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Identification of a candidate glycosaminoglycan‐binding adhesin of the Lyme disease spirochete Borrelia burgdorferi
Author(s) -
Parveen Nikhat,
Leong John M.
Publication year - 2000
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1046/j.1365-2958.2000.01792.x
Subject(s) - borrelia burgdorferi , biology , bacterial adhesin , microbiology and biotechnology , spirochaetaceae , glycosaminoglycan , recombinant dna , lyme disease , bacterial outer membrane , binding protein , antibody , virology , escherichia coli , biochemistry , immunology , gene
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 ( B orrelia G AG‐binding p rotein), 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 .