Phylogenetic Analysis of the Spirochetes<i>Borrelia parkeri</i>and<i>Borrelia turicatae</i>and the Potential for Tick-Borne Relapsing Fever in Florida

Schwan, Tom G.; Raffel, Sandra J.; Schrumpf, Merry E.; Policastro, Paul F.; Rawlings, Julie A.; Lane, Robert S.; Breitschwerdt, Edward B.; Porcella, Stephen F.

doi:10.1128/jcm.43.8.3851-3859.2005

Cited by 103 publications

(153 citation statements)

References 63 publications

(53 reference statements)

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“…parkeri and B. turicatae represent closely related spirochetes in the United States that are suspected to cause tickborne relapsing fever in humans (9). Although epidemiological evidence is strong for B. turicatae as a cause of human infections, isolation of B. turicatae and B. parkeri from human patients has not yet been documented (45). In this study, we have identified a receptor from B. parkeri for CFH and CFHR-1, two key soluble-phase inhibitory molecules of the alternative complement pathway, and we showed that binding of CFH to BpcA permits resistance to complement-mediated killing by NHS.…”

Section: Discussionmentioning

confidence: 99%

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Molecular Characterization of the Interaction ofBorrelia parkeriandBorrelia turicataewith Human Complement Regulators

et al. 2010

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In North America, tick-borne relapsing fever is caused by the species Borrelia hermsii, B. parkeri, and B. turicatae, which are transmitted to humans through the bite of the respective infected tick vectors. Here we describe the identification and functional characterization of a surface lipoprotein of B. parkeri, designated BpcA, that binds the human complement regulators factor H and factor H-related protein 1 and, simultaneously, the host protease plasminogen. In contrast, the homologous B. turicatae protein failed to bind human factor H and factor H-related protein 1 but retained its plasminogen binding capacity. Factor H bound to BpcA maintains its regulatory capacity to control C3b deposition and C3 convertase activity. Ectopic expression of BpcA in a serum-sensitive B. burgdorferi strain protects transformed cells from complement-mediated killing. Furthermore, bound plasminogen/plasmin endows B. parkeri and B. turicatae with the potential to degrade extracellular matrix components. These findings expand our understanding of the putative recent evolutionary separation of Borrelia parkeri and Borrelia turicatae, provide evidence that B. parkeri differs from B. turicatae in its ability to resist complement attack, and may help in understanding the pathological processes underlying tick-borne relapsing fever.

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Section: Discussionmentioning

confidence: 99%

“…Due to the availability of genetic tools and genome sequence data, discrimination between closely related species causing relapsing fever infections among humans is now feasible. Although B. hermsii has been isolated frequently from humans, direct evidence for B. parkeri and B. turicatae being pathogenic to humans is still missing (4,44,45).…”

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confidence: 99%

Molecular Characterization of the Interaction ofBorrelia parkeriandBorrelia turicataewith Human Complement Regulators

et al. 2010

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“…Genomic DNA samples from Legionella isolates (Table 1, codes 2 to 18) were examined for lpg2644 and mip homologues by Southern blot analysis under low-stringency conditions (72,76). The hybridization probes were designed from conserved regions of the respective genes and amplified from genomic DNA of L. pneumophila Lp02 with a PCR digoxigenin (DIG) probe synthesis kit (Roche Applied Science, Laval, QC, Canada) using primers 10 and 11 and primers 12 and 13 ( Table 3).…”

Section: Methodsmentioning

confidence: 99%

Lcl of Legionella pneumophila Is an Immunogenic GAG Binding Adhesin That Promotes Interactions with Lung Epithelial Cells and Plays a Crucial Role in Biofilm Formation

Duncan¹,

Prashar

et al. 2011

Infect Immun

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Legionellosis is mostly caused by Legionella pneumophila and is defined by a severe respiratory illness with a case fatality rate ranging from 5 to 80%. In vitro and in vivo, interactions of L. pneumophila with lung epithelial cells are mediated by the sulfated glycosaminoglycans (GAGs) of the host extracellular matrix. In this study, we have identified several Legionella heparin binding proteins. We have shown that one of these proteins, designated Lcl, is a polymorphic adhesin of L. pneumophila that is produced during legionellosis. Homologues of Lcl are ubiquitous in L. pneumophila serogroups but are undetected in other Legionella species. Recombinant Lcl binds to GAGs, and a ⌬lpg2644 mutant demonstrated reduced binding to GAGs and human lung epithelial cells. Importantly, we showed that the ⌬lpg2644 strain is dramatically impaired in biofilm formation. These data delineate the role of Lcl in the GAG binding properties of L. pneumophila and provide molecular evidence regarding its role in L. pneumophila adherence and biofilm formation.

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“…We studied 17 Borrelia isolates that originated primarily from ticks or humans in North America (Table 1) (Porcella et al, 2005;Schwan et al, 2005). All relapsing fever spirochaetes were cultured in modified Kelly's medium (complete BSK-H) (Sigma-Aldrich) supplemented with 12% rabbit serum.…”

Section: Borrelia Strains and Cultivationmentioning

confidence: 99%

Relapsing fever spirochaetes produce a serine protease that provides resistance to oxidative stress and killing by neutrophils

Guyard¹,

Battisti

Raffel

et al. 2006

Molecular Microbiology

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SummaryThe spirochaetes that cause tick-borne relapsing fever and Lyme disease are closely related human pathogens, yet they differ significantly in their ecology and pathogenicity. Genome sequencing of two species of relapsing fever spirochaetes, Borrelia hermsii and Borrelia turicatae, identified a chromosomal open reading frame, designated bhpA , not present in the Lyme disease spirochaete Borrelia burgdorferi . The predicted amino acid sequence of bhpA was homologous with the HtrA serine proteases, which are involved with stress responses and virulence in other bacteria. B. hermsii produced an active serine protease that was recognized by BhpA antibodies and the recombinant BhpA proteindegraded b -casein. bhpA was transcribed in vitro at all growth temperatures and transcription levels were slightly elevated at higher temperatures. These results correlated with the synthesis of BhpA during B. hermsii infection in mice. With the exception of Borrelia recurrentis , the bhpA gene, protein and enzymatic activity were found in all relapsing fever spirochaetes, but not in Lyme disease or related spirochaetes. Heterologous expression of bhpA in B. burgdorferi increased the spirochaete's resistance to both oxidative stress and killing by human neutrophils. Therefore, we propose that bhpA encodes a unique and functional serine protease in relapsing fever spirochaetes. This periplasmic enzyme may prevent the accumulation of proteins damaged by the innate immune response and contribute to the ability of the relapsing fever spirochaetes to achieve high cell densities in blood.

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Phylogenetic Analysis of the SpirochetesBorrelia parkeriandBorrelia turicataeand the Potential for Tick-Borne Relapsing Fever in Florida

Cited by 103 publications

References 63 publications

Molecular Characterization of the Interaction ofBorrelia parkeriandBorrelia turicataewith Human Complement Regulators

Molecular Characterization of the Interaction ofBorrelia parkeriandBorrelia turicataewith Human Complement Regulators

Lcl of Legionella pneumophila Is an Immunogenic GAG Binding Adhesin That Promotes Interactions with Lung Epithelial Cells and Plays a Crucial Role in Biofilm Formation

Relapsing fever spirochaetes produce a serine protease that provides resistance to oxidative stress and killing by neutrophils

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