The pep4 gene encoding proteinase <scp>A</scp> is involved in dimorphism and pathogenesis of <scp>U</scp>stilago maydis

Soberanes-Gutiérrez, Cinthia V; Juárez-Montiel, Margarita; Olguin-Rodriguez, Omar; Hernández‐Rodríguez, César; Ruíz-Herrera, José; Villa‐Tanaca, Lourdes

doi:10.1111/mpp.12240

Cited by 28 publications

(25 citation statements)

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“…Cmu1 is a secreted virulence factor that controls the metabolic status of plant cells during fungal colonization; deletion of cmu1 reduces U. maydis virulence in the solopathogenic strain CL13 (26). Pep4 is a proteinase A located at the vacuole, which is involved in the yeast to micelium dimorphic transition and whose deletion causes reduced virulence including incomplete teliospore maturation (27). On the other hand, Afg1 and Afg3 are arabinofuranosidases that participate in the degradation of arabinoxylan, a plant cell wall component.…”

Section: Resultsmentioning

confidence: 99%

N-glycosylation of the protein disulfide isomerase Pdi1 ensuresUstilago maydisvirulence

Marín-Menguiano

Moreno-Sánchez

Barrales

et al. 2019

Preprint

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27Fungal pathogenesis depends on accurate secretion and location of 28 virulence factors which drive host colonization. Protein glycosylation is a 29 common posttranslational modification of cell wall components and other 30 secreted factors, typically required for correct protein localization, secretion 31 and function. Thus, the absence of glycosylation is associated with animal 32 and plant pathogen avirulence. While the relevance of protein glycosylation 33 for pathogenesis has been well established, the main glycoproteins 34 responsible for the loss of virulence observed in glycosylation-defective fungi 35 have not been identified. Here, we devise a proteomics approach to identify 36 such proteins and use it to demonstrate a role for the highly conserved protein 37 disulfide isomerase Pdi1 in virulence. We show that efficient Pdi1 N-38 glycosylation, which promotes folding into the correct protein conformation, is 39 required for full pathogenic development of the corn smut fungus Ustilago 40 maydis. Remarkably, the observed virulence defects are reminiscent of those 41 seen in glycosylation-defective cells suggesting that the N-glycosylation of 42 Pdi1 is necessary for the full secretion of virulence factors. All these 43 observations, together with the fact that Pdi1 protein and RNA expression 44 levels rise upon virulence program induction, suggest that Pdi1 glycosylation 45 is a crucial event for pathogenic development in U. maydis. Our results 46 provide new insights into the role of glycosylation in fungal pathogenesis. 47 48 49 50 3 51 Author summary 52 Fungal pathogens require virulence factors to be properly secreted and 53 localized to guarantee complete infection. In common with many proteins, 54 virulence factors must be post-translationally modified by glycosylation for 55 normal localization, secretion and function. This is especially important for 56 virulence factors, which are mainly comprised of cell wall and secreted 57 proteins. Aberrant glycosylation leads to a loss of virulence in both animal and 58 plant pathogenic fungi. We have previously demonstrated that glycosylation is 59 important for virulence of the corn smut fungus, Ustilago maydis. However, 60 the glycoproteins involved and their specific roles in the infection process 61 have not yet been reported. Here, we describe a proteomic assay designed to 62 identify glycoproteins involved in plant infection. Using this method, we define 63 the role of Pdi1 protein disulfide isomerase in virulence. Interestingly, 64 abolishing Pdi1 N-glycosylation mimics pdi1 defects observed during 65 infection, suggesting that Pdi1 N-glycosylation is required for the secretion of 66 virulence factors. We hypothesize that Pdi1 N-glycosylation is crucial for 67 maintaining proper effector protein folding during the infection process, 68 especially in the harsh conditions found inside the maize plant. 69 4 70 Introduction 71 Protein glycosylation is a common eukaryotic post-translational 72 mechanism required for the correct folding, activity and sec...

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Section: Resultsmentioning

confidence: 99%

N-glycosylation of the protein disulfide isomerase Pdi1 ensuresUstilago maydisvirulence

Marín-Menguiano

Moreno-Sánchez

Barrales

et al. 2019

Preprint

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“…Peptidases provide alternative carbon sources for glucose starving cells through degrading proteins (Handtke et al, 2018), and promote various progresses, such as cell growth and differentiation, apoptosis, cell cycle, and signaling (Ng et al, 2009). Mutant in peptidase gene has been known as an important drive for fungal adaptation to hosts and environment (Soberanes-Gutierrez et al, 2015;Cervantes-Montelongo and Ruiz-Herrera, 2019). Interestingly, none of the genes related to Asparagine, Glutamate, and Threonine were previously predicted.…”

Section: Discussionmentioning

confidence: 99%

Comparative Genomic Data Provide New Insight on the Evolution of Pathogenicity in Sporothrix Species

Huang

Zhou

2020

Front. Microbiol.

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Sporothrix species are commonly isolated from environmental and clinical samples. As common causes of zoonotic mycosis, Sporothrix species may result in localized or disseminated infections, posing considerable threat to animal and human health. However, the pathogenic profiles of different Sporothrix species varied, in virulence, geographic location and host ranges, which have yet to be explored. Analysing the genomes of Sporothrix species are useful for understanding their pathogenicity. In this study, we analyzed the whole genome of 12 Sporothrix species and six S. globosa isolates from different clinical samples in China. By combining comparative analyses with Kyoto Encyclopedia of Genes and Genomes (KEGG), Carbohydrate-Active enZymes (CAZy), antiSMASH, Pfam, and PHI annotations, Sporothrix species showed exuberant primary and secondary metabolism processes. The genome sizes of four main clinical species, i.e., S. brasiliensis, S. schenckii, S. globosa, and S. luriei were significantly smaller than other environmental and clinical Sporothrix species. The contracted genes included mostly CAZymes and peptidases genes that were usually associated with the decay of plants, as well as the genes that were associated with the loss of pathogenicity and the reduced virulence. Our results could, to some extent, explain a habitat shift of Sporothrix species from a saprobic life in plant materials to a pathogenic life in mammals and the increased pathogenicity during the evolution. Gene clusters of melanin and clavaric acid were identified in this study, which improved our understanding on their pathogenicity and possible antitumor effects. Moreover, our analyses revealed no significant genomic variations among different clinical isolates of S. globosa from different regions in China.

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“…For example, in the phytopathogenic species Ustilago maydis , the pep4 gene was found to encode a vacuolar protease homologous to Sc Pep4. Deletion of this gene showed a strong effect on the yeast to mycelium dimorphic transition and reduced the virulence of the strain compared to the wild type strain 27 . Also, in Trichoderma species, which are mycoparasitic fungi that are used as biocontrol agents of phytopathogenic fungi, secreted hydrolytic enzymes such as Prb1 are thought to play a key role in the process of mycoparasitism 28 29 .…”

Section: Pep4 and Prb1 Homologs In Pathogenic Fungi: Interesting Candmentioning

confidence: 97%

A Cinderella story: how the vacuolar proteases Pep4 and Prb1 do more than cleaning up the cell’s mass degradation processes

Kerstens¹,

Dijck²

2018

Microb Cell

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Recently, several research groups have assigned non-vacuolar functions to the well-known Saccharomyces cerevisiae vacuolar proteases Pep4 and Prb1, which are also known as proteinases A and B. These non-vacuolar activities seem to be autophagy-independent and stress-induced and suggest an unexplored but possibly prominent role for the proteases outside the vacuole. The functions range from the involvement in programmed cell death, to protection from hazardous protein forms and regulation of gene expression. We propose that a deeper understanding of these molecular processes will provide new insights that will be important for both fungal biology as well as studies in mammalian cells, as they might open up perspectives in the search for novel drug targets. To illustrate this, we summarize the recent literature on non-vacuolar Pep4 and Prb1 functions in S. cerevisiae and review the current data on the protein homologs in pathogenic fungi.

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The pep4 gene encoding proteinase A is involved in dimorphism and pathogenesis of Ustilago maydis

Cited by 28 publications

References 45 publications

N-glycosylation of the protein disulfide isomerase Pdi1 ensuresUstilago maydisvirulence

N-glycosylation of the protein disulfide isomerase Pdi1 ensuresUstilago maydisvirulence

Comparative Genomic Data Provide New Insight on the Evolution of Pathogenicity in Sporothrix Species

A Cinderella story: how the vacuolar proteases Pep4 and Prb1 do more than cleaning up the cell’s mass degradation processes

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