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Conference Paper: Controlled redox and hemin utilization essential for Porphyromonas gingivalis persistence

TitleControlled redox and hemin utilization essential for Porphyromonas gingivalis persistence
Authors
Issue Date2016
PublisherSage Publications, Inc. The Journal's web site is located at http://jdr.sagepub.com/
Citation
The 94th General Session & Exhibition of the IADR, 3rd Meeting of the IADR Asia Pacific Region & 35th Annual Meeting of the IADR Korean Division, Seoul, Korea, 22-25 June 2016. In Journal of Dental Research, 2016, v. 95 Spec. Iss. B, abstract no. 892 How to Cite?
AbstractOBJECTIVES: Antibiotic-tolerant bacterial persisters critically account for common long-lasting complex infections and inflammation. Our recent in vitro study shows for the first time the presence of metronidazole-tolerant P. gingivalis persisters and hemin as an important modifier of these noxious persisters. This study further investigated the underlying survival mechanisms of P. gingivalis persisters by shotgun proteomics. METHODS: P. gingivalis ATCC 33277 was cultured anaerobically in broth containing 10μg/ml of hemin, and treated with 100μg/ml of metronidazole for 6 h. Subsequently, cellular proteins were extracted from the P. gingivalis persister fractions and controls followed by in solution digestion with trypsin. The resulting peptides were loaded on an LTQ-Orbitrap system and analyzed by LC-MS/MS. The proteomic data were subjected to statistical and bioinformatical analysis. RESULTS: Over 300 proteins were identified, and their expression was to different extent altered in the metronidazole-tolerant P. gingivalis persisters, with reference to the controls. Notably, the persisters exhibited significantly decreased protein expression of pyruvate:ferredoxin oxidoreductase (PFOR, e.g. PGN_1530 and PGN_1753) that is crucial for the activation of metronidazole. Additional proteins responsible for redox regulation (e.g. PGN_0033 and PGN_0302) were differentially expressed in the persisters. Interestingly, the hemin/iron uptake-associated proteins such as PGN_0659 and PGN_0728 were markedly downregulated, whereas a key iron-storage protein (PGN_0604) was significantly upregulated, which could result in reduced biosynthesis of redox-active proteins and impaired activation of metronidazole. CONCLUSIONS: This pioneering study demonstrates that regulation of cellular redox state may be essential for the tolerance of P. gingivalis persisters to metronidazole, and repression of hemin/iron utilization could contribute to the survival of these persisters.
DescriptionOral Session - Microbiology/Immunology-Host Response to Pathogens: no. 892
Persistent Identifierhttp://hdl.handle.net/10722/227498
ISSN
2015 Impact Factor: 4.602
2015 SCImago Journal Rankings: 1.714

 

DC FieldValueLanguage
dc.contributor.authorLi, P-
dc.contributor.authorFung, EYM-
dc.contributor.authorSeneviratne, C-
dc.contributor.authorChe, CM-
dc.contributor.authorJin, L-
dc.date.accessioned2016-07-18T09:11:04Z-
dc.date.available2016-07-18T09:11:04Z-
dc.date.issued2016-
dc.identifier.citationThe 94th General Session & Exhibition of the IADR, 3rd Meeting of the IADR Asia Pacific Region & 35th Annual Meeting of the IADR Korean Division, Seoul, Korea, 22-25 June 2016. In Journal of Dental Research, 2016, v. 95 Spec. Iss. B, abstract no. 892-
dc.identifier.issn0022-0345-
dc.identifier.urihttp://hdl.handle.net/10722/227498-
dc.descriptionOral Session - Microbiology/Immunology-Host Response to Pathogens: no. 892-
dc.description.abstractOBJECTIVES: Antibiotic-tolerant bacterial persisters critically account for common long-lasting complex infections and inflammation. Our recent in vitro study shows for the first time the presence of metronidazole-tolerant P. gingivalis persisters and hemin as an important modifier of these noxious persisters. This study further investigated the underlying survival mechanisms of P. gingivalis persisters by shotgun proteomics. METHODS: P. gingivalis ATCC 33277 was cultured anaerobically in broth containing 10μg/ml of hemin, and treated with 100μg/ml of metronidazole for 6 h. Subsequently, cellular proteins were extracted from the P. gingivalis persister fractions and controls followed by in solution digestion with trypsin. The resulting peptides were loaded on an LTQ-Orbitrap system and analyzed by LC-MS/MS. The proteomic data were subjected to statistical and bioinformatical analysis. RESULTS: Over 300 proteins were identified, and their expression was to different extent altered in the metronidazole-tolerant P. gingivalis persisters, with reference to the controls. Notably, the persisters exhibited significantly decreased protein expression of pyruvate:ferredoxin oxidoreductase (PFOR, e.g. PGN_1530 and PGN_1753) that is crucial for the activation of metronidazole. Additional proteins responsible for redox regulation (e.g. PGN_0033 and PGN_0302) were differentially expressed in the persisters. Interestingly, the hemin/iron uptake-associated proteins such as PGN_0659 and PGN_0728 were markedly downregulated, whereas a key iron-storage protein (PGN_0604) was significantly upregulated, which could result in reduced biosynthesis of redox-active proteins and impaired activation of metronidazole. CONCLUSIONS: This pioneering study demonstrates that regulation of cellular redox state may be essential for the tolerance of P. gingivalis persisters to metronidazole, and repression of hemin/iron utilization could contribute to the survival of these persisters.-
dc.languageeng-
dc.publisherSage Publications, Inc. The Journal's web site is located at http://jdr.sagepub.com/-
dc.relation.ispartofJournal of Dental Research-
dc.rightsJournal of Dental Research. Copyright © Sage Publications, Inc.-
dc.titleControlled redox and hemin utilization essential for Porphyromonas gingivalis persistence-
dc.typeConference_Paper-
dc.identifier.emailFung, EYM: eva.fungym@hku.hk-
dc.identifier.emailChe, CM: chemhead@hku.hk-
dc.identifier.emailJin, L: ljjin@hkucc.hku.hk-
dc.identifier.authorityFung, EYM=rp01986-
dc.identifier.authorityChe, CM=rp00670-
dc.identifier.authorityJin, L=rp00028-
dc.identifier.hkuros259741-
dc.identifier.volume95-
dc.identifier.issueSpec. Iss. B-
dc.publisher.placeUnited States-

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