R-SNARE Homolog MoSec22 Is Required for Conidiogenesis, Cell Wall Integrity, and Pathogenesis of Magnaporthe oryzae

Song, Wenwen; Dou, Xiaowei; Qi, Zhongqiang; Wang, Qi; Zhang, Xing; Zhang, Haifeng; Guo, Min; Dong, Suomeng; Wang, Ping; Zheng, Xiaobo

doi:10.1371/journal.pone.0013193

Cited by 84 publications

(105 citation statements)

References 71 publications

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“…The aim was to analyze whether chitinase expression patterns are altered during cell wall stress. T. virens was found to be very sensitive to Congo red and calcofluor white, and while for other fungi concentrations in the range of 50 to 200 g/ml of these substances are used (9,14,17), for T. virens, addition of more than 5 g/ml Congo red to the medium with the spore suspension in liquid, static cultures led to such a drastic decrease in growth that comparison with normal growth was not possible. Unfortunately, growth on calcofluor white was completely abolished even at 1 g/ml under these growth conditions.…”

Section: Resultsmentioning

confidence: 99%

Differential Regulation of Orthologous Chitinase Genes in Mycoparasitic Trichoderma Species

Gruber

Kubicek

Seidl‐Seiboth

2011

Appl Environ Microbiol

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Mycoparasitic Trichoderma species have expanded numbers of fungal subgroup C chitinases that contain multiple carbohydrate binding modules and could thus be important for fungal cell wall degradation during the mycoparasitic attack. In this study, we analyzed the gene regulation of subgroup C chitinases in the mycoparasite Trichoderma virens. In addition to regulation by nutritional stimuli, we found complex expression patterns in different parts of the fungal colony, and also, the mode of cultivation strongly influenced subgroup C chitinase transcript levels. Thus, the regulation of these genes is governed by a combination of colonyinternal and -external signals. Our results showed completely different expression profiles of subgroup C chitinase genes in T. virens than in a previous study with T. atroviride, although both fungi are potent mycoparasites. Only a few subgroup C chitinase orthologues were found in T. atroviride and T. virens, and even those showed substantially divergent gene expression patterns. Microscopic analysis revealed morphogenetic differences between T. atroviride and T. virens, which could be connected to differential subgroup C chitinase gene expression. The biological function of fungal subgroup C chitinases therefore might not be as clear-cut as previously anticipated. They could have pleiotropic roles and might be involved in both degradation of exogenous chitinous carbon sources, including other fungal cell walls, and recycling of their own cell walls during hyphal development and colony formation.Several species of the fungal genus Trichoderma (sexual form, Hypocrea) are mycoparasites and are thus able to antagonize, parasitize, and kill other fungi. An integral part of the mycoparasitic attack is degradation of the prey's cell wall by chitinases, glucanases, and proteases (1). Genome analysis revealed that the numbers of chitinase-encoding genes are strongly expanded in mycoparasitic Trichoderma spp. in comparison to other filamentous fungi. Fungal chitinases belong to glycoside hydrolase family 18 (GH 18) and can be further subdivided into 3 different subgroups, A, B, and C (10, 11). Subgroup A chitinases in general contain no carbohydrate binding modules (CBMs), but subgroup B chitinases frequently have a CBM at the C-terminal end. All subgroup C (sgC) chitinases have multiple CBMs and have either two CBM 18 (chitin binding) domains or one CBM 18 and two CBM 50 (LysM) domains N terminal of their GH 18 module (5). CBMs enable efficient adherence of the enzyme to insoluble substrates and processive catalytic cleavage of the substrate (2). The additional chitinases in mycoparasitic Trichoderma spp. are members of subgroups B and C. While the saprotrophic species Trichoderma reesei has only 4 sgC chitinases, T. atroviride has 9 and T. virens has 15, suggesting the potential involvement of these chitinases in mycoparasitism (7). Surprisingly, only five orthologue pairs can be found in the sgC chitinases of T. atroviride and T. virens (TAC2/TVC2, TAC4/ TVC4, TAC5/TVC5, TAC6/TVC6, and T...

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Section: Resultsmentioning

confidence: 99%

Differential Regulation of Orthologous Chitinase Genes in Mycoparasitic Trichoderma Species

Gruber

Kubicek

Seidl‐Seiboth

2011

Appl Environ Microbiol

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“…It has been reported that the SEC22 ortholog of M. oryzae can restore defects in the yeast sec22 mutant (Song et al, 2010). Because Co-SEC22 exhibits striking sequence similarity to Mo-SEC22 (80% identity), it is plausible that M. oryzae SEC22 and C. orbiculare SEC22 are functional orthologs of the yeast SEC22 involved in transport between the ER and the Golgi apparatus (Jahn and Scheller, 2006).…”

Section: Discussionmentioning

confidence: 99%

Colletotrichum orbiculare Secretes Virulence Effectors to a Biotrophic Interface at the Primary Hyphal Neck via Exocytosis Coupled with SEC22-Mediated Traffic

Irieda

Maeda

Akiyama³

et al. 2014

The Plant Cell

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The hemibiotrophic pathogen Colletotrichum orbiculare develops biotrophic hyphae inside cucumber (Cucumis sativus) cells via appressorial penetration; later, the pathogen switches to necrotrophy. C. orbiculare also expresses specific effectors at different stages. Here, we found that virulence-related effectors of C. orbiculare accumulate in a pathogen-host biotrophic interface. Fluorescence-tagged effectors accumulated in a ring-like region around the neck of the biotrophic primary hyphae. Fluorescence imaging of cellular components and transmission electron microscopy showed that the ring-like signals of the effectors localized at the pathogen-plant interface. Effector accumulation at the interface required induction of its expression during the early biotrophic phase, suggesting that transcriptional regulation may link to effector localization. We also investigated the route of effector secretion to the interface. An exocytosis-related component, the Rab GTPase SEC4, localized to the necks of biotrophic primary hyphae adjacent to the interface, thereby suggesting focal effector secretion. Disruption of SEC4 in C. orbiculare reduced virulence and impaired effector delivery to the ring signal interface. Disruption of the v-SNARE SEC22 also reduced effector delivery. These findings suggest that biotrophy-expressed effectors are secreted, via the endoplasmic reticulum-to-Golgi route and subsequent exocytosis, toward the interface generated between C. orbiculare and the host cell.

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“…81 MoSec22 and MoVam7, the orthologs of yeast SNARE proteins Sec22 and Vam7, can also be demonstrated to have functions in vacuole assembly, which underlie the growth, conidiation, appressorium formation, and pathogenicity of M. oryzae. 82,83 Similarly, MoMon1 and MoYpt7 are the orthologs of the yeast proteins Mon1 and Ypt7.…”

Section: Molecular Mechanisms Of Autophagy In Pathogenic Fungimentioning

confidence: 99%

Autophagy vitalizes the pathogenicity of pathogenic fungi

Liu

Gao

et al. 2012

Autophagy

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R-SNARE Homolog MoSec22 Is Required for Conidiogenesis, Cell Wall Integrity, and Pathogenesis of Magnaporthe oryzae

Cited by 84 publications

References 71 publications

Differential Regulation of Orthologous Chitinase Genes in Mycoparasitic Trichoderma Species

Differential Regulation of Orthologous Chitinase Genes in Mycoparasitic Trichoderma Species

Colletotrichum orbiculare Secretes Virulence Effectors to a Biotrophic Interface at the Primary Hyphal Neck via Exocytosis Coupled with SEC22-Mediated Traffic

Autophagy vitalizes the pathogenicity of pathogenic fungi

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