Adherence of Borrelia burgdorferi to the proteoglycan decorin

B. P. Guo, S. J. Norris, L. C. Rosenberg, M. Hook

Research output: Contribution to journalArticle

180 Scopus citations

Abstract

Lyme disease is a tick-borne infection that can develop into a chronic, multisystemic disorder. The causative agent, Borrelia burgdorferi, is initially deposited by the tick into the host dermis, where it associates with collagen fibers, replicates, and eventually disseminates to other tissues. We have examined the adherence of the spirochete to different components of the collagen fiber and demonstrated that decorin, a proteoglycan which decorates collagen fibers, can support the attachment of B. burgdorferi. No significant direct attachment to isolated type I or III collagens could be detected. Attachment of the spirochetes to decorin was highly specific, and the process could be inhibited by soluble decorin but not by various unlabeled, unrelated components. B. burgdorferi also bound soluble 125I-labeled decorin in a time- and concentration-dependent manner. Spirochete binding of soluble 125I-labeled decorin required intact proteoglycan and could not be inhibited by either isolated core protein or glycosaminoglycan chain. B. burgdorferi expresses two decorin-binding proteins with apparent molecular masses of 19 and 20 kDa as revealed in a Western blot (immunoblot)-type assay. Our results indicate that decorin may mediate the adherence of B. burgdorferi to collagen fibers in skin and other tissues.

Original languageEnglish (US)
Pages (from-to)3467-3472
Number of pages6
JournalInfection and Immunity
Volume63
Issue number9
DOIs
StatePublished - 1995

ASJC Scopus subject areas

  • Parasitology
  • Microbiology
  • Immunology
  • Infectious Diseases

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