The Role of Catalase-Peroxidase Secreted by <i>Magnaporthe oryzae</i> During Early Infection of Rice Cells

Tanabe, Shigeru; Ishii-Minami, Naoko; Saitoh, K; Otake, Yuko; Kaku, Hanae; Shibuya, Naoto; Nishizawa, Yuji; Minami, Eiichi

doi:10.1094/mpmi-07-10-0175

Cited by 68 publications

(68 citation statements)

References 42 publications

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“…CatB is required for host infection due to its role in strengthening the cell wall and appressoria melanization, but it is not required for detoxifying host-derived ROS (Skamnioti et al, 2007). In contrast, catalase peroxidase (CpxB) is required for neutralizing host-derived ROS but does not affect virulence (Tanabe et al, 2011). It is likely that low catalase activity is compensated by other antioxidation systems during infection.…”

Section: Hemibiotrophs: Linking Redox Homeostasis With Primary Metabomentioning

confidence: 99%

Reactive oxygen species metabolism and plant-fungal interactions

Segal

Wilson

2018

Fungal Genetics and Biology

155

103

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Fungal interactions with plants can involve specific morphogenetic developments to access host cells, the suppression of plant defenses, and the establishment of a feeding lifestyle that nourishes the colonizer oftenbut not always-at the expense of the host. Reactive oxygen species (ROS) metabolism is central to the infection process, and the stage-specific production and/or neutralization of ROS is critical to the success of the colonization process. ROS metabolism during infection is dynamicsometimes seemingly contradictory-and involves endogenous and exogenous sources. Yet, intriguingly, molecular decision-making involved in the spatio-temporal control of ROS metabolism is largely unknown. When also considering that ROS demands are similar between pathogenic and beneficial fungal-plant interactions despite the different outcomes, the intention of our review is to synthesize what is known about ROS metabolism and highlight knowledge gaps that could be hindering the discovery of novel means to mediate beneficial plant-microbe interactions at the expense of harmful plant-microbe interactions.

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Section: Hemibiotrophs: Linking Redox Homeostasis With Primary Metabomentioning

confidence: 99%

Reactive oxygen species metabolism and plant-fungal interactions

Segal

Wilson

2018

Fungal Genetics and Biology

155

103

View full text Add to dashboard Cite

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“…There are intracellular and extracellular fungal bifunctional catalase-peroxidases. The intracellular representatives are present both in nonpathogenic and pathogenic fungi and, most interestingly, extracellular representatives are exclusively found in phytopathogenic fungi which seem to play an important role in host-pathogen interaction [21][22][23][24]. The predicted protein (gi|340516521) found in complex II could have a protective function for T. reesei, because a Blast2GO analysis assigned it a superoxide dismutase activity.…”

Section: Resultsmentioning

confidence: 99%

Secretomic Analysis Reveals Multi-Enzymatic Complexes in Trichoderma reesei Grown in Media Containing Lactose or Galactose

et al. 2015

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The fungus Trichoderma reesei is a major producer of plant cell wall-degrading enzymes, such as cellulases and hemicellulases. These enzymes have been used to hydrolyze agro-industrial wastes in processes of second-generation biofuel production. The disaccharide lactose, the main byproduct of dairy industry, is considered the most attractive substrate for the commercial production of cellulases by T. reesei. In the present work, it was shown that T. reesei, cultivated in media supplemented with either lactose or galactose, secrete proteins which behave as multi-enzymatic complexes. Blue Native electrophoresis (BN-PAGE) displayed two major bands which were specific or present in higher amounts in each secretome sample, complex I in galactose medium and complex II in lactose medium. The protein components of complexes I and II were identified by means of LC-MS/MS. The complexes were composed of different glycosyl hydrolases and predicted proteins related to biopolymer metabolism. Zymography coupled to BN-PAGE showed that T. reesei secretome presents higher cellulolytic and xylanolytic activities in lactose than in galactose-induced medium. The results presented here corroborate the existence of hydrolysis based on multi-enzymatic complexes in T. reesei secretome, as observed previously in other fungi, such as Trichoderma harzianum and Penicillium purpurogenum.

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“…Similarly, Cryptococcus cells lacking multiple catalases are completely virulent in a mouse inhalation model (54). Normal virulence is also manifest for Candida glabrata yeasts lacking the Cta1 catalase (60) and Magnaporthe oryzae cells lacking the CpxB catalase (61).…”

Section: Discussionmentioning

confidence: 99%

Redundant Catalases Detoxify Phagocyte Reactive Oxygen and Facilitate Histoplasma capsulatum Pathogenesis

et al. 2013

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Histoplasma capsulatum is a respiratory pathogen that infects phagocytic cells. The mechanisms allowing Histoplasma to overcome toxic reactive oxygen molecules produced by the innate immune system are an integral part of Histoplasma's ability to survive during infection. To probe the contribution of Histoplasma catalases in oxidative stress defense, we created and analyzed the virulence defects of mutants lacking CatB and CatP, which are responsible for extracellular and intracellular catalase activities, respectively. Both CatB and CatP protected Histoplasma from peroxide challenge in vitro and from antimicrobial reactive oxygen produced by human neutrophils and activated macrophages. Optimal protection required both catalases, as the survival of a double mutant lacking both CatB and CatP was lower than that of single-catalase-deficient cells. Although CatB contributed to reactive oxygen species defenses in vitro, CatB was dispensable for lung infection and extrapulmonary dissemination in vivo. Loss of CatB from a strain also lacking superoxide dismutase (Sod3) did not further reduce the survival of Histoplasma yeasts. Nevertheless, some catalase function was required for pathogenesis since simultaneous loss of both CatB and CatP attenuated Histoplasma virulence in vivo. These results demonstrate that Histoplasma's dual catalases comprise a system that enables Histoplasma to efficiently overcome the reactive oxygen produced by the innate immune system.

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The Role of Catalase-Peroxidase Secreted by Magnaporthe oryzae During Early Infection of Rice Cells

Cited by 68 publications

References 42 publications

Reactive oxygen species metabolism and plant-fungal interactions

Reactive oxygen species metabolism and plant-fungal interactions

Secretomic Analysis Reveals Multi-Enzymatic Complexes in Trichoderma reesei Grown in Media Containing Lactose or Galactose

Redundant Catalases Detoxify Phagocyte Reactive Oxygen and Facilitate Histoplasma capsulatum Pathogenesis

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