Genetical and O-glycoproteomic analyses reveal the roles of three protein O-mannosyltransferases in phytopathogen Fusarium oxysporum f.sp. cucumerinum

Xu, Ye; Zhou, Hui; Zhao, Guangya; Yang, Jinghua; Luo, Yuanming; Sun, Shutao; Wang, Zhongfu; Li, Shaojie; Jin, Cheng

doi:10.1016/j.fgb.2019.103285

Cited by 13 publications

(11 citation statements)

References 43 publications

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“…Systematic study of glycosylation targets, including the profiling of the global repertoire of glycoproteins and their glycosites, will be critical to understand the mechanistic roles of glycosylation during fungal infection process. Although N‐ glycoproteomes of M. oryzae and F. graminearum (Yu et al ., 2016; Chen et al ., 2020), and O‐ glycoproteomes of F. oxysporum and B. cinerea have been generated and investigated recently (González et al ., 2014; Xu et al ., 2020), few O‐ glycoproteome and GPI anchoring proteomics studies have been performed to date. A comparative study of Penicillium species, for example, shows how much diversity in modifications is likely to exist within fungal glycoproteomes (Hykollari et al ., 2016).…”

Section: Conclusion and Future Perspectivesmentioning

confidence: 99%

Protein glycosylation during infection by plant pathogenic fungi

2021

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Summary Glycosylation is a conserved set of post‐translational modifications that exists in all eukaryotic cells. During the last decade, the role of glycosylation in plant pathogenic fungi has received significant attention and considerable progress has been made especially in Ustilago maydis and Magnaporthe oryzae. Here, we review recent advances in our understanding of the role of N‐glycosylation, O‐glycosylation and glycosylphosphatidylinositol (GPI) anchors during plant infection by pathogenic fungi. We highlight the roles of these processes in regulatory mechanisms associated with appressorium formation, host penetration, biotrophic growth and immune evasion. We argue that improved knowledge of glycosylation pathways and the impact of these modifications on fungal pathogenesis is overdue and could provide novel strategies for disease control.

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Section: Conclusion and Future Perspectivesmentioning

confidence: 99%

Protein glycosylation during infection by plant pathogenic fungi

2021

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“…For instance, the fact that deleting each member produces a phenotype that differs in pathogenesis suggests that Pmts have a range of substrates, most of which are still unidentified [ 14 ]. Significantly, the conservation of the crucial role of Pmt4 in fungal plant pathogenesis [ 16 , 38 , 40 , 41 ], together with the absence of Pmt4 orthologues in its hosts, makes Pmt4 an excellent candidate for targeting by antifungal drugs. Here, we summarize much of what is known about the structure, evolution, and function of Pmt family members.…”

Section: Protein Glycosylation In Fungimentioning

confidence: 99%

“…Our comparison of Pmts shows that Pmt1 is the extra Pmt family member in fungal divisions. In most fungi in which the Pmt family has been characterized, pmt1 mutants do not show major virulence defects; although the absence of Pmt1 leads to some growth defects in model organisms such as Botrytis cinerea , Fusarium oxysporum, C. albicans , and Magnaporthe oryzae , mutant cells do not show important virulence defects, except for a defect in plant penetration observed in B. cinerea ∆ pmt1 cells [ 38 , 41 , 59 , 60 ] ( Table 1 ). Similar results were found in A. nidulans : although some defects in growth were observed in pmt1 mutants, the penetrance of these defects is lower compared with that of other pmt mutants and no major defects in virulence were observed [ 54 ].…”

Section: The Role Of Pmts In Fungal Pathogenesis: Pmt4 As the Key Protein Factor In Virulencementioning

confidence: 99%

“…Among the three fungal Pmt proteins, Pmt4 is the most interesting from the point of view of virulence. Although it is not essential for viability in most of the fungal models in which its role has been explored, Pmt4 is crucial for pathogenic development [ 16 , 38 , 40 , 41 ]. Pmt4 might thus be the Pmt protein that O-mannosylates more virulence-related glycoproteins than the other Pmts do.…”

Section: The Role Of Pmts In Fungal Pathogenesis: Pmt4 As the Key Protein Factor In Virulencementioning

confidence: 99%

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Structural, Evolutionary, and Functional Analysis of the Protein O-Mannosyltransferase Family in Pathogenic Fungi

Pejenaute-Ochoa

Santana-Molina

Devos

et al. 2021

JoF

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Protein O-mannosyltransferases (Pmts) comprise a group of proteins that add mannoses to substrate proteins at the endoplasmic reticulum. This post-translational modification is important for the faithful transfer of nascent glycoproteins throughout the secretory pathway. Most fungi genomes encode three O-mannosyltransferases, usually named Pmt1, Pmt2, and Pmt4. In pathogenic fungi, Pmts, especially Pmt4, are key factors for virulence. Although the importance of Pmts for fungal pathogenesis is well established in a wide range of pathogens, questions remain regarding certain features of Pmts. For example, why does the single deletion of each pmt gene have an asymmetrical impact on host colonization? Here, we analyse the origin of Pmts in fungi and review the most important phenotypes associated with Pmt mutants in pathogenic fungi. Hence, we highlight the enormous relevance of these glycotransferases for fungal pathogenic development.

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“…Among these Fusarium pathogens, Fusarium oxysporum is a typical soilborne fungus that can colonize the plant vascular system and cause serious crop wilt disease (de Sain & Rep, 2015). The species affects more than 120 plant species, including some important crops such as banana, cotton, tomato, melon, and soybean (de Sain & Rep, 2015; Edel‐Hermann & Lecomte, 2019; Xu et al., 2020). However, strains usually only selectively infect one or a few host species (de Sain & Rep, 2015); these strains are classified as different formae speciales (ff.…”

Section: Introductionmentioning

confidence: 99%

FoEG1, a secreted glycoside hydrolase family 12 protein from Fusariumoxysporum, triggers cell death and modulates plant immunity

Zhang

Yan

et al. 2021

Molecular Plant Pathology

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Fusarium oxysporum is an important soilborne fungal pathogen with many different formae speciales that can colonize the plant vascular system and cause serious crop wilt disease worldwide. We found a glycoside hydrolase family 12 protein FoEG1, secreted by F. oxysporum, that acted as a pathogen‐associated molecular pattern (PAMP) targeting the apoplast of plants to induce cell death. Purified FoEG1 protein triggered cell death in different plants and induced the plant defence response to enhance the disease resistance of plants. The ability of FoEG1 to induce cell death was mediated by leucine‐rich repeat (LRR) receptor‐like kinases BAK1 and SOBIR1, and this ability was independent of its hydrolase activity. The mutants of cysteine residues did not affect the ability of FoEG1 to induce cell death, and an 86 amino acid fragment from amino acid positions 144 to 229 of FoEG1 was sufficient to induce cell death in Nicotiana benthamiana. In addition, the expression of FoEG1 was strongly induced in the early stage of F. oxysporum infection of host plants, and FoEG1 deletion or loss of enzyme activity reduced the virulence of F. oxysporum. Therefore, our results suggest that FoEG1 can contribute to the virulence of F. oxysporum depending on its enzyme activity and can also act as a PAMP to induce plant defence responses.

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Genetical and O-glycoproteomic analyses reveal the roles of three protein O-mannosyltransferases in phytopathogen Fusarium oxysporum f.sp. cucumerinum

Cited by 13 publications

References 43 publications

Protein glycosylation during infection by plant pathogenic fungi

Protein glycosylation during infection by plant pathogenic fungi

Structural, Evolutionary, and Functional Analysis of the Protein O-Mannosyltransferase Family in Pathogenic Fungi

FoEG1, a secreted glycoside hydrolase family 12 protein from Fusariumoxysporum, triggers cell death and modulates plant immunity

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