Changes in pH and the Production of Organic Acids During Colonization of Tomato Petioles by <i>Botrytis cinerea</i>

Verhoeff, Karl W.; Leeman, Mats; Peer, R. van; Posthuma, L.; Schot, Nelleke; Eijk, G. W. van

doi:10.1111/j.1439-0434.1988.tb01024.x

Cited by 52 publications

(30 citation statements)

References 18 publications

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“…First, a rise in pH during infection of either rice or barley, and a rise in pH together with ammonia production during fungal growth in vitro were monitored. Some plant pathogenic fungi like S. sclerotiorum and B. cinerea are known to acidify their environment during infection via the secretion of acids [15]. Others, like Alternaria alternata and several Colletotrichum species, tend to alkalinize the invaded plant tissues via the secretion of alkali like ammonia [33], [34].…”

Section: Discussionmentioning

confidence: 99%

“…One particular signal transduction pathway present in fungi relates to the sensing and adaptation to pH. As compared to other microorganisms, fungi are capable of growth and development over wide pH ranges, and several species, including plant pathogens, can modulate the pH of their environment by secreting acids or alkali [15], [16]. Thus far, a single pH-signaling pathway has been identified whose composition seems conserved throughout the fungal kingdom.…”

Section: Introductionmentioning

confidence: 99%

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Adaptation to pH and Role of PacC in the Rice Blast Fungus Magnaporthe oryzae

et al. 2013

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Fungi are known to adapt to pH partly via specific activation of the Pal signaling pathway and subsequent gene regulation through the transcription factor PacC. The role of PacC in pathogenic fungi has been explored in few species, and each time its partaking in virulence has been found. We studied the impact of pH and the role of PacC in the biology of the rice pathogen Magnaporthe oryzae. Conidia formation and germination were affected by pH whereas fungal growth and appressorium formation were not. Growth in vitro and in planta was characterized by alkalinization and ammonia accumulation in the surrounding medium. Expression of the MoPACC gene increased when the fungus was placed under alkaline conditions. Except for MoPALF, expression of the MoPAL genes encoding the pH-signaling components was not influenced by pH. Deletion of PACC caused a progressive loss in growth rate from pH 5 to pH 8, a loss in conidia production at pH 8 in vitro, a loss in regulation of the MoPALF gene, a decreased production of secreted lytic enzymes and a partial loss in virulence towards barley and rice. PacC therefore plays a significant role in M. oryzae’s biology, and pH is revealed as one component at work during interaction between the fungus and its host plants.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Adaptation to pH and Role of PacC in the Rice Blast Fungus Magnaporthe oryzae

et al. 2013

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“…The fungus acidifies its environment by secreting oxalic and citric acid (Verhoeff et al, 1988;Germeier et al, 1994;Manteau et al, 2003), presumably as part of its infection strategy (Germeier et al, 1994;Manteau et al, 2003;Prins et al, 2000;ten Have et al, 2002). There are numerous examples of the modulation of expression of genes encoding secreted enzymes in plantpathogenic fungi (Rollins & Dickman, 1998;St Leger et al, 1998;Wubben et al, 2000;Yakoby et al, 2000).…”

Section: B Cinerea Cultures Exclusively Contain Secreted Ap Activitymentioning

confidence: 99%

“…BcAP1 has an additional unique characteristic in that it does not contain a disulphide bridge. To remain properly folded and stable, the BcAP1 enzyme presumably resides extracellularly since this is the most acidic 'environment' for B. cinerea (Verhoeff et al, 1988;Germeier et al, 1994;Manteau et al, 2003).…”

Section: Features Of the Bcap Gene Familymentioning

confidence: 99%

An aspartic proteinase gene family in the filamentous fungus Botrytis cinerea contains members with novel features

et al. 2004

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Botrytis cinerea, an important fungal plant pathogen, secretes aspartic proteinase (AP) activity in axenic cultures. No cysteine, serine or metalloproteinase activity could be detected. Proteinase activity was higher in culture medium containing BSA or wheat germ extract, as compared to minimal medium. A proportion of the enzyme activity remained in the extracellular glucan sheath. AP was also the only type of proteinase activity in fluid obtained from B. cinerea-infected tissue of apple, pepper, tomato and zucchini. Five B. cinerea genes encoding an AP were cloned and denoted Bcap1–5. Features of the encoded proteins are discussed. BcAP1, especially, has novel characteristics. A phylogenetic analysis was performed comprising sequences originating from different kingdoms. BcAP1 and BcAP5 did not cluster in a bootstrap-supported clade. BcAP2 clusters with vacuolar APs. BcAP3 and BcAP4 cluster with secreted APs in a clade that also contains glycosylphosphatidylinositol-anchored proteinases from Saccharomyces cerevisiae and Candida albicans. All five Bcap genes are expressed in liquid cultures. Transcript levels of Bcap1, Bcap2, Bcap3 and Bcap4 are subject to glucose and peptone repression. Transcripts from all five Bcap genes were detected in infected plant tissue, indicating that at least part of the AP activity in planta originates from the pathogen.

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“…It can infect different organs including cotyledons, leaves, stems, roots, flowers and fruits at different stages of their development. B. cinerea, like the closely related necrotrophic fungus S. sclerotiorum, uses an infection strategy based on the acidification of the ambient environment via the production of organic acids (oxalic or citric acids) (Verhoeff et al, 1988) and on the secretion of numerous cell-walldegrading enzymes, including proteases (Manteau et al, 2003). It has been reported that B. cinerea secretes several acidic proteases during pathogenesis.…”

Section: Introductionmentioning

confidence: 99%

pH controls both transcription and post-translational processing of the protease BcACP1 in the phytopathogenic fungus Botrytis cinerea

et al. 2009

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During pathogenesis, the ascomycete Botrytis cinerea secretes a range of cell-wall-degrading enzymes such as polygalacturonases, glucanases and proteases. We report the identification of a new member of the G1 family of proteases, BcACP1, which is secreted by B. cinerea during infection. The production of BcACP1 correlates with the acidification of the plant tissue, and transcriptional analysis of the Bcacp1 gene showed that it is only expressed under acidic growth conditions. Using a transcriptional reporter system, we showed that pH regulation of Bcacp1 is not mediated by the canonical PacC transcription factor binding site. Like other G1 proteases, BcACP1 is produced as a pro-enzyme. Trapping of the zymogen form allowed investigation of its maturation process. Evidence is presented for an autocatalytic proteolysis of the enzyme that is triggered by acidic pH. Environmental pH therefore controls Bcacp1 production at both the transcriptional and post-translational level.

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Changes in pH and the Production of Organic Acids During Colonization of Tomato Petioles by Botrytis cinerea

Cited by 52 publications

References 18 publications

Adaptation to pH and Role of PacC in the Rice Blast Fungus Magnaporthe oryzae

Adaptation to pH and Role of PacC in the Rice Blast Fungus Magnaporthe oryzae

An aspartic proteinase gene family in the filamentous fungus Botrytis cinerea contains members with novel features

pH controls both transcription and post-translational processing of the protease BcACP1 in the phytopathogenic fungus Botrytis cinerea

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