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

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.

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

Infection and Immunity ◽

10.1128/iai.02035-05 ◽

2006 ◽

Vol 74 (6) ◽

pp. 3305-3313 ◽

Cited By ~ 68

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.

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

Molecular Microbiology ◽

10.1111/j.1365-2958.2011.07801.x ◽

2011 ◽

Vol 82 (1) ◽

pp. 99-113 ◽

Cited By ~ 69

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

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Identification of a 47 kDa fibronectin-binding protein expressed by Borrelia burgdorferi isolate B31

Molecular Microbiology ◽

10.1046/j.1365-2958.1998.01127.x ◽

1998 ◽

Vol 30 (5) ◽

pp. 1003-1015 ◽

Cited By ~ 199

Author(s):

William S. Probert ◽

Barbara J. B. Johnson

Keyword(s):

Borrelia Burgdorferi ◽

Binding Protein ◽

Fibronectin Binding Protein ◽

Fibronectin Binding

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

Infection and Immunity ◽

10.1128/iai.69.6.4129-4133.2001 ◽

2001 ◽

Vol 69 (6) ◽

pp. 4129-4133 ◽

Cited By ~ 57

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.

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Isolation of an amino-terminal fibronectin-binding protein on human U937 cells and rat peritoneal macrophages.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(19)50620-2 ◽

1992 ◽

Vol 267 (6) ◽

pp. 3968-3975

Author(s):

S.D. Blystone ◽

J.E. Kaplan

Keyword(s):

Binding Protein ◽

Peritoneal Macrophages ◽

U937 Cells ◽

Amino Terminal ◽

Fibronectin Binding Protein ◽

Fibronectin Binding

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Association between Resistance to Erythromycin and the Presence of the Fibronectin Binding Protein F1 Gene, prtF1, in Streptococcus pyogenes Isolates from German Pediatric Patients

Antimicrobial Agents and Chemotherapy ◽

10.1128/aac.49.7.2990-2993.2005 ◽

2005 ◽

Vol 49 (7) ◽

pp. 2990-2993 ◽

Cited By ~ 4

Author(s):

Maria Haller ◽

Kirsten Fluegge ◽

Sandra Jasminder Arri ◽

Brit Adams ◽

Reinhard Berner

Keyword(s):

Streptococcus Pyogenes ◽

Pediatric Patients ◽

Group A Streptococcus ◽

Binding Protein ◽

Macrolide Resistance ◽

Group A ◽

Fibronectin Binding Protein ◽

Fibronectin Binding ◽

Cell Invasiveness

ABSTRACT A total of 301 German pediatric group A streptococcus isolates were screened for the presence of macrolide resistance and the fibronectin binding protein F1 gene (prtF1) encoding an adhesin and cell invasiveness protein. The prtF1 gene was present significantly more often among macrolide-resistant isolates. The majority of these were not clonally related.

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