BBK32, a fibronectin-binding MSCRAMM from Borrelia burgdorferi contains a disordered region that undergoes a conformational change on ligand binding.

JH Kim, J Singvall, Ulrich Schwarz-Linek, BJB Johnson, JR Potts, M Höök

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55 Citations (Scopus)

Abstract

BBK32 is a fibronectin-binding lipoprotein on Borrelia burgdorferi, the causative agent of Lyme disease. Analysis using secondary structure prediction programs suggested that BBK32 is composed of two domains, an N-terminal segment lacking well defined secondary structure and a C-terminal segment composed largely of alpha-helices. Analysis of purified recombinant forms of the two domains by circular dichroism spectroscopy, gel permeation chromatography, and intrinsic viscosity determination were consistent with an N-terminal-extended, unstructured segment and a C-terminal globular domain in BBK32. Solid phase binding experiments suggest that the unstructured N-terminal domain binds fibronectin. Analysis of changes in circular dichroism spectra of the N-terminal segment of BBK32 upon binding of the N-terminal domain of fibronectin revealed an increase in beta-sheet content in the complex. Hence, BBK32, which belongs to a different family of proteins and shows no overall sequence similarity with the fibronectin binding MSCRAMMs (microbial surface components recognizing adhesive matrix molecules) of Gram-positive bacteria, binds fibronectin by a mechanism that is reminiscent of the "tandem beta-zipper" previously demonstrated for the fibronectin binding of streptococcal adhesins (Schwarz-Linek, U., Werner, J.M., Pickford, A. R., Gurusiddappa, S., Kim, J.H., Pilka, E. S., Briggs, J.A., Gough, T. S., Hook, M., Campbell, I. D., and Potts, J.R. (2003) Nature 423, 177-181).

Original languageEnglish
Pages (from-to)41706-41714
Number of pages9
JournalJournal of Biological Chemistry
Volume279
DOIs
Publication statusPublished - 1 Oct 2004

Keywords

  • LYME-DISEASE SPIROCHETE
  • STAPHYLOCOCCUS-AUREUS INFECTIONS
  • SURFACE PROTEIN-A
  • STREPTOCOCCUS-PYOGENES
  • DECORIN-BINDING
  • BACTERIAL ADHERENCE
  • CRYSTAL-STRUCTURE
  • EPITHELIAL-CELLS
  • EXPRESSION
  • HOST

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