Please use this identifier to cite or link to this item: http://bura.brunel.ac.uk/handle/2438/15140
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dc.contributor.authorPeak, IR-
dc.contributor.authorChen, A-
dc.contributor.authorJen, FE-C-
dc.contributor.authorJennings, C-
dc.contributor.authorSchuiz, BL-
dc.contributor.authorSaunders, NJ-
dc.contributor.authorKhan, A-
dc.contributor.authorSeifert, HS-
dc.contributor.authorJennings, MP-
dc.date.accessioned2017-09-12T13:26:21Z-
dc.date.available2016-08-01-
dc.date.available2017-09-12T13:26:21Z-
dc.date.issued2016-
dc.identifier.citationJOURNAL OF PROTEOME RESEARCH, 2016, 15 (8), pp. 2356 - 2365 (10)en_US
dc.identifier.issnhttp://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000381235900002&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=f12c8c83318cf2733e615e54d9ed7ad5-
dc.identifier.issnhttp://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000381235900002&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=f12c8c83318cf2733e615e54d9ed7ad5-
dc.identifier.issnhttp://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000381235900002&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=f12c8c83318cf2733e615e54d9ed7ad5-
dc.identifier.issn1535-3893-
dc.identifier.issn1535-3907-
dc.identifier.urihttp://bura.brunel.ac.uk/handle/2438/15140-
dc.description.abstractThe bacterial pathogen Neisseria meningitidis expresses two major outer-membrane porins. PorA expression is subject to phase-variation (high frequency, random, on-off switching) and both PorA and PorB are antigenically variable between strains. PorA expression is variable and not correlated with meningococcal colonisation or invasive disease, whereas all naturally-occurring strains express PorB suggesting strong selection for expression. We have generated N. meningitidis strains lacking expression of both major porins, demonstrating that they are dispensable for bacterial growth in vitro. The porAB mutant strain has an exponential growth rate similar to the parental strain, as do the single porA or porB mutants, but the porAB mutant strain does not reach the same cell density in stationary phase. Proteomic analysis suggests that the double mutant strain exhibits compensatory expression changes in proteins associated with cellular redox state, energy/nutrient metabolism, and membrane stability. On solid media, there is obvious growth impairment that is rescued by addition of blood or serum from mammalian species, particularly heme. These porin mutants are not impaired in their capacity to inhibit both staurosporine-induced apoptosis and a phorbol 12-myristate 13-acetate -induced oxidative burst in human neutrophils suggesting that the porins are not the only bacterial factors that can modulate these processes in host cells.en_US
dc.description.sponsorshipMPJ received funding from NHMRC program grant 565526, NHMRC program grant 1071659, and ARC Discovery Project grant 13010314. HSS received funding from NIH grants R01 AI044239 and R37 AI033493 to HSSen_US
dc.format.extent2356 - 2365 (10)-
dc.languageEnglish-
dc.language.isoenen_US
dc.publisherAMER CHEMICAL SOCen_US
dc.subjectScience & Technologyen_US
dc.subjectLife Sciences & Biomedicineen_US
dc.subjectBiochemical Research Methodsen_US
dc.subjectBiochemistry & Molecular Biologyen_US
dc.subjectNeisseria meningitidisen_US
dc.subjectPorinsen_US
dc.subjectPorAen_US
dc.subjectPorBen_US
dc.subjectOUTER-MEMBRANE PORINen_US
dc.subjectPOLYMORPHONUCLEAR LEUKOCYTESen_US
dc.subjectVARIABLE EXPRESSIONen_US
dc.subjectMASS-SPECTROMETRYen_US
dc.subjectEPITHELIAL-CELLSen_US
dc.subjectPROTECTS CELLSen_US
dc.subjectTARGET-CELLSen_US
dc.subjectGONORRHOEAEen_US
dc.subjectGLYCOSYLATIONen_US
dc.subjectMITOCHONDRIAen_US
dc.titleNeisseria meningitidis Lacking the Major Porins PorA and PorB Is Viable and Modulates Apoptosis and the Oxidative Burst of Neutrophilsen_US
dc.typeArticleen_US
dc.identifier.doihttp://dx.doi.org/10.1021/acs.jproteome.5b00938-
dc.relation.isPartOfJOURNAL OF PROTEOME RESEARCH-
pubs.issue8-
pubs.publication-statusPublished-
pubs.volume15-
Appears in Collections:Dept of Mechanical Aerospace and Civil Engineering Research Papers

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