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dc.contributor.authorZaric, Svetislav
dc.contributor.authorLappin, MJ
dc.contributor.authorFulton, CR
dc.contributor.authorLundy, FT
dc.contributor.authorCoulter, WA
dc.contributor.authorIrwin, CR
dc.date.accessioned2017-02-17T19:45:55Z
dc.date.available2017-02-17T19:45:55Z
dc.date.issued2017-02-16
dc.identifier.issn1753-4259
dc.identifier.issn1753-4267
dc.identifier.urihttp://hdl.handle.net/10026.1/8534
dc.description.abstract

Porphyromonas gingivalis produces different LPS isoforms with significant structural variations of their lipid A and O-antigen moieties that can affect its pro-inflammatory and bone-resorbing potential. We show here, for the first time, that P. gingivalis LPS isolated from W83 strain is highly sialylated and possesses significantly reduced inflammatory potential compared with less sialylated ATCC 33277 strain LPS. Nevertheless, the reduction in the endotoxin activity is not mediated by the presence of sialic acid LPS moieties as the sialic acid-free LPS produced by the mutant W83 strain exhibits a similar inflammatory potential to the wild type strain. Furthermore, our findings suggest that the interaction between the sialic acid LPS moieties and the inhibitory CD33 receptor is prevented by endogenously expressed sialic acid on the surface of THP-1 cells that cannot be out-competed by sialic acid containing P. gingivalis LPS. The present study also highlights the importance of endogenous sialic acid as a 'self-associated molecular pattern' and CD33 receptors in modulation of innate immune response as human gingival fibroblasts, which do not express CD33 receptors, and desialylated THP-1 cells have both been found to have much higher spontaneous IL-8 production than naïve THP-1 cells.

dc.format.extent1753425917694245-1753425917694245
dc.format.mediumPrint-Electronic
dc.languageen
dc.language.isoen
dc.publisherSAGE Publications
dc.subjectInflammation
dc.subjectLPS
dc.subjectPorphyromonas gingivalis
dc.subjectperiodontal diseases
dc.subjectsialic acid
dc.titleSialylation of Porphyromonas gingivalis LPS and its effect on bacterial-host interactions.
dc.typejournal-article
dc.typeJournal Article
plymouth.author-urlhttps://www.ncbi.nlm.nih.gov/pubmed/28205451
plymouth.issue3
plymouth.volume23
plymouth.publication-statusPublished online
plymouth.journalInnate Immun
dc.identifier.doi10.1177/1753425917694245
plymouth.organisational-group/Plymouth
plymouth.organisational-group/Plymouth/Faculty of Health
plymouth.organisational-group/Plymouth/Research Groups
plymouth.organisational-group/Plymouth/Research Groups/Institute of Translational and Stratified Medicine (ITSMED)
plymouth.organisational-group/Plymouth/Research Groups/Institute of Translational and Stratified Medicine (ITSMED)/CBR
plymouth.organisational-group/Plymouth/Users by role
dc.publisher.placeUnited States
dcterms.dateAccepted2017-01-17
dc.identifier.eissn1753-4267
dc.rights.embargoperiodNo embargo
rioxxterms.versionofrecord10.1177/1753425917694245
rioxxterms.licenseref.urihttp://www.rioxx.net/licenses/all-rights-reserved
rioxxterms.licenseref.startdate2017-02-16
rioxxterms.typeJournal Article/Review


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