Elucidating Duramycin's Bacterial Selectivity and Mode of Action on the Bacterial Cell Envelope.
Identifieur interne : 000F26 ( Main/Exploration ); précédent : 000F25; suivant : 000F27Elucidating Duramycin's Bacterial Selectivity and Mode of Action on the Bacterial Cell Envelope.
Auteurs : Sahar Hasim [États-Unis] ; David P. Allison [États-Unis] ; Berlin Mendez [États-Unis] ; Abigail T. Farmer [États-Unis] ; Dale A. Pelletier [États-Unis] ; Scott T. Retterer [États-Unis] ; Shawn R. Campagna [États-Unis] ; Todd B. Reynolds [États-Unis] ; Mitchel J. Doktycz [États-Unis]Source :
- Frontiers in microbiology [ 1664-302X ] ; 2018.
Abstract
The use of naturally occurring antimicrobial peptides provides a promising route to selectively target pathogenic agents and to shape microbiome structure. Lantibiotics, such as duramycin, are one class of bacterially produced peptidic natural products that can selectively inhibit the growth of other bacteria. However, despite longstanding characterization efforts, the microbial selectivity and mode of action of duramycin are still obscure. We describe here a suite of biological, chemical, and physical characterizations that shed new light on the selective and mechanistic aspects of duramycin activity. Bacterial screening assays have been performed using duramycin and Populus-derived bacterial isolates to determine species selectivity. Lipidomic profiles of selected resistant and sensitive strains show that the sensitivity of Gram-positive bacteria depends on the presence of phosphatidylethanolamine (PE) in the cell membrane. Further the surface and interface morphology were studied by high resolution atomic force microscopy and showed a progression of cellular changes in the cell envelope after treatment with duramycin for the susceptible bacterial strains. Together, these molecular and cellular level analyses provide insight into duramycin's mode of action and a better understanding of its selectivity.
DOI: 10.3389/fmicb.2018.00219
PubMed: 29491859
PubMed Central: PMC5817074
Affiliations:
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Doktycz</name><affiliation wicri:level="2"><nlm:affiliation>Biosciences Division, Oak Ridge National Laboratory, Oak Ridge, TN, United States.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Biosciences Division, Oak Ridge National Laboratory, Oak Ridge, TN</wicri:regionArea><placeName><region type="state">Tennessee</region></placeName></affiliation><affiliation wicri:level="2"><nlm:affiliation>Center for Nanophase Materials Sciences, Oak Ridge National Laboratory, Oak Ridge, TN, United States.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Center for Nanophase Materials Sciences, Oak Ridge National Laboratory, Oak Ridge, TN</wicri:regionArea><placeName><region type="state">Tennessee</region></placeName></affiliation></author></analytic><series><title level="j">Frontiers in microbiology</title><idno type="ISSN">1664-302X</idno><imprint><date when="2018" type="published">2018</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The use of naturally occurring antimicrobial peptides provides a promising route to selectively target pathogenic agents and to shape microbiome structure. Lantibiotics, such as duramycin, are one class of bacterially produced peptidic natural products that can selectively inhibit the growth of other bacteria. However, despite longstanding characterization efforts, the microbial selectivity and mode of action of duramycin are still obscure. We describe here a suite of biological, chemical, and physical characterizations that shed new light on the selective and mechanistic aspects of duramycin activity. Bacterial screening assays have been performed using duramycin and <i>Populus</i>-derived bacterial isolates to determine species selectivity. Lipidomic profiles of selected resistant and sensitive strains show that the sensitivity of Gram-positive bacteria depends on the presence of phosphatidylethanolamine (PE) in the cell membrane. Further the surface and interface morphology were studied by high resolution atomic force microscopy and showed a progression of cellular changes in the cell envelope after treatment with duramycin for the susceptible bacterial strains. Together, these molecular and cellular level analyses provide insight into duramycin's mode of action and a better understanding of its selectivity.</div></front></TEI><pubmed><MedlineCitation Status="PubMed-not-MEDLINE" Owner="NLM"><PMID Version="1">29491859</PMID><DateRevised><Year>2020</Year><Month>09</Month><Day>30</Day></DateRevised><Article PubModel="Electronic-eCollection"><Journal><ISSN IssnType="Print">1664-302X</ISSN><JournalIssue CitedMedium="Print"><Volume>9</Volume><PubDate><Year>2018</Year></PubDate></JournalIssue><Title>Frontiers in microbiology</Title><ISOAbbreviation>Front Microbiol</ISOAbbreviation></Journal><ArticleTitle>Elucidating Duramycin's Bacterial Selectivity and Mode of Action on the Bacterial Cell Envelope.</ArticleTitle><Pagination><MedlinePgn>219</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.3389/fmicb.2018.00219</ELocationID><Abstract><AbstractText>The use of naturally occurring antimicrobial peptides provides a promising route to selectively target pathogenic agents and to shape microbiome structure. Lantibiotics, such as duramycin, are one class of bacterially produced peptidic natural products that can selectively inhibit the growth of other bacteria. However, despite longstanding characterization efforts, the microbial selectivity and mode of action of duramycin are still obscure. We describe here a suite of biological, chemical, and physical characterizations that shed new light on the selective and mechanistic aspects of duramycin activity. Bacterial screening assays have been performed using duramycin and <i>Populus</i>-derived bacterial isolates to determine species selectivity. Lipidomic profiles of selected resistant and sensitive strains show that the sensitivity of Gram-positive bacteria depends on the presence of phosphatidylethanolamine (PE) in the cell membrane. Further the surface and interface morphology were studied by high resolution atomic force microscopy and showed a progression of cellular changes in the cell envelope after treatment with duramycin for the susceptible bacterial strains. Together, these molecular and cellular level analyses provide insight into duramycin's mode of action and a better understanding of its selectivity.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Hasim</LastName><ForeName>Sahar</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Department of Microbiology, University of Tennessee, Knoxville, TN, United States.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Biosciences Division, Oak Ridge National Laboratory, Oak Ridge, TN, United States.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Allison</LastName><ForeName>David P</ForeName><Initials>DP</Initials><AffiliationInfo><Affiliation>Biosciences Division, Oak Ridge National Laboratory, Oak Ridge, TN, United States.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Department of Biochemistry, Cellular and Molecular Biology, University of Tennessee, Knoxville, TN, United States.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Mendez</LastName><ForeName>Berlin</ForeName><Initials>B</Initials><AffiliationInfo><Affiliation>Biosciences Division, Oak Ridge National Laboratory, Oak Ridge, TN, United States.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Farmer</LastName><ForeName>Abigail T</ForeName><Initials>AT</Initials><AffiliationInfo><Affiliation>Department of Chemistry, University of Tennessee, Knoxville, TN, United States.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Pelletier</LastName><ForeName>Dale A</ForeName><Initials>DA</Initials><AffiliationInfo><Affiliation>Biosciences Division, Oak Ridge National Laboratory, Oak Ridge, TN, United States.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Retterer</LastName><ForeName>Scott T</ForeName><Initials>ST</Initials><AffiliationInfo><Affiliation>Biosciences Division, Oak Ridge National Laboratory, Oak Ridge, TN, United States.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Center for Nanophase Materials Sciences, Oak Ridge National Laboratory, Oak Ridge, TN, United States.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Campagna</LastName><ForeName>Shawn R</ForeName><Initials>SR</Initials><AffiliationInfo><Affiliation>Department of Chemistry, University of Tennessee, Knoxville, TN, United States.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Reynolds</LastName><ForeName>Todd B</ForeName><Initials>TB</Initials><AffiliationInfo><Affiliation>Department of Microbiology, University of Tennessee, Knoxville, TN, United States.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Doktycz</LastName><ForeName>Mitchel J</ForeName><Initials>MJ</Initials><AffiliationInfo><Affiliation>Biosciences Division, Oak Ridge National Laboratory, Oak Ridge, TN, United States.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Center for Nanophase Materials Sciences, Oak Ridge National Laboratory, Oak Ridge, TN, United States.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2018</Year><Month>02</Month><Day>14</Day></ArticleDate></Article><MedlineJournalInfo><Country>Switzerland</Country><MedlineTA>Front Microbiol</MedlineTA><NlmUniqueID>101548977</NlmUniqueID><ISSNLinking>1664-302X</ISSNLinking></MedlineJournalInfo><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">atomic force microscopy (AFM)</Keyword><Keyword MajorTopicYN="N">cell elasticity</Keyword><Keyword MajorTopicYN="N">duramycin</Keyword><Keyword MajorTopicYN="N">lipid</Keyword><Keyword MajorTopicYN="N">lipidomics</Keyword><Keyword MajorTopicYN="N">molecular adhesion force</Keyword><Keyword MajorTopicYN="N">peptidoglycan</Keyword><Keyword MajorTopicYN="N">phosphatidylethanolamine (PE)</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2017</Year><Month>11</Month><Day>16</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2018</Year><Month>01</Month><Day>30</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2018</Year><Month>3</Month><Day>2</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2018</Year><Month>3</Month><Day>2</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2018</Year><Month>3</Month><Day>2</Day><Hour>6</Hour><Minute>1</Minute></PubMedPubDate></History><PublicationStatus>epublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">29491859</ArticleId><ArticleId IdType="doi">10.3389/fmicb.2018.00219</ArticleId><ArticleId 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IdType="pubmed">23669379</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></pubmed><affiliations><list><country><li>États-Unis</li></country><region><li>Tennessee</li></region></list><tree><country name="États-Unis"><region name="Tennessee"><name sortKey="Hasim, Sahar" sort="Hasim, Sahar" uniqKey="Hasim S" first="Sahar" last="Hasim">Sahar Hasim</name></region><name sortKey="Allison, David P" sort="Allison, David P" uniqKey="Allison D" first="David P" last="Allison">David P. Allison</name><name sortKey="Allison, David P" sort="Allison, David P" uniqKey="Allison D" first="David P" last="Allison">David P. Allison</name><name sortKey="Campagna, Shawn R" sort="Campagna, Shawn R" uniqKey="Campagna S" first="Shawn R" last="Campagna">Shawn R. Campagna</name><name sortKey="Doktycz, Mitchel J" sort="Doktycz, Mitchel J" uniqKey="Doktycz M" first="Mitchel J" last="Doktycz">Mitchel J. Doktycz</name><name sortKey="Doktycz, Mitchel J" sort="Doktycz, Mitchel J" uniqKey="Doktycz M" first="Mitchel J" last="Doktycz">Mitchel J. Doktycz</name><name sortKey="Farmer, Abigail T" sort="Farmer, Abigail T" uniqKey="Farmer A" first="Abigail T" last="Farmer">Abigail T. Farmer</name><name sortKey="Hasim, Sahar" sort="Hasim, Sahar" uniqKey="Hasim S" first="Sahar" last="Hasim">Sahar Hasim</name><name sortKey="Mendez, Berlin" sort="Mendez, Berlin" uniqKey="Mendez B" first="Berlin" last="Mendez">Berlin Mendez</name><name sortKey="Pelletier, Dale A" sort="Pelletier, Dale A" uniqKey="Pelletier D" first="Dale A" last="Pelletier">Dale A. Pelletier</name><name sortKey="Retterer, Scott T" sort="Retterer, Scott T" uniqKey="Retterer S" first="Scott T" last="Retterer">Scott T. Retterer</name><name sortKey="Retterer, Scott T" sort="Retterer, Scott T" uniqKey="Retterer S" first="Scott T" last="Retterer">Scott T. Retterer</name><name sortKey="Reynolds, Todd B" sort="Reynolds, Todd B" uniqKey="Reynolds T" first="Todd B" last="Reynolds">Todd B. Reynolds</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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