Identification of a candidate glycosaminoglycan-binding adhesin of the Lyme disease spirochete Borrelia burgdorferi

Mol Microbiol. 2000 Mar;35(5):1220-34. doi: 10.1046/j.1365-2958.2000.01792.x.


Binding of glycosaminoglycans (GAGs) by Borrelia burgdorferi, the Lyme disease spirochete, has the potential to promote the colonization of diverse tissues. GAG binding by B. burgdorferi is associated with haemagglutination and we have identified a 26 kDa protein, which we have termed Bgp (Borrelia GAG-binding protein), on the basis of its ability to bind to heparin and erythrocytes. Bgp was found in outer membrane fractions of B. burgdorferi and on the surface of intact bacteria, as assayed by labelling with a membrane-impermeable biotinylating agent or anti-Bgp antibodies. Purified recombinant Bgp agglutinated erythrocytes, binds to the same spectrum of GAGs as the B. burgdorferi strain from which the cloned bgp sequence was obtained, and inhibited B. burgdorferi binding to purified GAGs and to cultured mammalian cells. Thus, Bgp is a strong candidate for a GAG-binding adhesin of B. burgdorferi.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Adhesins, Bacterial / metabolism*
  • Animals
  • Base Sequence
  • Borrelia burgdorferi Group / metabolism*
  • Borrelia burgdorferi*
  • DNA Primers
  • Erythrocyte Membrane / microbiology
  • Glycosaminoglycans / metabolism*
  • Hemagglutinins / metabolism
  • Heparin / metabolism
  • Mice
  • Mice, Inbred BALB C
  • Protein Binding
  • Recombinant Proteins / metabolism


  • Adhesins, Bacterial
  • DNA Primers
  • Glycosaminoglycans
  • Hemagglutinins
  • Recombinant Proteins
  • Heparin