The Fur Homologue in<i>Borrelia burgdorferi</i>

Katona, Laura I.; Tokarz, Rafal; Kuhlow, Christopher J.; Benach, J.; Benach, Jorge L.

doi:10.1128/jb.186.19.6443-6456.2004

Cited by 50 publications

(101 citation statements)

References 63 publications

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“…Finally, in a wide variety of bacterial pathogens, Mn contributes to virulence by regulating the expression of many virulence determinants (15,17,31). Similarly, Mn, possibly via the Mn-dependent Fur homolog BosR (23,33,37,38) Our study has demonstrated that the Lyme disease spirochete requires BmtA's Mn-associated transport function(s) to maintain its infectious cycle in nature. To date, only relatively few virulence factors, including OspC, DbpB/A, OspA/B, PncA, and BptA, have been identified in Bb, and the functions of most of these proteins remain obscure (4,5,(7)(8)(9)(10).…”

Section: Discussionmentioning

confidence: 95%

A manganese transporter, BB0219 (BmtA), is required for virulence by the Lyme disease spirochete, Borrelia burgdorferi

Ouyang

Oman

et al. 2009

Proc. Natl. Acad. Sci. U.S.A.

131

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Borrelia burgdorferi (Bb), the causative agent of Lyme disease, is transmitted to mammalian hosts through an arthropod (tick) vector. To establish infection, Bb must acquire essential nutrients, including transition metals, from its mammalian and tick hosts. Thus far, no metal transporter has been identified in Bb. Here, we report the identification of the first metal transporter, BmtA (BB0219), in Bb. BmtA-deficient mutants of virulent Bb were readily generated, and the mutants grew slightly slower than wild-type Bb in vitro. However, BmtA mutants were sensitive to the chelating actions of EDTA, suggesting a role for BmtA in metal utilization. Intracellular accumulation of manganese (Mn) was substantially diminished in the bmtA mutant, indicating that BmtA was operative in Mn uptake. Given that BmtA lacks homology to any known Mn transporter, we postulate that BmtA is part of a novel mechanism for Mn acquisition by a bacterial pathogen. BmtA also was essential to the infectious life cycle of Bb in ticks and mammals, thereby qualifying BmtA as a new borrelial virulence factor. In addition, the bmtA mutant was sensitive to treatment with t-butyl hydroperoxide, implying that BmtA, and thus Mn, is important to Bb for detoxifying reactive oxygen species, including those potentially liberated by immune effector cells during the innate immune response. Our discovery of the first molecule involved in metal transport in Bb provides a foundation for further elucidating metal homeostasis in this important human pathogen, which may lead to new strategies for thwarting Lyme disease. metal transport ͉ pathogenesis

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Section: Discussionmentioning

confidence: 95%

A manganese transporter, BB0219 (BmtA), is required for virulence by the Lyme disease spirochete, Borrelia burgdorferi

Ouyang

Oman

et al. 2009

Proc. Natl. Acad. Sci. U.S.A.

131

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“…pLK42/2 was constructed by PCR-amplifying the bosRR39K gene from pLK38/2 using primers FLAF and FRR (Table S2) and inserting it into the Nde I-Xho I site of pET28a (Novagen). pLK1/5 was from an earlier study (Katona et al, 2004).…”

Section: Methodsmentioning

confidence: 99%

“…Gel shift assays were carried out as previously described (Katona et al, 2004). Briefly, recombinant BosR (or BosRR39K) was mixed with target DNA in 20 mM Bistris/borate (pH 7.5) buffer containing 1.5 mM DTT, 1.3 mM MgCl 2 , 53 mM KCl, 3.3 % glycerol and 133 mg BSA ml 21 , incubated for 20 min at room temperature, and separated on a 6 % nondenaturing gel.…”

Section: Methodsmentioning

confidence: 99%

“…Recombinant proteins were prepared as previously described (Katona et al, 2004). Briefly, the His-tagged proteins were overexpressed in Escherichia coli BL21(DE3) from pLK1/5 or pLK42/2, purified by zinc chelate chromatography, and then treated with thrombin to free the N-terminal His tags.…”

Section: Methodsmentioning

confidence: 99%

“…Tricine SDS-PAGE was carried out as previously described (Katona et al, 2004 (Coleman & Benach, 1989), rat anti-OspC (kindly provided by Justin Radolf) or rat anti-BosR. Rat anti-BosR was raised against purified recombinant BosR that retained the Nterminal His tag.…”

Section: Methodsmentioning

confidence: 99%

See 2 more Smart Citations

The Fur homologue BosR requires Arg39 to activate rpoS transcription in Borrelia burgdorferi and thereby direct spirochaete infection in mice

Katona

2015

Microbiology

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Regulation of Gene and Protein Expression in the Lyme Disease Spirochete

Stevenson

Seshu

2017

Current Topics in Microbiology and Immunology

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The infectious cycle of Borrelia burgdorferi necessitates persistent infection of both vertebrates and ticks, and efficient means of transmission between those two very different types of hosts. The Lyme disease spirochete has evolved mechanisms to sense its location in the infectious cycle, and use that information to control production of the proteins and other factors required for each step. Numerous components of borrelial regulatory pathways have been characterized to date. Their effects are being pieced together, thereby providing glimpses into a complex web of cooperative and antagonistic interactions. In this chapter, we present a broad overview of B. burgdorferi gene and protein regulation during the natural infectious cycle, discussions of culture-based methods for elucidating regulatory mechanisms, and summaries of many of the known regulatory proteins and small molecules. We also highlight areas that are in need of substantially more research.

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The Fur Homologue inBorrelia burgdorferi

Cited by 50 publications

References 63 publications

A manganese transporter, BB0219 (BmtA), is required for virulence by the Lyme disease spirochete, Borrelia burgdorferi

A manganese transporter, BB0219 (BmtA), is required for virulence by the Lyme disease spirochete, Borrelia burgdorferi

The Fur homologue BosR requires Arg39 to activate rpoS transcription in Borrelia burgdorferi and thereby direct spirochaete infection in mice

Regulation of Gene and Protein Expression in the Lyme Disease Spirochete

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