Characterization of aspartic proteinases in C. cardunculus L. callus tissue for its prospective transformation

Oliveira, Ana I.; Pereira, Cláudia; Costa, Diana Soares da; Teixeira, Jorge; Fidalgo, Fernanda; Pereira, Susana; Pissarra, José

doi:10.1016/j.plantsci.2009.11.008

Cited by 22 publications

(13 citation statements)

References 18 publications

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“…This study evaluated and characterized specially the diversity of cardosins as a basis for the selection of cardoon genotypes well adapted for traditional and innovative applications in the Mediterranean region. Although all previous studies showed that cardosin A is clearly dominant over the others, in our study we obtained four main groups of cardosins with a wide diversity in concentration and proportion between them. Three of the genotypes, namely 1M, 2M and 3M, did not reveal the peak of cardosin A at the normal retention volume in ion‐exchange chromatography.…”

Section: Discussioncontrasting

confidence: 59%

Selected Cardoon (Cynara cardunculus L.) Genotypes Suitable for PDO Cheeses in Mediterranean Regions

Barracosa

Rosa

Barros

et al. 2018

Chemistry & Biodiversity

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Cardoon flower extract is a traditional and exclusive rennet used for some PDO cheeses in several Mediterranean regions, due to its extremely high concentration in cardosins. In this preliminary study, six individual cardoon genotypes (1M - 6M) were selected because they revealed a wide and consistent diversity of total and specific cardosin concentrations in flowers. During three growing seasons, the stability of 12 biochemical characteristics of flower extracts and 26 plant morphological descriptors was confirmed. Surprisingly, the cardosin profiles of each genotype, based on four main groups A0, A1, A and B, were stable during the annual flower harvesting period and over all three years using ion-exchange chromatography and native-PAGE electrophoresis. This knowledge will allow an improvement in the quality and standardization of cardosin profiles from cardoon flowers used for cheese production and other innovative applications. The results obtained are promising for the development of a plant breeding program based on biochemical and morphological characteristics in order to obtain the most adapted plant architecture for combined purposes related to specific cardosins composition, flower and plant biomass production, and ease of harvesting.

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Section: Discussioncontrasting

confidence: 59%

Selected Cardoon (Cynara cardunculus L.) Genotypes Suitable for PDO Cheeses in Mediterranean Regions

Barracosa

Rosa

Barros

et al. 2018

Chemistry & Biodiversity

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“…The vacuolar sorting of aspartic proteinases (APs) (for a review, see Simões and Faro, 2004) is expected to follow yet another mechanism, as no common VSDs have been identified so far for this protein family. Moreover, the APs are an intriguing group of proteins: different APs accumulate in distinct compartments, and the same protein can be either secreted to the apoplast or directed to the vacuole, depending on the cell type and developmental stage, and suggesting a tight mechanism of regulation of trafficking Oliveira et al, 2010).…”

Section: Introductionmentioning

confidence: 99%

“…Despite their high degree of similarity in protein sequence, cardosin A and cardosin B may accumulate in different cell compartments during plant development (Vieira et al, 2001). Cardosin A has mostly a vacuolar localization, in lytic or storage vacuoles, depending on the organ it is expressed in and on specific cell needs (Ramalho-Santos et al, 1997;Pissarra et al, 2007;Pereira et al, 2008;Oliveira et al, 2010). Cardosin A was also localized in vacuoles when expressed in heterologous systems, such as Arabidopsis thaliana or Nicotiana tabacum (Duarte et al, 2008).…”

Section: Introductionmentioning

confidence: 99%

Cardosin A contains two vacuolar sorting signals using different vacuolar routes in tobacco epidermal cells

Pereira

Satiat‐Jeunemaître

et al. 2013

The Plant Journal

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SUMMARYSeveral vacuolar sorting determinants (VSDs) have been described for protein trafficking to the vacuoles in plant cells. Because of the variety in plant models, cell types and experimental approaches used to decipher vacuolar targeting processes, it is not clear whether the three well-known groups of VSDs identified so far exhaust all the targeting mechanisms, nor if they reflect certain protein types or families. The vacuolar targeting mechanisms of the aspartic proteinases family, for instance, are not yet fully understood. In previous studies, cardosin A has proven to be a good reporter for studying the vacuolar sorting of aspartic proteinases. We therefore propose to explore the roles of two different cardosin A domains, common to several aspartic proteinases [i.e. the plant-specific insert (PSI) and the C-terminal peptide VGFAEAA] in vacuolar sorting. Several truncated versions of the protein conjugated with fluorescent protein were made, with and without these putative sorting determinants. These domains were also tested independently, for their ability to sort other proteins, rather than cardosin A, to the vacuole. Fluorescent chimaeras were tracked in vivo, by confocal laser scanning microscopy, in Nicotiana tabacum cells. Results demonstrate that either the PSI or the C terminal was necessary and sufficient to direct fluorescent proteins to the vacuole, confirming that they are indeed vacuolar sorting determinants. Further analysis using blockage experiments of the secretory pathway revealed that these two VSDs mediate two different trafficking pathways.

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“…Oliveira and coworkers studied the expression of cardosins A and B in thistle callus and demonstrated the de novo production of these cardosins, which were shown to accumulate in the ER in an unprocessed state. This work demonstrated that these undifferentiated cells were able to produce cardosins, but their processing was different from that found in the flowers [37]. Although the results showed that the use of thistle callus cultures as an alternative source of cardosins might not be viable, it provided important fundamental data relating to AP processing in the system.…”

Section: Molecular Farming Of Aspartic Proteasesmentioning

confidence: 78%

“…The study of cardosins in other tissues has shown that their expression is not limited to the flowers and that the protein processing is tissue-dependent. Both cardosins A and B were found during postembryonic development of thistle [36], in the callus of thistle tissues [37], and also accumulated in the vacuoles when expressed in heterologous systems such as Arabidopsis thaliana or tobacco leaves [38,39]. This different behavior led to trafficking studies to further understand the movement of cardosins within cells.…”

Section: Cellular and Intracellular Localization Of Cardosinsmentioning

confidence: 99%

Plant Aspartic Proteases for Industrial Applications: Thistle Get Better

Folgado

Abranches

2020

Plants

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Plant proteases have a number of applications in industrial processes including cheese manufacturing. The flower of the cardoon plant (Cynara cardunculus L.) is traditionally used as a milk-clotting agent in protected designation of origin cheeses made from goat and sheep milk. Plant-derived rennets are of particular importance to consumers who wish to eat cheeses that are produced without harming any animals. In this review, we have highlighted the importance of plant proteases, particularly aspartic proteases, in industrial processes, as well as exploring more fundamental aspects of their synthesis. We have also reviewed and discussed the production of these enzymes using sustainable and cost-effective alternative platforms.

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Characterization of aspartic proteinases in C. cardunculus L. callus tissue for its prospective transformation

Cited by 22 publications

References 18 publications

Selected Cardoon (Cynara cardunculus L.) Genotypes Suitable for PDO Cheeses in Mediterranean Regions

Selected Cardoon (Cynara cardunculus L.) Genotypes Suitable for PDO Cheeses in Mediterranean Regions

Cardosin A contains two vacuolar sorting signals using different vacuolar routes in tobacco epidermal cells

Plant Aspartic Proteases for Industrial Applications: Thistle Get Better

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