scholarly journals Mapping the Ligand-Binding Region of Borrelia burgdorferi Fibronectin-Binding Protein BBK32

2001 ◽  
Vol 69 (6) ◽  
pp. 4129-4133 ◽  
Author(s):  
William S. Probert ◽  
Jung Hwa Kim ◽  
Magnus Höök ◽  
Barbara J. B. Johnson
Keyword(s):  
Borrelia Burgdorferi ◽  
Ligand Binding ◽  
Binding Protein ◽  
Cellular Adhesion ◽  
Binding Activity ◽  
Common Mechanism ◽  
Binding Region ◽  
Cellular Attachment ◽  
Fibronectin Binding Protein ◽  
Fibronectin Binding

ABSTRACT The cellular attachment and entry of pathogenic microorganisms can be facilitated by the expression of microbial adhesins that bind fibronectin. We have previously described a Borrelia burgdorferi gene, bbk32, that encodes a 47-kDa fibronectin-binding protein. In this study, the ligand-binding region of BBK32 from B. burgdorferi isolate B31 was localized to 32 amino acids. The bbk32 gene was cloned and sequenced from three additional B. burgdorferi isolates representing different genospecies of B. burgdorferi sensu lato. All four bbk32 genes encoded proteins having fibronectin-binding activity when expressed in Escherichia coli, and the deduced proteins shared 81 to 91% amino acid sequence identity within the ligand-binding domain. In addition, the ligand-binding region of BBK32 was found to share sequence homology with a fibronectin-binding peptide defined for protein F1 ofStreptococcus pyogenes. The structural and functional similarity between the ligand-binding region of BBK32 and the UR region of protein F1 suggests a common mechanism of cellular adhesion and entry for B. burgdorferi and S. pyogenes.

scholarly journals Borrelia burgdorferi Lacking BBK32, a Fibronectin-Binding Protein, Retains Full Pathogenicity

2006 ◽  
Vol 74 (6) ◽  
pp. 3305-3313 ◽  
Author(s):  
Xin Li ◽  
Xianzhong Liu ◽  
Deborah S. Beck ◽  
Fred S. Kantor ◽  
Erol Fikrig
Keyword(s):  
Life Cycle ◽  
Borrelia Burgdorferi ◽  
Deletion Mutant ◽  
Binding Protein ◽  
Kanamycin Resistance ◽  
Binding Activity ◽  
Mammalian Host ◽  
Wild Type ◽  
Fibronectin Binding Protein ◽  
Fibronectin Binding

ABSTRACT BBK32, a fibronectin-binding protein of Borrelia burgdorferi, is one of many surface lipoproteins that are differentially expressed by the Lyme disease spirochete at various stages of its life cycle. The level of BBK32 expression in B. burgdorferi is highest during infection of the mammalian host and lowest in flat ticks. This temporal expression profile, along with its fibronectin-binding activity, strongly suggests that BBK32 may play an important role in Lyme pathogenesis in the host. To test this hypothesis, we constructed an isogenic BBK32 deletion mutant from wild-type B. burgdorferi B31 by replacing the BBK32 gene with a kanamycin resistance cassette through homologous recombination. We examined both the wild-type strain and the BBK32 deletion mutant extensively in the experimental mouse-tick model of the Borrelia life cycle. Our data indicated that B. burgdorferi lacking BBK32 retained full pathogenicity in mice, regardless of whether mice were infected artificially by syringe inoculation or naturally by tick bite. The loss of BBK32 expression in the mutant had no adverse effect on spirochete acquisition (mouse-to-tick) and transmission (tick-to-mouse) processes. These results suggest that additional B. burgdorferi proteins can complement the function of BBK32, fibronectin binding or otherwise, during the natural spirochete life cycle.

scholarly journals Mapping the Ligand-Binding Region of Borrelia hermsii Fibronectin-Binding Protein

PLoS ONE ◽  
2013 ◽  
Vol 8 (5) ◽  
pp. e63437 ◽  
Author(s):  
Christiane Brenner ◽  
Katharina Bomans ◽  
Jüri Habicht ◽  
Markus M. Simon ◽  
Reinhard Wallich
Keyword(s):  
Ligand Binding ◽  
Binding Protein ◽  
Binding Region ◽  
Borrelia Hermsii ◽  
Fibronectin Binding Protein ◽  
Fibronectin Binding

scholarly journals Bioluminescent imaging of Borrelia burgdorferi in vivo demonstrates that the fibronectin-binding protein BBK32 is required for optimal infectivity

2011 ◽  
Vol 82 (1) ◽  
pp. 99-113 ◽  
Author(s):  
Jenny A. Hyde ◽  
Eric H. Weening ◽  
MiHee Chang ◽  
Jerome P. Trzeciakowski ◽  
Magnus Höök ◽  
...  
Keyword(s):  
Borrelia Burgdorferi ◽  
Binding Protein ◽  
Bioluminescent Imaging ◽  
Fibronectin Binding Protein ◽  
Fibronectin Binding

scholarly journals Regulation of Expression of the Fibronectin-Binding Protein BBK32 in Borrelia burgdorferi

2007 ◽  
Vol 189 (22) ◽  
pp. 8377-8380 ◽  
Author(s):  
Ming He ◽  
Bethany K. Boardman ◽  
Dalai Yan ◽  
X. Frank Yang
Keyword(s):  
Environmental Factors ◽  
Borrelia Burgdorferi ◽  
Response Regulator ◽  
Binding Protein ◽  
Regulation Of Expression ◽  
Fibronectin Binding Protein ◽  
Fibronectin Binding

ABSTRACT The BBK32 protein binds to host extracellular ligand fibronectin and contributes to the pathogenesis of Borrelia burgdorferi. Here we showed that expression of the BBK32 gene is influenced by multiple environmental factors and that its regulation is governed by the response regulator Rrp2 and RpoN-RpoS (σ54-σS) sigma cascade in B. burgdorferi.

Identification of a fibronectin-binding protein of Treponema lecithinolyticum by two-dimensional gel electrophoresis and ligand binding assay

2007 ◽  
Vol 53 (10) ◽  
pp. 1185-1190 ◽  
Author(s):  
Hae-Ri Lee ◽  
Bong-Kyu Choi
Keyword(s):  
Ligand Binding ◽  
Gel Electrophoresis ◽  
Binding Assay ◽  
Binding Protein ◽  
Bacterial Attachment ◽  
Host Cells ◽  
Ligand Binding Assay ◽  
Two Dimensional Gel Electrophoresis ◽  
Fibronectin Binding Protein ◽  
Fibronectin Binding

Treponema lecithinolyticum is associated with periodontitis and endodontic infections. As a critical early step in the infection process, fibronectin-binding protein (Fbp) is known to be involved in the adhesion of bacteria to cell surfaces for colonization and, hence, is considered to be a virulence factor. In this study, we identified an Fbp from the T. lecithinolyticum cell surface with a molecular mass of about 52 kDa by using 2-dimensional gel electrophoresis followed by a ligand binding assay. As T. lecithinolyticum is capable of binding to soluble and immobilized fibronectin, this Fbp may contribute to bacterial attachment to host cells.

scholarly journals Characterization of the Domain of Fibronectin-Binding Protein I of Streptococcus pyogenes Responsible for Elicitation of a Protective Immune Response

2001 ◽  
Vol 69 (1) ◽  
pp. 622-625 ◽  
Author(s):  
Kai Schulze ◽  
Eva Medina ◽  
Susanne R. Talay ◽  
Rebecca J. Towers ◽  
Gursharan S. Chhatwal ◽  
...  
Keyword(s):  
Streptococcus Pyogenes ◽  
Binding Protein ◽  
Immunoglobulin A ◽  
Control Group ◽  
Binding Region ◽  
Lethal Challenge ◽  
Heterologous Challenge ◽  
Fibronectin Binding Protein ◽  
Efficient Protection ◽  
Fibronectin Binding

ABSTRACT Fibronectin-binding protein I (SfbI) represents a major adhesin ofStreptococcus pyogenes. Mice were intranasally immunized with recombinant proteins spanning different portions of SfbI to identify the minimal fragment able to elicit a protective response against a lethal challenge with S. pyogenes. The strongest cellular responses and the highest levels of antigen-specific secretory immunoglobulin A (IgA) were detected in mice immunized with the fibronectin-binding region of SfbI. In contrast, animals vaccinated with a polypeptide spanning the aromatic and proline-rich regions showed the highest titers and fastest IgG response in serum. Vaccination with either SfbI without a membrane anchor and signal peptide or a polypeptide encompassing its fibronectin-binding regions resulted in efficient protection against heterologous challenge (60% and 80%, respectively), whereas the use of a polypeptide lacking this region conferred marginal protection (10%) with respect to the control group (0%). These results demonstrate that the fibronectin-binding region of SfbI is a promising candidate antigen for developing anti-S. pyogenes vaccines.

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