Isolation and biological characterization of staphyloferrin B, a compound with siderophore activity from staphylococci

Haag, Hubert

doi:10.1016/0378-1097(94)90002-7

Cited by 21 publications

(38 citation statements)

References 15 publications

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“…The chemical structure (Fig. 3 C ) and biosynthetic pathways have been determined (13, 14, 21); however, the conformation of FeSB was previously unknown. Electron density for FeSB was obvious upon inspection of the SirA binding pocket.…”

Section: Resultsmentioning

confidence: 99%

“…The enzymatic pathways for SA and SB synthesis have been identified and shown to be encoded by the sfa and sbn operons, respectively (20–23). The sfa operon is present in all sequenced staphylococcal genomes, whereas the sbn operon is unique to S. aureus strains, although the original characterization of SB was from Staphylococcus hyicus culture supernatants (13, 14, 21). The only other documented occurrence of the SB biosynthetic operons in sequenced genomes are in the Gram-negative plant pathogen Ralstonia solanacearum , which was shown to synthesize SB, and the soil bacterium Cupriavidus metallidurans (23, 24).…”

Section: Introductionmentioning

confidence: 99%

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Specificity of Staphyloferrin B Recognition by the SirA Receptor from Staphylococcus aureus

Grigg

Cheung

Heinrichs

et al. 2010

Journal of Biological Chemistry

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Many organisms use sophisticated systems to acquire growth-limiting iron. Iron limitation is especially apparent in bacterial pathogens of mammalian hosts where free iron concentrations are physiologically negligible. A common strategy is to secrete low molecular weight iron chelators, termed siderophores, and express high affinity receptors for the siderophore-iron complex. Staphylococcus aureus, a widespread pathogen, produces two siderophores, staphyloferrin A (SA) and staphyloferrin B (SB). We have determined the crystal structure of the staphyloferrin B receptor, SirA, at high resolution in both the apo and Fe(III)-SB (FeSB)-bound forms. SirA, a member of the class III binding protein family of metal receptors, has N- and C-terminal domains, each composed of mainly a β-stranded core and α-helical periphery. The domains are bridged by a single α-helix and together form the FeSB binding site. SB coordinates Fe(III) through five oxygen atoms and one nitrogen atom in distorted octahedral geometry. SirA undergoes conformational change upon siderophore binding, largely securing two loops from the C-terminal domain to enclose FeSB with a low nanomolar dissociation constant. The staphyloferrin A receptor, HtsA, homologous to SirA, also encloses its cognate siderophore (FeSA); however, the largest conformational rearrangements involve a different region of the C-terminal domain. FeSB is uniquely situated in the binding pocket of SirA with few of the contacting residues being conserved with those of HtsA interacting with FeSA. Although both SirA and HtsA bind siderophores from the same α-hydroxycarboxylate class, the unique structural features of each receptor provides an explanation for their distinct specificity.

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Specificity of Staphyloferrin B Recognition by the SirA Receptor from Staphylococcus aureus

Grigg

Cheung

Heinrichs

et al. 2010

Journal of Biological Chemistry

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“…It remains unclear whether this effect simply results from enhanced iron uptake or some other process. 210 Staphyloferrin B does not contain catecholate moieties, 205,211,212 so a direct analogy to the protective role that enterobactin plays in this regard is unwarranted.…”

Section: Protection From Oxidative Stressmentioning

confidence: 99%

Beyond iron: non-classical biological functions of bacterial siderophores

2015

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Bacteria secrete small molecules known as siderophores to acquire iron from their surroundings. For over 60 years, investigations into the bioinorganic chemistry of these molecules, including fundamental coordination chemistry studies, have provided insight into the crucial role that siderophores play in bacterial iron homeostasis. The importance of understanding the fundamental chemistry underlying bacterial life has been highlighted evermore in recent years because of the emergence of antibiotic-resistant bacteria and the need to prevent the global rise of these superbugs. Increasing reports of siderophores functioning in capacities other than iron transport have appeared recently, but reports of “non-classical” siderophore functions have long paralleled those of iron transport. One particular non-classical function of these iron chelators, namely antibiotic activity, was even documented before the role of siderophores in iron transport was established. In this Perspective, we present an exposition of past and current work into non-classical functions of siderophores and highlight the directions in which we anticipate that this research is headed. Examples include the ability of siderophores to function as zincophores, chalkophores, and metallophores for a variety of other metals, sequester heavy metal toxins, transport boron, act as signalling molecules, regulate oxidative stress, and provide antibacterial activity.

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“…Among members of the staphylococci, two siderophores may be produced, staphyloferrin A (SA) and staphyloferrin B (SB) (Konetschny-Rapp et al, 1990; Meiwes et al, 1990; Drechsel et al, 1993; Haag et al, 1994). Enzymes for the synthesis of SA and SB are encoded from the sfaABCD and sbnABCDEFGHI loci, respectively (Dale et al, 2004a,b; Beasley et al, 2009; Cheung et al, 2009; Cotton et al, 2009) (Figure 2A).…”

Section: The Staphylococcal Irlps: Functions In Iron Acquisitionmentioning

confidence: 99%

The iron-regulated staphylococcal lipoproteins

Sheldon¹,

Heinrichs²

2012

Front. Cell. Inf. Microbio.

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Lipoproteins fulfill diverse roles in antibiotic resistance, adhesion, protein secretion, signaling and sensing, and many also serve as the substrate binding protein (SBP) partner to ABC transporters for the acquisition of a diverse array of nutrients including peptides, sugars, and scarcely abundant metals. In the staphylococci, the iron-regulated SBPs are significantly upregulated during iron starvation and function to sequester and deliver iron into the bacterial cell, enabling staphylococci to circumvent iron restriction imposed by the host environment. Accordingly, this subset of lipoproteins has been implicated in staphylococcal pathogenesis and virulence. Lipoproteins also activate the host innate immune response, triggered through Toll-like receptor-2 (TLR2) and, notably, the iron-regulated subset of lipoproteins are particularly immunogenic. In this review, we discuss the iron-regulated staphylococcal lipoproteins with regard to their biogenesis, substrate specificity, and impact on the host innate immune response.

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Isolation and biological characterization of staphyloferrin B, a compound with siderophore activity from staphylococci

Cited by 21 publications

References 15 publications

Specificity of Staphyloferrin B Recognition by the SirA Receptor from Staphylococcus aureus

Specificity of Staphyloferrin B Recognition by the SirA Receptor from Staphylococcus aureus

Beyond iron: non-classical biological functions of bacterial siderophores

The iron-regulated staphylococcal lipoproteins

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