BcIEB1, a Botrytis cinerea secreted protein, elicits a defense response in plants

Frías, Marcos; González, Mario; González, Celedonio; Brito, Nélida

doi:10.1016/j.plantsci.2016.06.009

Cited by 40 publications

(79 citation statements)

References 49 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In order to test the usefulness of the yeast expression systems reported here, several B. cinerea secretory proteins previously characterized by our group were selected (Table S1): BcSpl1 (Frías et al ., , ), BcIEB1 (Frías et al ., ; González et al ., ), BcSUN1 (Pérez‐Hernández et al ., ), and the xylanases BcXyn11A (Brito et al ., ; Noda et al ., ), BcXyn11B and BcXyn11C (García et al ., ). These six proteins had also been experimentally identified in various proteomic studies as components of the B. cinerea secretome (González et al ., ).…”

Section: Resultsmentioning

confidence: 99%

New tools for high‐throughput expression of fungal secretory proteins in Saccharomyces cerevisiae and Pichia pastoris

González

Brito

Hernández-Bolaños

et al. 2018

Microbial Biotechnology

Self Cite

View full text Add to dashboard Cite

Summary Heterologous protein expression in yeast, mostly in Saccharomyces cerevisiae and Pichia pastoris, is a well‐established and widely used technique. It typically requires the construction of an expression vector in Escherichia coli containing the foreign gene and its subsequent transformation into yeast. Although simple, this procedure has important limitations for the expression of large numbers of proteins, that is, for the generation of protein libraries. We describe here the development of a novel system for the easy and fast expression of heterologous proteins both in S. cerevisiae and in P. pastoris, under the control of the GAL1 and AOX1 promoters respectively. Expression in S. cerevisiae requires only the transformation of yeast cells with an unpurified PCR product carrying the gene to be expressed, and the expression of the same gene in P. pastoris requires only the isolation of the plasmid generated in S. cerevisiae and its transformation into this second yeast, thus making this system suitable for high‐throughput projects. The system has been tested by the extracellular expression of 30 secretory fungal proteins.

show abstract

Section: Resultsmentioning

confidence: 99%

New tools for high‐throughput expression of fungal secretory proteins in Saccharomyces cerevisiae and Pichia pastoris

González

Brito

Hernández-Bolaños

et al. 2018

Microbial Biotechnology

Self Cite

View full text Add to dashboard Cite

show abstract

“…cinerea early secretome (Espino et al , 2010) and an abundant component of the late glycosecretome (González et al , 2014). This glycoprotein has no similarity to any characterized protein family, and the knockout of the Bcieb1 gene revealed that BcIEB1 is not involved in virulence (Frías et al , 2016). The isolated protein is able to cause necrosis of plant tissue and to induce other defence‐related symptoms in the plant (ion leakage, oxidative burst, and up‐regulation of defence genes), suggesting that BcIEB1 is recognized as a pathogen‐associated molecular pattern (PAMP) by plant cells (Frías et al , 2016).…”

Section: Introductionmentioning

confidence: 99%

“…This glycoprotein has no similarity to any characterized protein family, and the knockout of the Bcieb1 gene revealed that BcIEB1 is not involved in virulence (Frías et al , 2016). The isolated protein is able to cause necrosis of plant tissue and to induce other defence‐related symptoms in the plant (ion leakage, oxidative burst, and up‐regulation of defence genes), suggesting that BcIEB1 is recognized as a pathogen‐associated molecular pattern (PAMP) by plant cells (Frías et al , 2016). A conserved 35‐residue region of the protein, named ieb35, has been identified as the key functional region of this proteinaceous elicitor, as the ieb35 peptide by itself is able to induce a plant response almost identical to that of the whole BcIEB1 protein (Frías et al , 2016).…”

Section: Introductionmentioning

confidence: 99%

“…Additionally, BcIEB1 has also been shown to induce the systemic acquired resistance (SAR) response to B . cinerea in tobacco (Frías et al , 2016; González et al , 2017). SAR is a mechanism of induced resistance in plants that allows a faster and more efficient response against pathogen attack by “remembering” earlier exposure to microbes or to elicitor compounds (Fu and Dong, 2013).…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

The elicitor protein BcIEB1 and the derived peptide ieb35 provide long‐term plant protection

Pérez‐Hernández

González

et al. 2020

Plant Pathology

Self Cite

View full text Add to dashboard Cite

BcIEB is a small protein secreted by the phytopathogenic fungus Botrytis cinerea that is recognized as a pathogen-associated molecular pattern (PAMP) by plants. This activity is mapped to a highly conserved region of 35 amino acids, the peptide ieb35.Moreover, it has been shown that the protein and the peptide induce systemic resistance to B. cinerea after their infiltration into tobacco leaves. In this work, the possible use of BcIBE1 or ieb35 as plant protective agents has been tested. Tobacco plants were sprayed, infiltrated, or treated at the seedling stage with the protein or the peptide, and plant susceptibility to pathogens with different lifestyles was then studied at various times after treatment. The results showed that both BcIEB1 and ieb35 caused a similar reduction in the lesion sizes caused by B. cinerea and in colonization by Pseudomonas syringae pv. tabaci (reduced by c. 30% and c. 40%, respectively), independently of the treatment type. In addition, the number of B. cinerea inoculations leading to successful infections was also reduced in plants infiltrated or sprayed with BcIEB1/ieb35. The defence-related genes PR1a, NPR1, and osmotin ap24 were all induced by the protein and the peptide. BcIEB1, and especially ieb35, may be considered as a potential environmentally friendly treatment to increase plant resistance to pathogens. K E Y W O R D S Botrytis cinerea, elicitor, plant immunity, plant protection, systemic response S U PP O RTI N G I N FO R M ATI O N Additional supporting information may be found online in the Supporting Information section. How to cite this article: Pérez-Hernández A, González M, González C, Brito N. The elicitor protein BcIEB1 and the derived peptide ieb35 provide long-term plant protection.

show abstract

“…fungi that produce hyphae as growth structures, or in fungi which have at least a pseudohyphal growth stage. [12][13][14][15] However, the presence and abundant expression of CPPs in fungi with all types of life-styles suggests that the main biological functions are not solely related to fungal-plant interactions but to other, more general aspects of fungal growth. [9][10][11] CPPs are important factors in fungal-plant interactions.…”

Section: Introductionmentioning

confidence: 99%

The fungal cerato-platanin protein EPL1 forms highly ordered layers at hydrophobic/hydrophilic interfaces

et al. 2015

View full text Add to dashboard Cite

Cerato-platanin proteins (CPPs) and hydrophobins are two classes of small, secreted proteins that are exclusively found in fungi. CPPs are known as chitin-binding proteins, and were recently also shown to form protein layers at air/water interfaces, but the features of these layers were not investigated on the molecular level yet. In this study, by means of atomic force microscopy (AFM), EPL1, a member of the CPP family was shown to form highly ordered monolayers at a hydrophobic surface/liquid-interface. Furthermore, two new hydrophobins were analysed, and the influence of EPL1 on hydrophobin layers was studied in situ. Hydrophobins are amphiphilic proteins that are able to self-assemble at hydrophobic/hydrophilic interfaces, thereby inverting the polarity of the surface. This renders fungal growth structures such as spores water repellent. The combination of AFM data and wettability experiments led to the conclusion that in presence of both, hydrophobins and EPL1, a previously unknown hybrid layer is formed. This mixed protein layer is on one hand not inverting but enhancing the hydrophobicity of HOPG (highly oriented pyrolytic graphite), typical for EPL1, and on the other hand, it is stable and water insoluble, which is reminiscent of hydrophobin layers.

show abstract

BcIEB1, a Botrytis cinerea secreted protein, elicits a defense response in plants

Cited by 40 publications

References 49 publications

New tools for high‐throughput expression of fungal secretory proteins in Saccharomyces cerevisiae and Pichia pastoris

New tools for high‐throughput expression of fungal secretory proteins in Saccharomyces cerevisiae and Pichia pastoris

The elicitor protein BcIEB1 and the derived peptide ieb35 provide long‐term plant protection

The fungal cerato-platanin protein EPL1 forms highly ordered layers at hydrophobic/hydrophilic interfaces

Contact Info

Product

Resources

About