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 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 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.

scholarly journals Analysis of the Borrelia burgdorferi Cyclic-di-GMP-Binding Protein PlzA Reveals a Role in Motility and Virulence

2011 ◽  
Vol 79 (5) ◽  
pp. 1815-1825 ◽  
Author(s):  
Joshua E. Pitzer ◽  
Syed Z. Sultan ◽  
Yoshihiro Hayakawa ◽  
Gerry Hobbs ◽  
Michael R. Miller ◽  
...  
Keyword(s):  
Life Cycle ◽  
Borrelia Burgdorferi ◽  
Binding Protein ◽  
Survival Rates ◽  
Wild Type ◽  
Content Type ◽  
Infectious Dose ◽  
Swimming Pattern ◽  
Bacteria Inactivation ◽  
Mutant Cells

ABSTRACTThe cyclic-dimeric-GMP (c-di-GMP)-binding protein PilZ has been implicated in bacterial motility and pathogenesis. Although BB0733 (PlzA), the only PilZ domain-containing protein inBorrelia burgdorferi, was reported to bind c-di-GMP, neither its role in motility or virulence nor it's affinity for c-di-GMP has been reported. We determined that PlzA specifically binds c-di-GMP with high affinity (dissociation constant [Kd], 1.25 μM), consistent withKdvalues reported for c-di-GMP-binding proteins from other bacteria. Inactivation of the monocistronically transcribedplzAresulted in an opaque/solid colony morphology, whereas the wild-type colonies were translucent. While the swimming pattern of mutant cells appeared normal, on swarm plates, mutant cells exhibited a significantly reduced swarm diameter, demonstrating a role ofplzAin motility. Furthermore, theplzAmutant cells were significantly less infectious in experimental mice (as determined by 50% infectious dose [ID50]) relative to wild-type spirochetes. The mutant also had survival rates in fed ticks lower than those of the wild type. Consequently,plzAmutant cells failed to complete the mouse-tick-mouse infection cycle, indicatingplzAis essential for the enzootic life cycle ofB. burgdorferi. All of these defects were corrected when the mutant was complemented incis. We propose that failure ofplzAmutant cells to infect mice was due to altered motility; however, the possibility that an unidentified factor(s) contributed to interruption of theB. burgdorferienzootic life cycle cannot yet be excluded.

scholarly journals The Fibronectin-Binding Protein EfbA Contributes to Pathogenesis and Protects against Infective Endocarditis Caused by Enterococcus faecalis

2015 ◽  
Vol 83 (12) ◽  
pp. 4487-4494 ◽  
Author(s):  
Kavindra V. Singh ◽  
Sabina Leanti La Rosa ◽  
Sudha R. Somarajan ◽  
Jung Hyeob Roh ◽  
Barbara E. Murray
Keyword(s):  
Enterococcus Faecalis ◽  
Biofilm Formation ◽  
Deletion Mutant ◽  
Chromosomal Location ◽  
Wild Type ◽  
Content Type ◽  
High Affinity ◽  
Mixed Inoculum ◽  
Fibronectin Binding Protein ◽  
Fibronectin Binding

EfbA is a PavA-like fibronectin adhesin ofEnterococcus faecalispreviously shown to be important in experimental urinary tract infection. Here, we expressed and purified theE. faecalisOG1RF EfbA and confirmed that this protein binds with high affinity to immobilized fibronectin, collagen I, and collagen V. We constructed anefbAdeletion mutant and demonstrated that its virulence was significantly attenuated (P< 0.0006) versus the wild type in a mixed inoculum rat endocarditis model. Furthermore,efbAdeletion resulted in diminished ability to bind fibronectin (P< 0.0001) and reduced biofilm (P< 0.001). Reintroduction ofefbAinto the original chromosomal location restored virulence, adherence to fibronectin, and biofilm formation to wild-type levels. Finally, vaccination of rats with purified recombinant EfbA protein protected against OG1RF endocarditis (P= 0.008versuscontrol). Taken together, our results demonstrate that EfbA is an important factor involved inE. faecalisendocarditis and that rEfbA immunization is effective in preventing such infection, likely by interfering with bacterial adherence.

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

2005 ◽  
Vol 49 (7) ◽  
pp. 2990-2993 ◽  
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.

scholarly journals Protective Immunity againstStreptococcus pyogenesChallenge in Mice after Immunization with Fibronectin‐Binding Protein

2005 ◽  
Vol 192 (12) ◽  
pp. 2081-2091 ◽  
Author(s):  
Yutaka Terao ◽  
Shigefumi Okamoto ◽  
Kosuke Kataoka ◽  
Shigeyuki Hamada ◽  
Shigetada Kawabata
Keyword(s):  
Protective Immunity ◽  
Binding Protein ◽  
Fibronectin Binding Protein ◽  
Fibronectin Binding

scholarly journals Contribution of fibronectin-binding protein to pathogenesis ofStreptococcus equissp. zooepidemicus

2013 ◽  
Vol 67 (3) ◽  
pp. 174-183 ◽  
Author(s):  
Li Yi ◽  
Yang Wang ◽  
Zhe Ma ◽  
Hui Zhang ◽  
Yue Li ◽  
...  
Keyword(s):  
Binding Protein ◽  
Fibronectin Binding Protein ◽  
Fibronectin Binding
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