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    Structural requirements for glycosaminoglycan recognition by the Lyme disease spirochete, Borrelia burgdorferi

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    Authors
    Leong, John M.
    Robbins, Douglas
    Rosenfeld, Louis
    Lahiri, Biswajit
    Parveen, Nikhat
    UMass Chan Affiliations
    Department of Molecular Genetics and Microbiology
    Document Type
    Journal Article
    Publication Date
    1998-11-24
    Keywords
    Animals
    *Bacterial Adhesion
    Binding, Competitive
    *Borrelia burgdorferi
    Borrelia burgdorferi Group
    Cercopithecus aethiops
    Glycosaminoglycans
    Hemagglutination Tests
    Heparin
    Structure-Activity Relationship
    Vero Cells
    Microbiology
    Molecular Genetics
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    Abstract
    Borrelia burgdorferi, the Lyme disease agent, binds glycosaminoglycans (GAGs) such as heparin, heparan sulfate, and dermatan sulfate. Heparin or heparan sulfate fractions separated by size or charge were tested for their ability to inhibit attachment of B. burgdorferi to Vero cells. GAG chains of increasing length and/or charge showed increasing inhibitory potency, and detectable heparin inhibition of bacterial binding required a minimum of 16 residues. The ability of a given heparin fraction to inhibit binding to Vero cells was strongly predictive of its ability to inhibit hemagglutination, suggesting that hemagglutination reflects the capacity of B. burgdorferi to bind to GAGs.
    Source
    Infect Immun. 1998 Dec;66(12):6045-8.
    Permanent Link to this Item
    http://hdl.handle.net/20.500.14038/42266
    PubMed ID
    9826395
    Related Resources
    Link to Article in PubMed
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    UMass Chan Faculty and Researcher Publications

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