Show simple item record

dc.contributor.authorDashper, SG
dc.contributor.authorButler, CA
dc.contributor.authorLissel, JP
dc.contributor.authorPaolini, RA
dc.contributor.authorHoffmann, B
dc.contributor.authorVeith, PD
dc.contributor.authorO'Brien-Simpson, NM
dc.contributor.authorSnelgrove, SL
dc.contributor.authorTsiros, JT
dc.contributor.authorReynolds, EC
dc.date.available2014-05-21T19:37:37Z
dc.date.issued2005-07-29
dc.identifierpii: M503896200
dc.identifier.citationDashper, S. G., Butler, C. A., Lissel, J. P., Paolini, R. A., Hoffmann, B., Veith, P. D., O'Brien-Simpson, N. M., Snelgrove, S. L., Tsiros, J. T. & Reynolds, E. C. (2005). A novel Porphyromonas gingivalis FeoB plays a role in manganese accumulation. JOURNAL OF BIOLOGICAL CHEMISTRY, 280 (30), pp.28095-28102. https://doi.org/10.1074/jbc.M503896200.
dc.identifier.issn0021-9258
dc.identifier.urihttp://hdl.handle.net/11343/26552
dc.descriptionC1 - Journal Articles Refereed
dc.description.abstractFeoB is an atypical transporter that has been shown to exclusively mediate ferrous ion transport in some bacteria. Unusually the genome of the periodontal pathogen Porphyromonas gingivalis has two genes (feoB1 and feoB2) encoding FeoB homologs, both of which are expressed in bicistronic operons. Kinetic analysis of ferrous ion transport by P. gingivalis W50 revealed the presence of a single, high affinity system with a K(t) of 0.31 microM. FeoB1 was found to be solely responsible for this transport as energized cells of the isogenic FeoB1 mutant (W50FB1) did not transport radiolabeled iron, while the isogenic FeoB2 mutant (W50FB2) transported radiolabeled iron at a rate similar to wild type. This was reflected in the iron content of W50FB1 grown in iron excess conditions which was approximately half that of the wild type and W50FB2. The W50FB1 mutant had increased sensitivity to both oxygen and hydrogen peroxide and was avirulent in an animal model of infection whereas W50FB2 exhibited the same virulence as the wild type. Analysis of manganous ion uptake using inductively coupled plasma-mass spectrometry revealed a greater than 3-fold decrease in intracellular manganese accumulation in W50FB2 which was also unable to grow in manganese-limited media. The protein co-expressed with FeoB2 appears to be a novel FeoA-MntR fusion protein that exhibits homology to a manganese-responsive, DNA-binding metalloregulatory protein. These results indicate that FeoB2 is not involved in iron transport but plays a novel role in manganese transport.
dc.formatapplication/pdf
dc.languageEnglish
dc.publisherAMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
dc.subjectAnalytical Biochemistry; Bacteriology ; Treatments (e.g. Chemicals
dc.subjectAntibiotics); Dental Health
dc.titleA novel Porphyromonas gingivalis FeoB plays a role in manganese accumulation
dc.typeJournal Article
dc.identifier.doi10.1074/jbc.M503896200
melbourne.peerreviewPeer Reviewed
melbourne.affiliationThe University of Melbourne
melbourne.affiliation.departmentDental Science
melbourne.source.titleJOURNAL OF BIOLOGICAL CHEMISTRY
melbourne.source.volume280
melbourne.source.issue30
melbourne.source.pages28095-28102
dc.research.coderfcd270101
dc.research.coderfcd270301
dc.research.codeseo1998670403
dc.research.codeseo1998730214
melbourne.publicationid41715
melbourne.elementsid271776
melbourne.contributor.authorDashper, Stuart
melbourne.contributor.authorButler, Catherine
melbourne.contributor.authorPaolini, Rita
melbourne.contributor.authorHoffmann, Brigitte
melbourne.contributor.authorVeith, Paul
melbourne.contributor.authorO'Brien-Simpson, Neil
melbourne.contributor.authorReynolds, Eric
melbourne.contributor.authorLISSEL, JASMIN
melbourne.contributor.authorSNELGROVE, SARAH LOUISE
dc.identifier.eissn1083-351X
melbourne.accessrightsThis item is currently not available from this repository


Files in this item

FilesSizeFormatView

There are no files associated with this item.

This item appears in the following Collection(s)

Show simple item record