Fibronectin binding protein BBK32 of the Lyme disease spirochete promotes bacterial attachment to glycosaminoglycans
UMass Chan Affiliations
Department of Molecular Genetics and MicrobiologyProgram in Immunology and Virology
Document Type
Journal ArticlePublication Date
2005-12-22Keywords
AnimalsBacterial Adhesion
Bacterial Proteins
Borrelia burgdorferi
Cell Line
Cell Line, Tumor
Cell Wall
Fibronectins
Glycosaminoglycans
Heparin
Humans
Lipoproteins
Lyme Disease
Rats
Immunology and Infectious Disease
Microbiology
Molecular Genetics
Virology
Metadata
Show full item recordAbstract
Borrelia burgdorferi, the agent of Lyme disease, causes a multisystemic illness that can affect the skin, heart, joints, and nervous system and is capable of attachment to diverse cell types. Among the host components recognized by this spirochete are fibronectin and glycosaminoglycans (GAGs). Three surface-localized GAG-binding bacterial ligands, Bgp, DbpA, and DbpB, have been previously identified, but recent studies suggested that at least one additional GAG-binding ligand is expressed on the spirochetal surface when the spirochete is adapted to the mammalian host environment. BBK32 is a surface lipoprotein that is produced during infection and that has been shown to bind to fibronectin. In this study, we show that, when BBK32 was produced from a shuttle vector in an otherwise nonadherent high-passage B. burgdorferi strain, the protein localized on the bacterial surface and conferred attachment to fibronectin and to mammalian cell monolayers. In addition, the high-passage strain producing BBK32 bound to purified preparations of the GAGs dermatan sulfate and heparin, as well as to these GAGs on the surfaces of cultured mammalian cells. Recombinant BBK32 recognized purified heparin, indicating that the bacterial attachment to GAGs was due to direct binding by BBK32. This GAG-binding activity of BBK32 is apparently independent of fibronectin recognition, because exogenous heparin had no effect on BBK32-mediated bacterial binding to fibronectin.Source
Infect Immun. 2006 Jan;74(1):435-41. Link to article on publisher's site
DOI
10.1128/IAI.74.1.435-441.2006Permanent Link to this Item
http://hdl.handle.net/20.500.14038/42262PubMed ID
16368999Related Resources
Rights
Copyright © 2006, American Society for Microbiology. Publisher PDF posted as allowed by the publisher's author rights policy at http://journals.asm.org/site/misc/ASM_Author_Statement.xhtml.ae974a485f413a2113503eed53cd6c53
10.1128/IAI.74.1.435-441.2006