Stimulation of maize invertase activity following infection by Ustilago maydis

Billett, E. Ellen; Billett, Michael A.; Burnett, J. H.

doi:10.1016/s0031-9422(00)94352-8

Cited by 41 publications

(16 citation statements)

References 14 publications

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“…Galls are known to act as sinks for plant assimilates (Bronner, 1977(Bronner, , 1983Larson and Whitham, 1997), and high levels of soluble invertase are associated with the establishment of sink characteristics (Patrick, 1990;Sturm and Chrispeels, 1990;Yelle et al, 1991). Within the gall tissue, vacuolar acid invertase may hydrolyze sucrose to provide the hexoses required for elevated metabolic activity (Billet et al, 1977;Zhang et al, 1996), and invertases in the nutritive tissue are known to hydrolyze sucrose to glucose and fructose (Bronner, 1977). While gypsy moth wounding may also elicit invertase activity (Arnold and Schultz, 2002), the increase brought about by gallers was much greater than that caused by 1 wk of gypsy moth feeding in this study.…”

Section: Discussionmentioning

confidence: 99%

Biochemical Responses of Chestnut Oak to a Galling Cynipid

Allison

Schultz

2005

J Chem Ecol

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Abstract-We characterized the distribution of nutritional and defensive biochemical traits in galls elicited on chestnut oak (Quercus prinus L.) by the gall wasp Andricus petiolicolus Basse (Cynipidae) in comparison with gypsy moth-wounded and unwounded leaves. Gall cortex and epidermis exhibited elevated soluble peroxidase (POX) and soluble invertase activities, and greater condensed tannin concentrations than did nutritive tissues or leaves. Nutritive tissue, on which the insect feeds, contained few polyphenols, and lower POX and invertase activities compared with other gall tissues and leaves. Elevated total POX activity arose from a complex pattern of enhanced and suppressed isoform activities in galls. Invertase enzyme activity decreased in all tissues over the course of the 7-d study, although gypsy moth wounding suppressed this decline slightly in ungalled leaves. Our results indicate that the distribution of biochemical defenses in this typical cynipid gall differs significantly from the leaf tissue from which it is formed and support a role for invertases in establishing the gall as a sink. A. petiolicolus larvae do not induce, and may suppress, plant defense responses in nutritive tissue, while enzymatic activity and phenolic accumulation are enhanced in gall tissues surrounding feeding sites. These patterns suggest that the gall is manipulated by the insect to enhance its food and protective value.

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Section: Discussionmentioning

confidence: 99%

Biochemical Responses of Chestnut Oak to a Galling Cynipid

Allison

Schultz

2005

J Chem Ecol

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“…Understandably, much interest has been directed toward understanding the precise function of certain lytic enzymes, such as chitinases and ,B-1 ,3-glucanases, because of their proposed antifungal activity (3,4,8,9,30). However, increases in the activity of other enzymes, such as invertase, in plants challenged by pathogens (7,14,22) Figure 3. Transmission electron micrographs of tomato (susceptible cultivar, cv Bonny Best) root tissues infected by F. oxysporum radicislycopersici.…”

Section: Discussionmentioning

confidence: 99%

Accumulation of β-Fructosidase in the Cell Walls of Tomato Roots following Infection by a Fungal Wilt Pathogen

Benhamou¹,

Grenier²,

Chrispeels³

1991

Plant Physiol.

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Active defense in plants is associated with marked metabolic alterations, but little is known about the exact role of the reported changes in specific activity of several enzymes in infected plant tissues. ,j-Fructosidase (invertase), the enzyme that converts sucrose into glucose and fructose, increases upon infection by fungi and bacteria. To understand the relationship between fungal growth and #l-fructosidase accumulation, we used an antiserum raised against a purified deglycosylated carrot cell wall j-fructosidase to study by immunogold labeling the spatial and temporal distribution of the enzyme in susceptible and resistant tomato (Lycopersicon esculentum) root tissues infected with the necrotrophic fungus, Fusarium oxysporum f. sp. racidis-Iycopersici. In susceptible plants, the enzyme started to accumulate in host cell walls about 72 hours after inoculation. Accumulation occurred only in colonized cells and was mainly restricted to areas where the walls of both partners contacted each other. In resistant plants, accumulation of #l-fructosidase was noticeable as soon as 48 hours after inoculation and appeared to reach an optimum by 72 hours after inoculation. Increase in wall-bound #-fructosidase was not restricted to infected cells but occurred also, to a large extent, in tissues that remained uncolonized during the infection process. The enzyme also accumulated in wall appositions (papillae) and intercellular spaces. This pattern of enzyme distribution suggests that induction of s-fructosidase upon fungal infection is part of the plant's defense response. The possible physiological role(s) of this enzyme in infected tomato plants is discussed in relation to the high demand in energy and carbon sources during pathogenesis.An attack by potential pathogens elicits a complex plant defense response in which numerous genes are activated, resulting in the synthesis and accumulation of secondary metabolites (phytoalexins and phenolics), structural macromolecules (callose, lignin, and hydroxyproline-rich glycoproteins), and a variety ofproteins (pathogenesis-related proteins, enzyme inhibitors, hydrolytic enzymes, and enzymes of secondary metabolism) (2,8,12,18,20). Thus, infection of a plant by a pathogen is accompanied by a considerable metabolic change (15). One physiology that has not received much attention concerns the reported increase in the metabolic rate ofinfected plant tissues (24, 34, 35). Little is known about the enzymatic processes underlying this marked increase, which allows the plant cells to sustain their defense response. A growing body of evidence from several reports supports the concept that fungal infection causes a significant increase in fl-fructosidase, the enzyme that hydrolyzes sucrose into glucose and fructose (21,24, 28, 31). In accord with these observations, Sturm and Chrispeels (37) found that infection of carrot storage roots by Erwinia carotovora was associated with a rapid and marked increase in the level ofmRNA encoding extracellular ,B-fructosidase. Another line o...

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“…There are a number of publications indicating an increase in invertase activity as a response to biotic stress stimuli (Benhamou et al 1991;Fotopoulos et al 2003;Heisterüber et al 1994;Tang et al 1996;Wright et al 1995). However, for most of the systems analyzed, it has not been possible to distinguish the contribution of plant or fungus to the observed invertase activity increase (Billett et al 1977;Callow et al 1980;Krishnan and Pueppke 1988;Williams et al 1984). Only for the necrotrophic parasite Botrytis cinerea has it been possible to show a contribution of the fungus to the invertase increase during infection of Vitis vinifera (Ruffner et al 1992;Ruiz and Ruffner 2002).…”

mentioning

confidence: 99%

Cloning and Characterization of a Novel Invertase from the Obligate Biotroph Uromyces fabae and Analysis of Expression Patterns of Host and Pathogen Invertases in the Course of Infection

Voegele

Wirsel²,

Möll³

et al. 2006

MPMI

101

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Invertases are key enzymes in carbon partitioning in higher plants. They gain additional importance in the distribution of carbohydrates in the event of wounding or pathogen attack. Although many researchers have found an increase in invertase activity upon infection, only a few studies were able to determine whether the source of this activity was host or parasite. This article analyzes the role of invertases involved in the biotrophic interaction of the rust fungus Uromyces fabae and its host plant, Vicia faba. We have identified a fungal gene, Uf-INV1, with homology to invertases and assessed its contribution to pathogenesis. Expression analysis indicated that transcription began upon penetration of the fungus into the leaf, with high expression levels in haustoria. Heterologous expression of Uf-INV1 in Saccharomyces cerevisiae and Pichia pastoris allowed a biochemical characterization of the enzymatic activity associated with the secreted gene product INV1p. Expression analysis of the known vacuolar and cell-wallbound invertase isoforms of V. faba indicated a decrease in the expression of a vacuolar invertase, whereas one cellwall-associated invertase exhibited increased expression. These changes were not confined to the infected tissue, and effects also were observed in remote plant organs, such as roots. These findings hint at systemic effects of pathogen infection. Our results support the hypothesis that pathogen infection establishes new sinks which compete with physiological sink organs.

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Stimulation of maize invertase activity following infection by Ustilago maydis

Cited by 41 publications

References 14 publications

Biochemical Responses of Chestnut Oak to a Galling Cynipid

Biochemical Responses of Chestnut Oak to a Galling Cynipid

Accumulation of β-Fructosidase in the Cell Walls of Tomato Roots following Infection by a Fungal Wilt Pathogen

Cloning and Characterization of a Novel Invertase from the Obligate Biotroph Uromyces fabae and Analysis of Expression Patterns of Host and Pathogen Invertases in the Course of Infection

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