Role of glycolipids in the pathogenesis of Enterococcus faecalis urinary tract infection

Abstract: BackgroundAfter uropathogenic Escherichia coli (UPEC), Enterococcus faecalis is the second most common pathogen causing urinary tract infections. Monoglucosyl-diacylglycerol (MGlcDAG) and diglucosyl-diacylglycerol (DGlcDAG) are the main glycolipids of the E. faecalis cell membrane. Examination of two mutants in genes bgsB and bgsA (both glycosyltransferases) showed that these genes are involved in cell membrane glycolipid biosynthesis, and that their inactivation leads to loss of glycolipids DGlcDAG (bgsA) or both MGlcDAG and DGlcDAG (bgsB). Here we investigate the function of bgsB and bgsA regarding their role in the pathogenesis in a mouse model of urinary tract infection and in bacterial adhesion to T24 bladder epithelial cells.ResultsIn a mouse model of urinary tract infection, we showed that E. faecalis 12030ΔbgsB and E. faecalis 12030ΔbgsA mutants, colonize uroepithelial surfaces more efficiently than wild-type bacteria. We also demonstrated that these mutants showed a more than three-fold increased binding to human bladder carcinoma cells line T24 compared to the wild-type strain. Bacterial binding could be specifically inhibited by purified glycolipids. Lipoteichoic acid (LTA), wall-teichoic acid (WTA), and glycosaminoglycans (GAGs) were not significantly involved in binding of E. faecalis to the bladder epithelial cell line.ConclusionsOur data show that the deletion of bgsB and bgsA and the absence of the major glycolipid diglucosyl-diacylglycerol increases colonization and binding to uroepithelial cells. We hypothesize that secreted diglucosyl-diacylglycerol blocks host binding sites, thereby preventing bacterial adhesion. Further experiments will be needed to clarify the exact mechanism underlying the adhesion through glycolipids and their cognate receptors

Standort
Deutsche Nationalbibliothek Frankfurt am Main
Umfang
Online-Ressource
Sprache
Englisch
Anmerkungen
PLoS ONE. 9, 5 (2014), e96295, DOI 10.1371/journal.pone.0096295, issn: 1932-6203
IN COPYRIGHT http://rightsstatements.org/page/InC/1.0 rs

Klassifikation
Medizin, Gesundheit
Schlagwort
Streptococcus faecalis
Glykolipide
Blase
Lyasen
Heparin
Infektion
Infektiologie

Ereignis
Veröffentlichung
(wo)
Freiburg
(wer)
Universität
(wann)
2014
Urheber

DOI
10.1371/journal.pone.0096295
URN
urn:nbn:de:bsz:25-freidok-119984
Rechteinformation
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Letzte Aktualisierung
15.08.2025, 07:20 MESZ

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  • 2014

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