Purification of yersiniabactin: a siderophore and possible virulence factor of Yersinia enterocolitica

Haag, Hubert; Hantke, Klaus; Drechsel, Hartmut; Stojiljković, Igor; Jung, Günther; Zähner, Hans

doi:10.1099/00221287-139-9-2159

Cited by 101 publications

(89 citation statements)

References 18 publications

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“…To explore this further, we extracted the 130b and Philadelphia-1 supernatants with several organic solvents and then assayed for loss of CAS reactivity. The siderophore activity was not extracted by either ethyl acetate or dichloromethane, further indicating that it is not a classic catecholate or phenolate (5,12,15,37,68,74,85). The reactivity was also not extractable with butanol, confirming that it is not a typical alcohol-soluble hydroxamate (68,74).…”

Section: Resultsmentioning

confidence: 95%

“…For a number of reasons, we strongly believe that this CAS-reactive substance represents a bona fide siderophore. First, the CAS assay has reliably identified and characterized a range of siderophores encompassing the iron chelators of over 20 bacterial genera (2,3,5,12,18,20,21,27,33,36,37,38,47,48,51,58,66,68,74,80,82,85,98). Second, the presence of CAS-reactive material correlated with enhanced aerobic growth in an iron-depleted defined medium (68).…”

Section: Discussionmentioning

confidence: 99%

“…This list has grown appreciably in recent years, largely due to the availability of the CAS assay. There are a number of other bacterial siderophores that, like legiobactin, do not possess the classic catecholate or hydroxamate structure and thus were or would have been overlooked by the Arnow and Csáky assays (12,15,18,33,37,61,68,85,94). In some ways, it is not surprising that L. pneumophila produces a siderophore.…”

Section: Discussionmentioning

confidence: 99%

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Discovery of a Nonclassical Siderophore, Legiobactin, Produced by Strains ofLegionella pneumophila

2000

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The mechanisms by which Legionella pneumophila, a facultative intracellular parasite and the agent of Legionnaires' disease, acquires iron are largely unexplained. Several earlier studies indicated that L. pneumophila does not elaborate siderophores. However, we now present evidence that supernatants from L. pneumophila cultures can contain a nonproteinaceous, high-affinity iron chelator. More specifically, when aerobically grown in a low-iron, chemically defined medium (CDM), L. pneumophila secretes a substance that is reactive in the chrome azurol S (CAS) assay. Importantly, the siderophore-like activity was only observed when the CDM cultures were inoculated to relatively high density with bacteria that had been grown overnight to log or early stationary phase in CDM or buffered yeast extract. Inocula derived from late-stationary-phase cultures, despite ultimately growing, consistently failed to result in the elaboration of siderophore-like activity. The Legionella CAS reactivity was detected in the culture supernatants of the serogroup 1 strains 130b and Philadelphia-1, as well as those from representatives of other serogroups and other Legionella species. The CAS-reactive substance was resistant to boiling and protease treatment and was associated with the <1-kDa supernatant fraction. As would also be expected for a siderophore, the addition of 0.5 or 2.0 M iron to the cultures repressed the expression of the CAS-reactive substance. Interestingly, the supernatants were negative in the Arnow, Csáky, and Rioux assays, indicating that the Legionella siderophore was not a classic catecholate or hydroxamate and, hence, might have a novel structure. We have designated the L. pneumophila siderophore legiobactin.The bacterium Legionella pneumophila is a ubiquitous inhabitant of natural and man-made aquatic environments, surviving both free, in biofilms, and as an intracellular parasite of protozoa (1,8,26,49,50). Yet, this gram-negative microbe is best known for being the principal etiologic agent of Legionnaires' disease, a potentially fatal form of human pneumonia (59,95). Within the lung, L. pneumophila flourishes as an intracellular parasite of the alveolar macrophages and perhaps the epithelium (1,8,13,41,63,84). A variety of studies indicate that iron is a key requirement for L. pneumophila extracellular replication, intracellular infection, and virulence (7,9,10,25,31,39,40,44,45,60,65,71,72,76,77,78,86,89,91). Despite this, the molecular basis of Legionella iron acquisition, particularly its earliest stages, is relatively unclear.Among all of the considerations regarding Legionella iron acquisition, it is the issue of siderophore production by L. pneumophila that has been the most controversial. In the early 1980s, shortly after the discovery of the Legionella genus, it was reported that L. pneumophila does not produce siderophores (79). This conclusion was based upon the negative results that were obtained from a standard bioassay, as well as the Arnow and Csáky assays, the customary methods for detecting ...

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Section: Resultsmentioning

confidence: 95%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

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Discovery of a Nonclassical Siderophore, Legiobactin, Produced by Strains ofLegionella pneumophila

2000

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“…The situation is reminiscent of pesticin production in Yersinia pestis: pesticin kills cells that utilize the Y. pestis siderophore yersiniabactin via the common receptor FyuA (Haag et al, 1993). This might be a mechanism to select against bacteria competing for a siderophore.…”

Section: Discussionmentioning

confidence: 99%

The colicin G, H and X determinants encode microcins M and H47, which might utilize the catecholate siderophore receptors FepA, Cir, Fiu and IroN

et al. 2003

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The colicin G producer Escherichia coli CA46, the colicin H producer E. coli CA58 and E. coli Nissle 1917 (DSM 6601) were shown to produce microcin H47 and the newly described microcin M. Both microcins were exported like colicin V by an RND-type export system, including TolC. The gene cluster encoding microcins H47 and M in strains CA46 and CA58 is nearly identical to that in strain DSM 6601, except that two additional genes are included. A Fur box identified in front of the microcin-encoding genes explained the observed iron regulation of microcin production. The catecholate siderophore receptors Fiu, Cir and FepA from E. coli and IroN, Cir and FepA from Salmonella were identified as receptors for microcins M, H47 and E492. IroN takes up the glucose-containing catecholate siderophore salmochelin, whose synthesis is encoded in the iro gene cluster found in Salmonella and certain, often uropathogenic, E. coli strains. A gene in this iro cluster, iroB, which encodes a putative glycosyltransferase, was also found in the microcin H47/M and microcin E492 gene clusters. These microcins could aid the producing strain in competing against enterobacteria that utilize catecholate siderophores.

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“…The pesticin receptor was designated FyuA because it also functions as a receptor for ferric yersiniabactin uptake (29). Yersiniabactin is a siderophore which is produced by Y. enterocolitica biotype 1B strains (24,27,29). We were able to demonstrate that both production of yersiniabactin and ferric yersiniabactin uptake via FyuA are required for mouse virulence (27,29,39).…”

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confidence: 88%

Evidence for two evolutionary lineages of highly pathogenic Yersinia species

1995

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Sensitivity to Yersinia pestis bacteriocin pesticin correlates with the existence of two groups of human pathogenic yersiniae, mouse lethal and mouse nonlethal. The presence of the outer membrane pesticin receptor (FyuA) in mouse-lethal yersiniae is a prerequisite for pesticin sensitivity. Genes that code for FyuA (fyuA) were identified and sequenced from pesticin-sensitive bacteria, including Y. enterocolitica biotype 1B (serotypes O8, O13, O20, and O21), Y. pseudotuberculosis serotype O1, Y. pestis, two known pesticin-sensitive Escherichia coli isolates (E. coli Phi and E. coli CA42), and two newly discovered pesticin-sensitive isolates, E. coli K49 and K235. A 2,318-bp fyuA sequence was shown to be highly conserved in all pesticin-sensitive bacteria, including E. coli strains (DNA sequence homology was 98.5 to 99.9%). The same degree of DNA homology (97.8 to 100%) was established for the sequenced 276-bp fragment of the irp2 gene that encodes high-molecular-weight protein 2, which is also thought to be involved in the expression of virulence by Yersinia species. Highly conserved irp2 was also found in all pesticin-sensitive E. coli strains. On the basis of the fyuA and irp2 sequence homologies, two evolutionary groups of highly pathogenic Yersinia species can be established. One group includes Y. enterocolitica biotype 1B strains, while the second includes Y. pestis, Y. pseudotuberculosis serotype O1, and irp2-positive Y. pseudotuberculosis serotype O3 strains. E. coli Phi, CA42, K49, and K235 belong to the second group. The possible proximity of these two iron-regulated genes (fyuA and irp2), as well as their high levels of sequence conservation and similar G؉C contents (56.2 and 59.8 mol%), leads to the assumption that these two genes may represent part of an unstable pathogenicity island that has been acquired by pesticin-sensitive bacteria as a result of a horizontal transfer.Human pathogenic yersiniae are known either as the causative agent of plague (Yersinia pestis) or as food-borne pathogens (Yersinia pseudotuberculosis and Yersinia enterocolitica) that cause intestinal diseases (5). The pathogenicity of each of these species depends on the presence of a closely related 70-kb virulence plasmid, pYV (1,17,22,38). Although the presence of pYV is absolutely required for pathogenicity, strains of these species can be distinguished by their virulence for mice, suggesting that the mouse virulence or lethality trait is determined by an additional chromosomal locus. Accordingly, pYV-harboring yersiniae can be divided into two groups. (i) Y. pestis, Y. pseudotuberculosis, and Y. enterocolitica biotype 1B belong to the mouse-lethal group (50% lethal intravenous dose [LD 50 ], Ͻ10 3 organisms), and (ii) the mouse-nonlethal group (intravenous LD 50 , Ͼ10 5 organisms) consists of Y. enterocolitica strains of non-1B biotypes (8,11,28).It has been shown that the mouse lethality trait in yersiniae is closely related to sensitivity to the lethal effect of pesticin, a bacteriocin produced by Y. pestis (6,7,26). The ex...

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Purification of yersiniabactin: a siderophore and possible virulence factor of Yersinia enterocolitica

Cited by 101 publications

References 18 publications

Discovery of a Nonclassical Siderophore, Legiobactin, Produced by Strains ofLegionella pneumophila

Discovery of a Nonclassical Siderophore, Legiobactin, Produced by Strains ofLegionella pneumophila

The colicin G, H and X determinants encode microcins M and H47, which might utilize the catecholate siderophore receptors FepA, Cir, Fiu and IroN

Evidence for two evolutionary lineages of highly pathogenic Yersinia species

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