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From the same journal

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

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Published copy (DOI)

Author(s)

  • Jung Hwa Kim
  • Jenny Singvall
  • Ulrich Schwarz-Linek
  • Barbara J B Johnson
  • Jennifer R Potts
  • Magnus Höök

Department/unit(s)

Publication details

JournalJournal of Biological Chemistry
DatePublished - 2004
Issue number40
Volume279
Number of pages9
Pages (from-to)41706-14
Original languageEnglish

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.

    Research areas

  • Adhesins, Bacterial, Amino Acid Motifs, Bacterial Proteins, Borrelia burgdorferi Group, Fibronectins, Ligands, Protein Binding, Protein Conformation, Protein Structure, Secondary

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