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Novel interactions of glycosaminoglycans and bacterial glycolipids mediate binding of enterococci to human cells

dc.rights.licenseOpen Access
dc.rights.licenseA full text version is available in DSpace@RPI
dc.contributor.authorSava, Irina G.
dc.contributor.authorZhang, Fuming
dc.contributor.authorToma, Ioana
dc.contributor.authorTheilacker, Christian
dc.contributor.authorLi, Boyangzhi
dc.contributor.authorBaumert, Thomas F.
dc.contributor.authorHolst, Otto
dc.contributor.authorLinhardt, Robert J.
dc.contributor.authorHuebner, Johannes
dc.date2009
dc.date.accessioned2022-06-23T01:38:25Z
dc.date.available2022-06-23T01:38:25Z
dc.date.issued2009-07-03
dc.identifier.citationNovel interactions of glycosaminoglycans and bacterial glycolipids mediate binding of enterococci to human cells, I. G. Sava, F. Zhang, I. Toma, C. Theilacker, B. Li, T. F. Baumert, O. Holst, R. J. Linhardt, J. Huebner, Journal of Biological Chemistry, 284, 18194 - 18201, 2009.
dc.identifier.issn1083351X
dc.identifier.issn219258
dc.identifier.urihttps://doi.org/10.1074/jbc.M901460200
dc.descriptionJournal of Biological Chemistry, 284, 18194-18201
dc.descriptionNote : if this item contains full text it may be a preprint, author manuscript, or a Gold OA copy that permits redistribution with a license such as CC BY. The final version is available through the publisher’s platform.
dc.description.abstractEnterococcus faecalis is among the most important nosocomial pathogens. The intestinal mucosa is considered to be the main site used by these bacteria for entrance and dissemination. A better understanding of the mechanisms involved in colonization and invasion of enterococci may help to devise methods to prevent infections in hospitalized patients. Glycosaminoglycans, which are present on the surface of all eukaryotic cells, were investigated with regard to their role as host receptors for adhesion of E. faecalis. Competitive binding assays, enzymatic digestion, and reduction of the sulfation of the glycosaminoglycan chains indicated that heparin and heparan sulfate, but not chondroitin sulfate B, played important roles in adhesion of E. faecalis 12030 to Caco2 cells. By using proteinases and carbohydrate oxidation by sodium meta-periodate to modify the bacterial surface, it could be demonstrated that a sugar-containing molecule rather than a protein is the bacterial ligand mediating adhesion to eukaryotic cells. Preincubation of Caco2 cells with the enterococcal glycolipid diglucosyldiacylglycerol but not other carbohydrate cell wall components inhibited bacterial binding. These results may indicate that heparin and/or heparan sulfate on host epithelial cells and diglucosyldiacylglycerol, either itself or as a partial structure of lipoteichoic acid, are involved in enterococcal adhesion to colonic epithelia, the first step in translocation from the intestinal tract.
dc.description.sponsorshipNational Institute of General Medical Sciences
dc.languageENG
dc.language.isoen_US
dc.publisherElsevier
dc.relation.ispartofThe Linhardt Research Labs Online Collection
dc.relation.ispartofRensselaer Polytechnic Institute, Troy, NY
dc.relation.ispartofJournal of Biological Chemistry
dc.relation.urihttps://harc.rpi.edu/
dc.rightsAttribution 3.0 United States*
dc.rights.urihttp://creativecommons.org/licenses/by/3.0/us/*
dc.subjectBiology
dc.subjectChemistry and chemical biology
dc.subjectChemical and biological engineering
dc.subjectBiomedical engineering
dc.titleNovel interactions of glycosaminoglycans and bacterial glycolipids mediate binding of enterococci to human cellsen_US
dc.titleNovel interactions of glycosaminoglycans and bacterial glycolipids mediate binding of enterococci to human cells
dc.typeArticle
dcterms.accessRightsA full text version is available in DSpace@RPI
dcterms.isPartOfJournal
dcterms.isVersionOfhttps://doi.org/10.1074/jbc.M901460200
dc.rights.holderCC BY : this license allows reusers to distribute, remix, adapt, and build upon the material in any medium or format, so long as attribution is given to the creator. The license allows for commercial use. Credit must be given to the authors and the original work must be properly cited.
dc.creator.identifierhttps://orcid.org/0000-0003-2219-5833
dc.relation.departmentThe Linhardt Research Labs.
dc.relation.departmentThe Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS)
rpi.description.pages18194-18201
rpi.description.volume284


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