Plant antifungal proteins and their applications in agriculture

Yan, Juan; Yuan, Susu; Jiang, Luan-luan; Ye, Xiujuan; Ng, Tzi Bun; Wu, Zujian

doi:10.1007/s00253-015-6654-6

Cited by 59 publications

(27 citation statements)

References 247 publications

(221 reference statements)

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“…Certain plants produce antifungal proteins to defend against fungal growth. 10 Isolating these antifungal proteins and inserting them into different plants increases resistance against fungal pathogens in these new host plants. These proteins include chitinases and glucanases.…”

Section: Introductionmentioning

confidence: 99%

Improved antifungal activity of barley derived chitinase I gene that overexpress a 32 kDa recombinant chitinase in Escherichia coli host

Toufiq

Tabassum

Bhatti

et al. 2018

Brazilian Journal of Microbiology

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Agricultural crops suffer many diseases, including fungal and bacterial infections, causing significant yield losses. The identification and characterisation of pathogenesis-related protein genes, such as chitinases, can lead to reduction in pathogen growth, thereby increasing tolerance against fungal pathogens. In the present study, the chitinase I gene was isolated from the genomic DNA of Barley (Hordeum vulgare L.) cultivar, Haider-93. The isolated DNA was used as template for the amplification of the ∼935 bp full-length chitinase I gene. Based on the sequence of the amplified gene fragment, class I barley chitinase shares 93% amino acid sequence homology with class II wheat chitinase. Interestingly, barley class I chitinase and class II chitinase do not share sequence homology. Furthermore, the amplified fragment was expressed in Escherichia coli Rosetta strain under the control of T7 promoter in pET 30a vector. Recombinant chitinase protein of 35 kDa exhibited highest expression at 0.5 mM concentration of IPTG. Expressed recombinant protein of 35 kDa was purified to homogeneity with affinity chromatography. Following purification, a Western blot assay for recombinant chitinase protein measuring 35 kDa was developed with His-tag specific antibodies. The purified recombinant chitinase protein was demonstrated to inhibit significantly the important phytopathogenic fungi Alternaria solani, Fusarium spp, Rhizoctonia solani and Verticillium dahliae compared to the control at concentrations of 80 μg and 200 μg.

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Section: Introductionmentioning

confidence: 99%

Improved antifungal activity of barley derived chitinase I gene that overexpress a 32 kDa recombinant chitinase in Escherichia coli host

Toufiq

Tabassum

Bhatti

et al. 2018

Brazilian Journal of Microbiology

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“…and it was found that the purified protein remained thermostable up to 60°C and exerted inhibitory effect on pathogengic fungal growth, but it was rapidly inactivated when incubated at temperature above 60 C. Plants defend themselves against pathogens by producing secondary metabolites and proteins with antifungal activity. Yan . (2015) reviewed plant antifungal proteins and their applications in agriculture emphasizing thermostability and activity over a wide range of pH as desirable traits of such proteins.…”

Section: Isolation Of Proteinmentioning

confidence: 99%

Purification and characterization of a novel thermostable antifungal protein with chitinase activity from mung bean

Solanki¹,

Kumar²,

Parihar³

et al. 2018

JEB

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Aim : Methodology :Results : Interpretation :Antifungal proteins are produced by many plant species and participate in defence mechanisms against number of fungal pathogens. The main objective of the study was to purify and characterize the thermo-stable antifungal compound with chitinase activity from mung bean seeds to assess their antifungal potency.The antifungal protein was isolated through ammonium sulphate precipitation method followed by its purification through ion-exchange chromatography. The purified protein was characterized by evaluating its antifungal efficacy, thermal stability, chitinase activity and SDS PAGE profiling.Molecular mass of characterized antifungal protein was 50.6 kDa. Purified protein exhibited antifungal activity against pathogenic fungi and and sustained its thermo-stability up to 60°C with chitinase activity.The isolated antifungal proteins showed unique column chromatographic behaviour, molecular weight, specificity of chitinase activity and relatively high thermo-stability with potent antifungal activity. It can be used in different biomedical and pharmaceutical applications as bio-pesticides.

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“…Thus, it is of utmost importance to screen for new antifungal substances characterized by safety, high efficiency, environmental friendliness, and lower fungicide resistance. Among the candidates, antifungal peptides have considerable application potential and attracted attention [9,10,11,12].…”

Section: Introductionmentioning

confidence: 99%

Purification of an Antifungal Peptide from Seeds of Brassica oleracea var. gongylodes and Investigation of Its Antifungal Activity and Mechanism of Action

Wang

Zhang

et al. 2019

Molecules

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In this study, a 8.5-kDa antifungal peptide designated as BGAP was purified from the crude extract of the seeds of Brassica oleracea var. gongylodes by employing a protocol that comprised cation exchange chromatography on SP-Sepharose, cation exchange chromatography on Mono S and gel filtration chromatography on Superdex peptide. BGAP showed the highest amino acid sequence similarity to defensin peptides by mass spectrometric analysis. BGAP showed a broad spectrum of antifungal activity with a half maximal inhibitory concentration at 17.33 μg/mL, 12.37 μg/mL, 16.81 μg/mL, and 5.60 μg/mL toward Colletotrichum higginsianum, Exserohilum turcicum, Magnaporthe oryzae and Mycosphaerella arachidicola, respectively. The antifungal activity of BGAP remained stable (i) after heat treatment at 40–100 °C for 15 min; (ii) after exposure to solutions of pH 1–3 and 11–13 for 15 min; (iii) after incubation with solutions containing K+, Ca2+, Mg2+, Mn2+ or Fe3+ ions at the concentrations of 20–150 mmol/L for 2 h; and (iv) following treatment with 10% methyl alcohol, 10% ethanol, 10% isopropanol or 10% chloroform for 2 h. Fluorescence staining experiments showed that BGAP brought about an increase in cell membrane permeability, a rise in reactive oxygen species production, a decrease in mitochondrial membrane potential, and an accumulation of chitin at the hyphal tips of Mycosphaerella arachidicola.

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Plant antifungal proteins and their applications in agriculture

Cited by 59 publications

References 247 publications

Improved antifungal activity of barley derived chitinase I gene that overexpress a 32 kDa recombinant chitinase in Escherichia coli host

Improved antifungal activity of barley derived chitinase I gene that overexpress a 32 kDa recombinant chitinase in Escherichia coli host

Purification and characterization of a novel thermostable antifungal protein with chitinase activity from mung bean

Purification of an Antifungal Peptide from Seeds of Brassica oleracea var. gongylodes and Investigation of Its Antifungal Activity and Mechanism of Action

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