Characterization of maize chitinase‐A, a tough allergenic molecule

Volpicella, Mariateresa; Leoni, Claudia; Fanizza, Immacolata; Distaso, Maria; Leoni, Guido; Farioli, Laura; Naumann, Todd A.; Pastorello, Elide A.; Ceci, Luigi R.

doi:10.1111/all.13164

Cited by 15 publications

(11 citation statements)

References 20 publications

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“…The role of some CWPs in biotic stress have been studied in different plant species. For example, chitinase and endochitinase A have antifungal activity against chitin-containing fungal pathogens [51,52]. Overexpressing extensin enhanced Arabidopsis resistance to Pseudomonas syringae by promoting cell wall stiffness [53].…”

Section: Resultsmentioning

confidence: 99%

Defensive forwards: stress-responsive proteins in cell walls of crop plants

Niu

Wang

2020

Preprint

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12As the vital component of plant cell wall, proteins play important roles in stress response 13 through modifying wall structure and involving in wall integrity signaling. However, the 14 potential of cell wall proteins (CWPs) in improvement of crop stress tolerance has probably 15 been underestimated. Recently, we have critically reviewed the predictors, databases and 16 cross-referencing of subcellular locations of possible CWPs in plants (Briefings in 17 Bioinformatics 2018;19:1130-1140). In this study, taking maize (Zea mays) as an example, 18 we retrieved 1873 entries of probable maize CWPs recorded in UniProtKB. As a result, 863 19 maize CWPs are curated and classified as 59 kinds of protein families. By referring to GO 20 annotation and gene differential expression in Expression Atlas, we highlight the potential of 21 CWPs as defensive forwards in abiotic and biotic stress responses. In particular, several 22 CWPs are found to play key roles in adaptation to many stresses. String analysis also reveals 23 possibly strong interactions among many CWPs, especially those stress-responsive enzymes. 24The results allow us to narrow down the list of CWPs to a few specific proteins that could be 25 candidates to enhance maize resistance. 26

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Section: Resultsmentioning

confidence: 99%

Defensive forwards: stress-responsive proteins in cell walls of crop plants

Niu

Wang

2020

Preprint

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“…Proteomic analysis in Arabidopsis revealed that CWPs such as endochitinase A (ECA), pectinesterase, peroxidase, polygalacturonase, and xyloglucan endotransglucosylase/hydrolase were significantly changed in infected plants by Pseudomonas syringae, resulting in enhanced resistance (Jia et al, 2018). Chitinases have antifungal activity against chitin-containing fungal pathogens (Huynh et al, 1992;Volpicella et al, 2017). Overexpressing extensin enhanced the resistance of Arabidopsis toward Pseudomonas syringae by promoting cell wall stiffness (Wei and Shirsat, 2006).…”

Section: Potential Applications Of Cwps In Developing Stress-resistanmentioning

confidence: 99%

Digging for Stress-Responsive Cell Wall Proteins for Developing Stress-Resistant Maize

2020

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As a vital component of plant cell walls, proteins play important roles in stress response by modifying the structure of cell walls and involving in the wall integrity signaling pathway. Recently, we have critically reviewed the predictors, databases, and cross-referencing of the subcellular locations of possible cell wall proteins (CWPs) in plants (Briefings in Bioinformatics 2018;19:1130-1140). Here, we briefly introduce strategies for isolating CWPs during proteomic analysis. Taking maize (Zea mays) as an example, we retrieved 1873 probable maize CWPs recorded in the UniProt KnowledgeBase (UniProtKB). After curation, 863 maize CWPs were identified and classified into 59 kinds of protein families. By referring to gene ontology (GO) annotations and gene differential expression in the Expression Atlas, we have highlighted the potential of CWPs acting in the front line of defense against biotic and abiotic stresses. Moreover, the analysis results of cis-acting elements revealed the responsiveness of the genes encoding CWPs toward phytohormones and various stresses. We suggest that the stress-responsive CWPs could be promising candidates for applications in developing varieties of stressresistant maize.

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“…50 ChitA is a class IV chitinase found primarily in developing maize kernels of Zea mays that exhibits endochitinase activity. 51 Both chitinases are responsible for protecting the plants against fungal pathogens. 41,42,51,52 AppA is a periplasmic protein native to E. coli that acts as a phytase.…”

Section: Prototyping Proteins -Enzymesmentioning

confidence: 99%

“…51 Both chitinases are responsible for protecting the plants against fungal pathogens. 41,42,51,52 AppA is a periplasmic protein native to E. coli that acts as a phytase. 43 Phytases are an interesting class of enzymes because they break down phytate which is considered an antinutrient and reduces nutrient absorption from seeds (grains, beans, and nuts) in monogastric animals.…”

Section: Prototyping Proteins -Enzymesmentioning

confidence: 99%

Simple, Functional, Inexpensive Cell Extract forin vitroPrototyping of Proteins with Disulfide Bonds

Dopp

Reuel

2019

Preprint

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In vitro expression of proteins from E. coli extract is a useful method for prototyping and production of cytotoxic or unnatural products. However, proteins that have multiple disulfide bonds require custom extract that to date requires careful addition of exogenous, purified isomerase enzymes. Many important proteins such as enzymes, cytokines, and monoclonal antibodies require disulfide bonds for stabilization and/or proper activity. Currently the only solution to expressing these products is to purchase commercial kits (such as PUREfrex® (GeneFrontier) or PURExpress® (New England BioLabs)) or to grow up the KGK10 strain and supplement with purified enzymes (T7 RNA polymerase and disulfide bond isomerase C). This multistep process can limit the accessibility of such extract to some groups that wish to rapidly prototype proteins with disulfide bonds. In this work, we present a "one-pot" solution that does not require addition of supplemental enzymes. This is done using a commercially available SHuffle® T7 Express lysY strain of E. coli that can express both the needed T7 polymerase and DsbC isomerase enzymes. We find optimal growth conditions for our 1 L cultures in 2.5 L shake flasks (5.6 and 3.9 hr for harvest and induction respectively) using a luciferase (from Gaussia princeps) that contains 5 disulfide bonds as our reporter protein. The method presented here uses a continuous pass homogenizer and pilot scale lyophilizer to produce large volumes of extract; also, optimal reconstitution ratios of the dried extract are found. To show the broad applicability of the extract, three other enzymes containing ≥ 3 disulfide bonds (hevamine, endochitinase A, and periplasmic AppA) were also expressed from minimal genetic templates that had undergone rolling circle amplification.

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Characterization of maize chitinase‐A, a tough allergenic molecule

Cited by 15 publications

References 20 publications

Defensive forwards: stress-responsive proteins in cell walls of crop plants

Defensive forwards: stress-responsive proteins in cell walls of crop plants

Digging for Stress-Responsive Cell Wall Proteins for Developing Stress-Resistant Maize

Simple, Functional, Inexpensive Cell Extract forin vitroPrototyping of Proteins with Disulfide Bonds

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