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dc.contributor.authorParveen, Nikhat
dc.contributor.authorRobbins, Douglas
dc.contributor.authorLeong, John M.
dc.date2022-08-11T08:10:03.000
dc.date.accessioned2022-08-23T16:53:24Z
dc.date.available2022-08-23T16:53:24Z
dc.date.issued1999-03-20
dc.date.submitted2008-07-15
dc.identifier.citationInfect Immun. 1999 Apr;67(4):1743-9.
dc.identifier.issn0019-9567 (Print)
dc.identifier.pmid10085013
dc.identifier.urihttp://hdl.handle.net/20.500.14038/42265
dc.description.abstractLyme disease, a chronic multisystemic disorder that can affect the skin, heart, joints, and nervous system is caused by Borrelia burgdorferi sensu lato. Lyme disease spirochetes were previously shown to bind glycosaminoglycans (GAGs). In the current study, the GAG-binding properties of eight Lyme disease strains were determined. Binding by two high-passage HB19 derivatives to Vero cells could not be inhibited by enzymatic removal of GAGs or by the addition of exogenous GAG. The other six strains, which included a different high-passage HB19 derivative (HB19 clone 1), were shown to recognize both heparan sulfate and dermatan sulfate in cell-binding assays, but the relative efficiency of binding to these two GAGs varied among the strains. Strains N40, CA20-2A, and PBi bound predominantly to heparan sulfate, PBo bound both heparan sulfate and dermatan sulfate roughly equally, and VS461 and HB19 clone 1 recognized primarily dermatan sulfate. Cell binding by strain HB19 clone 1 was inhibited better by exogenous dermatan sulfate than by heparin, whereas heparin was the better inhibitor of binding by strain N40. The GAG-binding preference of a Lyme disease strain was reflected in its cell-type-specific binding. Strains that recognized predominantly heparan sulfate bound efficiently to both C6 glioma cells and EA-Hy926 cells, whereas strains that recognized predominantly dermatan sulfate bound well only to the glial cells. The effect of lyase treatment of these cells on bacterial binding was consistent with the model that cell-type-specific binding was a reflection of the GAG-binding preference. We conclude that the GAG-binding preference varies with the strain of Lyme disease spirochete and that this variation influences cell-type-specific binding in vitro.
dc.language.isoen_US
dc.relation<a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=10085013&dopt=Abstract">Link to Article in PubMed</a>
dc.subjectAnimals
dc.subjectBacterial Adhesion
dc.subjectBorrelia burgdorferi Group
dc.subjectCercopithecus aethiops
dc.subjectEndothelium, Vascular
dc.subjectGlycosaminoglycans
dc.subjectHumans
dc.subjectLyme Disease
dc.subjectNeuroglia
dc.subjectRats
dc.subjectSpirochaetales
dc.subjectVero Cells
dc.subjectMicrobiology
dc.subjectMolecular Genetics
dc.titleStrain variation in glycosaminoglycan recognition influences cell-type-specific binding by lyme disease spirochetes
dc.typeJournal Article
dc.source.journaltitleInfection and immunity
dc.source.volume67
dc.source.issue4
dc.identifier.legacyfulltexthttps://escholarship.umassmed.edu/cgi/viewcontent.cgi?article=1627&amp;context=oapubs&amp;unstamped=1
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/oapubs/628
dc.identifier.contextkey549057
refterms.dateFOA2022-08-23T16:53:24Z
html.description.abstract<p>Lyme disease, a chronic multisystemic disorder that can affect the skin, heart, joints, and nervous system is caused by Borrelia burgdorferi sensu lato. Lyme disease spirochetes were previously shown to bind glycosaminoglycans (GAGs). In the current study, the GAG-binding properties of eight Lyme disease strains were determined. Binding by two high-passage HB19 derivatives to Vero cells could not be inhibited by enzymatic removal of GAGs or by the addition of exogenous GAG. The other six strains, which included a different high-passage HB19 derivative (HB19 clone 1), were shown to recognize both heparan sulfate and dermatan sulfate in cell-binding assays, but the relative efficiency of binding to these two GAGs varied among the strains. Strains N40, CA20-2A, and PBi bound predominantly to heparan sulfate, PBo bound both heparan sulfate and dermatan sulfate roughly equally, and VS461 and HB19 clone 1 recognized primarily dermatan sulfate. Cell binding by strain HB19 clone 1 was inhibited better by exogenous dermatan sulfate than by heparin, whereas heparin was the better inhibitor of binding by strain N40. The GAG-binding preference of a Lyme disease strain was reflected in its cell-type-specific binding. Strains that recognized predominantly heparan sulfate bound efficiently to both C6 glioma cells and EA-Hy926 cells, whereas strains that recognized predominantly dermatan sulfate bound well only to the glial cells. The effect of lyase treatment of these cells on bacterial binding was consistent with the model that cell-type-specific binding was a reflection of the GAG-binding preference. We conclude that the GAG-binding preference varies with the strain of Lyme disease spirochete and that this variation influences cell-type-specific binding in vitro.</p>
dc.identifier.submissionpathoapubs/628
dc.contributor.departmentDepartment of Molecular Genetics and Microbiology
dc.source.pages1743-9


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