in order to be able to grow in the presence of excess copper. Here, we have determined quantitatively how S. aureus alters its proteome during growth under copper stress conditions, comparing this adaptive response in two different types of growth regime. We found that the adaptive response involves induction of the conserved copper detoxification system as well as induction of enzymes of central carbon metabolism, with only limited induction of proteins involved in the oxidative stress response. Further, we identified a protein that binds copper inside S. aureus cells when stressed by copper excess. This copper-binding enzyme, a glyceraldehyde-3-phosphate dehydrogenase essential for glycolysis, is inhibited by copper in vitro and inside S. aureus cells. Together, our data demonstrate that copper stress leads to the inhibition of glycolysis in S. aureus, and that the bacterium adapts to this stress by altering its central carbon utilisation pathways.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">30443649</PMID><DateCompleted><Year>2020</Year><Month>04</Month><Day>14</Day></DateCompleted><DateRevised><Year>2020</Year><Month>04</Month><Day>14</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Electronic">1756-591X</ISSN><JournalIssue CitedMedium="Internet"><Volume>11</Volume><Issue>1</Issue><PubDate><Year>2019</Year><Month>01</Month><Day>23</Day></PubDate></JournalIssue><Title>Metallomics : integrated biometal science</Title><ISOAbbreviation>Metallomics</ISOAbbreviation></Journal><ArticleTitle>Copper stress in Staphylococcus aureus leads to adaptive changes in central carbon metabolism.</ArticleTitle><Pagination><MedlinePgn>183-200</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1039/c8mt00239h</ELocationID><Abstract><AbstractText>Copper toxicity has been a long-term selection pressure on bacteria due to its presence in the environment and its use as an antimicrobial agent by grazing protozoa, by phagocytic cells of the immune system, and in man-made medical and commercial products. There is recent evidence that exposure to increased copper stress may have been a key driver in the evolution and spread of methicillin-resistant Staphylococcus aureus, a globally important pathogen that causes significant mortality and morbidity worldwide. Yet it is unclear how S. aureus physiology is affected by copper stress or how it adapts in order to be able to grow in the presence of excess copper. Here, we have determined quantitatively how S. aureus alters its proteome during growth under copper stress conditions, comparing this adaptive response in two different types of growth regime. We found that the adaptive response involves induction of the conserved copper detoxification system as well as induction of enzymes of central carbon metabolism, with only limited induction of proteins involved in the oxidative stress response. Further, we identified a protein that binds copper inside S. aureus cells when stressed by copper excess. This copper-binding enzyme, a glyceraldehyde-3-phosphate dehydrogenase essential for glycolysis, is inhibited by copper in vitro and inside S. aureus cells. Together, our data demonstrate that copper stress leads to the inhibition of glycolysis in S. aureus, and that the bacterium adapts to this stress by altering its central carbon utilisation pathways.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Tarrant</LastName><ForeName>Emma</ForeName><Initials>E</Initials><AffiliationInfo><Affiliation>Institute for Cell & Molecular Biosciences, Faculty of Medical Sciences, Newcastle University, Framlington Place, Newcastle upon Tyne, NE2 4HH, UK. kevin.waldron@ncl.ac.uk.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>P Riboldi</LastName><ForeName>Gustavo</ForeName><Initials>G</Initials></Author><Author ValidYN="Y"><LastName>McIlvin</LastName><ForeName>Matthew R</ForeName><Initials>MR</Initials></Author><Author ValidYN="Y"><LastName>Stevenson</LastName><ForeName>Jack</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Barwinska-Sendra</LastName><ForeName>Anna</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Stewart</LastName><ForeName>Louisa J</ForeName><Initials>LJ</Initials></Author><Author ValidYN="Y"><LastName>Saito</LastName><ForeName>Mak A</ForeName><Initials>MA</Initials></Author><Author ValidYN="Y"><LastName>Waldron</LastName><ForeName>Kevin J</ForeName><Initials>KJ</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>098375/Z/12/Z</GrantID><Acronym>WT_</Acronym><Agency>Wellcome Trust</Agency><Country>United Kingdom</Country></Grant><Grant><GrantID>BB/F015895/1</GrantID><Acronym>BB_</Acronym><Agency>Biotechnology and Biological Sciences Research Council</Agency><Country>United Kingdom</Country></Grant><Grant><GrantID>BB/J014516/1</GrantID><Acronym>BB_</Acronym><Agency>Biotechnology and Biological Sciences Research Council</Agency><Country>United Kingdom</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Metallomics</MedlineTA><NlmUniqueID>101478346</NlmUniqueID><ISSNLinking>1756-5901</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000890">Anti-Infective Agents</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D001426">Bacterial Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>7440-44-0</RegistryNumber><NameOfSubstance UI="D002244">Carbon</NameOfSubstance></Chemical><Chemical><RegistryNumber>789U1901C5</RegistryNumber><NameOfSubstance UI="D003300">Copper</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.2.1.-</RegistryNumber><NameOfSubstance 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MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018384" MajorTopicYN="N">Oxidative Stress</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013203" MajorTopicYN="N">Staphylococcal Infections</DescriptorName><QualifierName UI="Q000382" MajorTopicYN="Y">microbiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013211" MajorTopicYN="N">Staphylococcus aureus</DescriptorName><QualifierName UI="Q000254" MajorTopicYN="Y">growth & development</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013312" MajorTopicYN="N">Stress, Physiological</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate 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Mcilvin</name><name sortKey="P Riboldi, Gustavo" sort="P Riboldi, Gustavo" uniqKey="P Riboldi G" first="Gustavo" last="P Riboldi">Gustavo P Riboldi</name><name sortKey="Saito, Mak A" sort="Saito, Mak A" uniqKey="Saito M" first="Mak A" last="Saito">Mak A. Saito</name><name sortKey="Stevenson, Jack" sort="Stevenson, Jack" uniqKey="Stevenson J" first="Jack" last="Stevenson">Jack Stevenson</name><name sortKey="Stewart, Louisa J" sort="Stewart, Louisa J" uniqKey="Stewart L" first="Louisa J" last="Stewart">Louisa J. Stewart</name><name sortKey="Waldron, Kevin J" sort="Waldron, Kevin J" uniqKey="Waldron K" first="Kevin J" last="Waldron">Kevin J. Waldron</name></noCountry><country name="Royaume-Uni"><noRegion><name sortKey="Tarrant, Emma" sort="Tarrant, Emma" uniqKey="Tarrant E" first="Emma" last="Tarrant">Emma Tarrant</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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