ArticleThe Journal of biological chemistry2013
A manganese-rich environment supports superoxide dismutase activity in a Lyme disease pathogen, Borrelia burgdorferi.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.
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Who cites it
49 citing papers in PubMed, 82 citations in OpenAlex.
- Article
- Article
- CspZ variant-specific interaction with factor H incorporates a metal site to support Lyme borreliae complement evasion.The Journal of biological chemistry · 2025Article
- Bacterial Metallostasis: Metal Sensing, Metalloproteome Remodeling, and Metal Trafficking.Chemical reviews · 2024Review
- Proteomic strategies to interrogate the Fe-S proteome.Biochimica et biophysica acta. Molecular cell research · 2024Review
- Assessment of the hypothetical protein BB0616 in the murine infection ofInfection and immunity · 2024Article
- The Arsenal ofAntioxidants (Basel, Switzerland) · 2023Review
- Why is manganese so valuable to bacterial pathogens?Frontiers in cellular and infection microbiology · 2023Review
- Large-Scale Sequencing ofGenes · 2022Review
- Old dogs, new tricks: New insights into the iron/manganese superoxide dismutase family.Journal of inorganic biochemistry · 2022Article
- Characterization of the metalloproteome of Pseudoalteromonas (BB2-AT2): biogeochemical underpinnings for zinc, manganese, cobalt, and nickel cycling in a ubiquitous marine heterotroph.Metallomics : integrated biometal science · 2021Article
- Regulation and distinct physiological roles of manganese in bacteria.FEMS microbiology reviews · 2021Review
- Review
- The Brilliance ofPathogens (Basel, Switzerland) · 2021Review
- Article
- Transcriptome Analysis Reveals Cr(VI) Adaptation Mechanisms inFrontiers in microbiology · 2021Article
- Lyme Disease Pathogenesis.Current issues in molecular biology · 2021Review
- Characterization of the Fe metalloproteome of a ubiquitous marine heterotroph, Pseudoalteromonas (BB2-AT2): multiple bacterioferritin copies enable significant Fe storage.Metallomics : integrated biometal science · 2020Article
- Establishment of an in vitro RNA polymerase transcription system: a new tool to study transcriptional activation in Borrelia burgdorferi.Scientific reports · 2020Article
- The Lyme disease spirochete's BpuR DNA/RNA-binding protein is differentially expressed during the mammal-tick infectious cycle, which affects translation of the SodA superoxide dismutase.Molecular microbiology · 2019Article
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Authors and funding
10 authors at 5 institutions in 1 country.
Funding
Abstract
The Lyme disease pathogen Borrelia burgdorferi represents a novel organism in which to study metalloprotein biology in that this spirochete has uniquely evolved with no requirement for iron. Not only is iron low, but we show here that B. burgdorferi has the capacity to accumulate remarkably high levels of manganese. This high manganese is necessary to activate the SodA superoxide dismutase (SOD) essential for virulence. Using a metalloproteomic approach, we demonstrate that a bulk of B. burgdorferi SodA directly associates with manganese, and a smaller pool of inactive enzyme accumulates as apoprotein. Other metalloproteins may have similarly adapted to using manganese as co-factor, including the BB0366 aminopeptidase. Whereas B. burgdorferi SodA has evolved in a manganese-rich, iron-poor environment, the opposite is true for Mn-SODs of organisms such as Escherichia coli and bakers' yeast. These Mn-SODs still capture manganese in an iron-rich cell, and we tested whether the same is true for Borrelia SodA. When expressed in the iron-rich mitochondria of Saccharomyces cerevisiae, B. burgdorferi SodA was inactive. Activity was only possible when cells accumulated extremely high levels of manganese that exceeded cellular iron. Moreover, there was no evidence for iron inactivation of the SOD. B. burgdorferi SodA shows strong overall homology with other members of the Mn-SOD family, but computer-assisted modeling revealed some unusual features of the hydrogen bonding network near the enzyme's active site. The unique properties of B. burgdorferi SodA may represent adaptation to expression in the manganese-rich and iron-poor environment of the spirochete.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.