Manganese (Mn) is an essential micronutrient that is not readily available to pathogens during infection due to an active host defense mechanism known as nutritional immunity. To overcome this nutrient restriction, bacteria utilize high-affinity transporters that allow them to compete with host metal-binding proteins. Despite the established role of Mn in bacterial pathogenesis, little is known about the relevance of Mn in the pathophysiology of E. faecalis. Here, we identified and characterized the major Mn acquisition systems of E. faecalis. We discovered that the ABC-type permease EfaCBA and two Nramp-type transporters, named MntH1 and MntH2, work collectively to promote cell growth under Mn-restricted conditions. The simultaneous inactivation of EfaCBA, MntH1 and MntH2 (ΔefaΔmntH1ΔmntH2 strain) led to drastic reductions (>95%) in cellular Mn content, severe growth defects in body fluids (serum and urine) ex vivo, significant loss of virulence in Galleria mellonella, and virtually complete loss of virulence in rabbit endocarditis and murine catheter-associated urinary tract infection (CAUTI) models. Despite the functional redundancy of EfaCBA, MntH1 and MntH2 under in vitro or ex vivo conditions and in the invertebrate model, dual inactivation of efaCBA and mntH2 (ΔefaΔmntH2 strain) was sufficient to prompt maximal sensitivity to calprotectin, a Mn- and Zn-chelating host antimicrobial protein, and for the loss of virulence in mammalian models. Interestingly, EfaCBA appears to play a prominent role during systemic infection, whereas MntH2 was more important during CAUTI. The different roles of EfaCBA and MntH2 in these sites could be attributed, at least in part, to the differential expression of efaA and mntH2 in cells isolated from hearts or from bladders. Collectively, this study demonstrates that Mn acquisition is essential for the pathogenesis of E. faecalis and validates Mn uptake systems as promising targets for the development of new antimicrobials.
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http://dx.doi.org/10.1371/journal.ppat.1007102 | DOI Listing |
PLoS Pathog
September 2018
Department of Oral Biology, University of Florida College of Dentistry, Gainesville, Florida, United States of America.
Manganese (Mn) is an essential micronutrient that is not readily available to pathogens during infection due to an active host defense mechanism known as nutritional immunity. To overcome this nutrient restriction, bacteria utilize high-affinity transporters that allow them to compete with host metal-binding proteins. Despite the established role of Mn in bacterial pathogenesis, little is known about the relevance of Mn in the pathophysiology of E.
View Article and Find Full Text PDFBiosci Microbiota Food Health
February 2018
Yakult Central Institute, 5-11 Izumi, Kunitachi-shi, Tokyo 186-8650, Japan.
The / group accumulates a high level of manganese, which works to scavenge superoxide anions produced during aerobic growth. The genome of strain Shirota, however, also codes the gene for superoxide dismutase (SOD), , which catalyzes the dismutation of superoxide anion into hydrogen peroxide and oxygen. We anticipated that the SOD and/or manganese may contribute to the aerobic growth of Shirota and tried to clarify how Shirota can eliminate the toxicity of superoxide anion.
View Article and Find Full Text PDFFood Microbiol
February 2011
Technische Universität München, Lehrstuhl Technische Mikrobiologie, Freising, Germany.
Lactobacillus sanfranciscensis is the key bacterium in traditional sourdough fermentation. The molecular background of its oxygen tolerance was investigated by comparison of wild type and NADH-oxidase (Nox) knock out mutants. The nox gene of L.
View Article and Find Full Text PDFMicrobiology (Reading)
April 2005
Wageningen Centre for Food Sciences, NIZO Food Research, Kernhemseweg 2, PO Box 20, 6710 BA Ede, The Netherlands.
Manganese serves an important function in Lactobacillus plantarum in protection against oxidative stress and this bacterium can accumulate Mn(2+) up to millimolar levels intracellularly. Although the physiological role of Mn(2+) and the uptake of this metal ion have been well documented, the only uptake system described so far for this bacterium is the Mn(2+)- and Cd(2+)-specific P-type ATPase (MntA). Recently, the genome of L.
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