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Chapter 26 : , a Plant Pathogen

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Abstract:

The ability to produce a wider range of enzymes or isoenzymes more rapidly and in larger quantities than that of pectolytic saprophytic microorganisms enables species to invade living plants. Pectin is the major component of primary plant cell walls. Latent infection of potato tubers by the soft rot species is widespread, and because disease tends to develop only when host resistance is impaired, the species have often been described as opportunistic pathogens. Epidemiological studies of soft rot diseases have revealed that pectolytic species are generally not endemic in soil. In common with many other plant-pathogenic bacteria, the soft rot species can overwinter in contaminated plant residues remaining in the soil after harvest. The bacteria persist, albeit in decreased numbers, as long as the plant material is not completely decomposed. This chapter focuses on the one of the siderophores, chrysobactin, and the role of iron in this disease. The temporal pattern of expression of the pectate lyase-encoding genes was compared to that of the chrysobactin operon in bacteria grown in planta. A rapid destruction of plant tissues must allow the bacteria to overcome the host defenses and be somehow independent of the type III secretion system. It has recently been shown that 3937 induces systemic symptoms in the plant model . Such a pathosystem should help to identify plant iron mobilization reactions that may occur during pathogenesis.

Citation: Expert D, Rauscher L, Franza T. 2004. , a Plant Pathogen, p 402-412. In Crosa J, Mey A, Payne S, Iron Transport in Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555816544.ch26

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Type III Secretion System
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Figures

Image of FIGURE 1
FIGURE 1

Structures of the siderophores chrysobactin and achromobactin produced by 3937. Enterobactin produced by K-12 is used by as a xenosiderophore.

Citation: Expert D, Rauscher L, Franza T. 2004. , a Plant Pathogen, p 402-412. In Crosa J, Mey A, Payne S, Iron Transport in Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555816544.ch26
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Image of FIGURE 2
FIGURE 2

Comparison of the genetic organization of the loci involved in enterobactin (K-12) and chrysobactin ( 3937) biosynthesis and transport. Squares and arrows represent bidirectional promoters and genes or operons, respectively. In 3937, only the bidirectional promoter has been determined experimentally.

Citation: Expert D, Rauscher L, Franza T. 2004. , a Plant Pathogen, p 402-412. In Crosa J, Mey A, Payne S, Iron Transport in Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555816544.ch26
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Image of FIGURE 3
FIGURE 3

Modular structure of the chrysobactin synthetase CbsF protein. The different catalytic domains involved in the last steps of chrysobactin biosynthesis are shown.

Citation: Expert D, Rauscher L, Franza T. 2004. , a Plant Pathogen, p 402-412. In Crosa J, Mey A, Payne S, Iron Transport in Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555816544.ch26
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Image of FIGURE 4
FIGURE 4

Schematic view of the promoter regions of the , and , genes from 3937. The −35 and −10 promoter elements are represented by black rectangles. KdgR- and CRP-binding sites identified by foot-printing experiments are indicated by hatched and white boxes, respectively. The confirmed Fur-binding regions are underlined with circles.

Citation: Expert D, Rauscher L, Franza T. 2004. , a Plant Pathogen, p 402-412. In Crosa J, Mey A, Payne S, Iron Transport in Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555816544.ch26
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Image of FIGURE 5
FIGURE 5

Coordinated regulation of pectinolysis and iron transport in 3937. Under low-iron conditions, the Fur-mediated transcriptional repression of the genes involved in iron transport and pectinolysis is relieved. In the presence of iron, intracellular accumulation of the pectin degradation product KDG turns on the transcription of the pectinase-encoding genes by inactivation of the transcriptional repressor KdgR, as well as that of the genes involved in iron acquisition by an unknown mechanism.

Citation: Expert D, Rauscher L, Franza T. 2004. , a Plant Pathogen, p 402-412. In Crosa J, Mey A, Payne S, Iron Transport in Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555816544.ch26
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References

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1. El Hassouni, M.,, J.-P. Chambost,, D. Expert,, F. van Gigsegem,, and F. Barras. 1999. The minimal gene set member mrsA, encoding peptide methionine sulfoxide reductase, is a virulence determinant of the plant pathogen Erwinia chrysanthemi. Proc. Natl. Acad. Sci. USA 96: 887 892.
2. Enard, C.,, A. Diolez,, and D. Expert. 1988. Systemic virulence of Erwinia chrysanthemi 3937 requires a functional iron assimilation system. J. Bacteriol. 170: 2419 2426.
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12. Münzinger, M.,, H. Budzikiewicz,, D. Expert,, C. Enard,, and J.-M. Meyer. 2000. Achromobactin, a new citrate siderophore of Erwinia chrysanthemi. Z. Naturforsch. 55C: 328 332.
13. Nachin, L.,, M. El Hassouni,, L. Loiseau,, D. Expert,, and F. Barras. 2001. SoxR-dependent response to oxidative stress and virulence of Erwinia chrysanthemi: the key role of SufC, an orphan ABC ATPase. Mol. Microbiol. 39: 969 972.
14. Neema, C.,, J.-P. Laulhe`re,, and D. Expert. 1993. Iron deficiency induced by chrysosbactin in Saint-paulia leaves inoculated with Erwinia chrysanthemi. Plant Physiol. 102: 967 973.
15. Perombelon, M. C. M. 2002. Potato diseases caused by soft rot erwinias: an overview of pathogenesis. Plant Pathol. 51: 1 12.
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17. Persmark, M.,, D. Expert,, and J. B. Neilands. 1992. Ferric iron uptake in Erwinia chrysanthemi mediated by chrysobactin and related catechol type compounds. J. Bacteriol. 174: 4783 4789.
18. Rauscher, L.,, D. Expert,, B. F. Matzanke,, and A. X. Trautwein. 2002. Chrysobactin-dependent iron acquisition in Erwinia chrysanthemi: functional study of an homologue of the Escherichia coli ferric enterobactin esterase. J. Biol. Chem. 277: 2385 2395.
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Tables

Generic image for table
TABLE 1

Proteins involved in the biosynthesis of chrysobactin and transport of its ferric complex

Citation: Expert D, Rauscher L, Franza T. 2004. , a Plant Pathogen, p 402-412. In Crosa J, Mey A, Payne S, Iron Transport in Bacteria. ASM Press, Washington, DC. doi: 10.1128/9781555816544.ch26

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