Utilization of exogenous siderophores and natural catechols by Listeria monocytogenes

Simon, N. T.; Coulanges, Valerie; André, Philippe; Vidon, Dominique J.-M.

doi:10.1128/aem.61.4.1643-1645.1995

Cited by 31 publications

(14 citation statements)

References 13 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…We previously reported that of a series of 10 iron-chelating agents tested, tropolone and 8-hydroxyquinoline were the most effective in inhibiting the growth of L. monocytogenes (47) and that this growth inhibitory effect was completely reversed by ferric citrate (7). In addition, we showed that L. monocytogenes was able to grow in tropolone or 8-hydroxyquinoline ironrestricted medium in the presence of various siderophores or some natural catechols or catecholamines (44).…”

mentioning

confidence: 92%

Utilization of iron-catecholamine complexes involving ferric reductase activity in Listeria monocytogenes

Coulanges¹,

André²,

Ziegler³

et al. 1997

Infect Immun

Self Cite

View full text Add to dashboard Cite

Listeria monocytogenes is a ubiquitous potentially pathogenic organism requiring iron for growth and virulence. Although it does not produce siderophores, L. monocytogenes is able to obtain iron by using either exogenous siderophores produced by various microorganisms or natural catechol compounds widespread in the environment. In the presence of tropolone, an iron-chelating agent, growth of L. monocytogenes is completely inhibited. However, the growth inhibition can be relieved by the addition of dopamine or norepinephrine under their different isomeric forms, while the catecholamine derivatives 4-hydroxy-3-methoxyphenylglycol and normetanephrine did not relieve the inhibitory effect of tropolone. Preincubation of L. monocytogenes with chlorpromazine and yohimbine did not antagonize the growth-promoting effect of catecholamines in ironcomplexed medium. In addition, norepinephrine stimulated the growth-promoting effect induced by human transferrin in iron-limited medium. Furthermore, dopamine and norepinephrine allowed 55 Fe uptake by iron-deprived bacterial cells. The uptake of iron was energy dependent, as indicated by inhibition of 55 Fe uptake at 0°C as well as by preincubating the bacteria with KCN. Inhibition of 55 Fe uptake by L. monocytogenes was also observed in the presence of Pt(II). Moreover, when assessed by a whole-cell ferric reductase assay, reductase activity of L. monocytogenes was inhibited by Pt(II). These data demonstrate that dopamine and norepinephrine can function as siderophore-like compounds in L. monocytogenes owing to their ortho-diphenol function and that catecholamine-mediated iron acquisition does not involve specific catecholamine receptors but acts through a cell-bound ferrireductase activity.

show abstract

mentioning

confidence: 92%

Utilization of iron-catecholamine complexes involving ferric reductase activity in Listeria monocytogenes

Coulanges¹,

André²,

Ziegler³

et al. 1997

Infect Immun

Self Cite

View full text Add to dashboard Cite

show abstract

“…But, L. monocytogenes does not secrete iron chelators. Rather, it utilizes the ferric siderophores of other organisms or other iron-containing compounds, including catecholamines (Simon et al ., 1995;Coulanges et al ., 1996), citrate (Adams et al ., 1990) and transferrin (Hartford et al ., 1993). The genetic systems, membrane permeases, or surface receptors for such ferric complexes are not yet known.…”

Section: Introductionmentioning

confidence: 99%

Iron acquisition systems for ferric hydroxamates, haemin and haemoglobin in Listeria monocytogenes

Jin

Newton

Shao

et al. 2005

Molecular Microbiology

View full text Add to dashboard Cite

SummaryListeria monocytogenes is a Gram-positive bacterium that causes severe opportunistic infections in humans and animals. We biochemically characterized, for the first time, the iron uptake processes of this facultative intracellular pathogen, and identified the genetic loci encoding two of its membrane iron transporters. Strain EGD-e used iron complexes of hydroxamates (ferrichrome and ferrichrome A, ferrioxamine B), catecholates (ferric enterobactin, ferric corynebactin) and eukaryotic binding proteins (transferrin, lactoferrin, ferritin, haemoglobin). Quantitative determinations showed 10-100-fold lower affinity for ferric siderophores ( K m ª 1-10 nM) than Gramnegative bacteria, and generally lower uptake rates.

show abstract

“…Similarly to the case in other pathogenic bacteria, acquisition of iron by L. monocytogenes is indispensable for its viability and pathogenicity (Newton et al, 2005;Sword, 1966;Conte et al, 1996). In an iron-limited environment, L. monocytogenes has been shown to modulate a variety of iron-uptake systems such as a citrateinducible receptor of ferric citrate (Adams et al, 1990), siderophores, catechol siderophore-like molecules (Simon et al, 1995), a cell-surface transferrin-binding protein (Hartford et al, 1993) and ABC transporters acquiring ferric hydroxamates (Fhu) or haemin/haemoglobin (Hup) (Jin et al, 2006). Haem degradation is a critical step for haem utilization, but few studies of haem utilization in this organism have been conducted.…”

Section: Introductionmentioning

confidence: 99%

Structural and functional characterization of an Isd-type haem-degradation enzyme from Listeria monocytogenes

Duong

Park

Kim

et al. 2014

Acta Cryst D Biol Crystallogr

View full text Add to dashboard Cite

Bacterial pathogens have evolved diverse types of efficient machinery to acquire haem, the most abundant source of iron in the human body, and degrade it for the utilization of iron. Gram-positive bacteria commonly encode IsdG-family proteins as haem-degrading monooxygenases. Listeria monocytogenes is predicted to possess an IsdG-type protein (Lmo2213), but the residues involved in haem monooxygenase activity are not well conserved and there is an extra N-terminal domain in Lmo2213. Therefore, its function and mechanism of action cannot be predicted. In this study, the crystal structure of Lmo2213 was determined at 1.75 Å resolution and its haem-binding and haem-degradation activities were confirmed. Structure-based mutational and functional assays of this protein, designated as an Isd-type L. monocytogenes haem-degrading enzyme (Isd-LmHde), identified that Glu71, Tyr87 and Trp129 play important roles in haem degradation and that the N-terminal domain is also critical for its haem-degrading activity. The haem-degradation product of Isd-LmHde is verified to be biliverdin, which is also known to be the degradation product of other bacterial haem oxygenases. This study, the first structural and functional report of the haem-degradation system in L. monocytogenes, sheds light on the concealed haem-utilization system in this life-threatening human pathogen.

show abstract

Utilization of exogenous siderophores and natural catechols by Listeria monocytogenes

Cited by 31 publications

References 13 publications

Utilization of iron-catecholamine complexes involving ferric reductase activity in Listeria monocytogenes

Utilization of iron-catecholamine complexes involving ferric reductase activity in Listeria monocytogenes

Iron acquisition systems for ferric hydroxamates, haemin and haemoglobin in Listeria monocytogenes

Structural and functional characterization of an Isd-type haem-degradation enzyme from Listeria monocytogenes

Contact Info

Product

Resources

About