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

John M. Leong, Douglas Robbins, Louis Rosenfeld, Biswajit Lahiri, Nikhat Parveen

Research output: Contribution to journalArticlepeer-review

28 Scopus citations

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 or 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.

Original languageEnglish (US)
Pages (from-to)6045-6048
Number of pages4
JournalInfection and immunity
Volume66
Issue number12
DOIs
StatePublished - Dec 1998
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Infectious Diseases
  • Parasitology
  • Microbiology
  • Immunology

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