Identification of a cowpea γ‐thionin with bactericidal activity

Franco, Octávio L.; Murad, André M.; Leite, José Roberto S. A.; Mendes, Paulo A.M.; Prates, Maura V.; Bloch, Carlos

doi:10.1111/j.1742-4658.2006.05349.x

Cited by 88 publications

(59 citation statements)

References 63 publications

(84 reference statements)

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“…They are commonly found in antimicrobial and cell-penetrating peptides, which frequently contain a great number of cationic residues joined with hydrophobic residues across different structures [30,31]. It has been demonstrated that some antimicrobial peptide classes, such as human a-defensins [32] and plant c-defensins [33], need arginines exposed on the peptide surface and their removal or substitution reduced bacterial killing activity. Moreover, although some reports have described the need for several arginines [33], Cn-AMP1 just shows a single Arg-5 exposed, which suggests that a single arginine is sufficient to start the antimicrobial activity process.…”

Section: Resultsmentioning

confidence: 99%

“…It has been demonstrated that some antimicrobial peptide classes, such as human a-defensins [32] and plant c-defensins [33], need arginines exposed on the peptide surface and their removal or substitution reduced bacterial killing activity. Moreover, although some reports have described the need for several arginines [33], Cn-AMP1 just shows a single Arg-5 exposed, which suggests that a single arginine is sufficient to start the antimicrobial activity process. This fact was corroborated by simulations performed by MacCallum et al [34] that suggest that transfer of multiple arginine residues into the membrane bilayer core is non-additive.…”

Section: Resultsmentioning

confidence: 99%

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Structural insights into Cn‐AMP1, a short disulfide‐free multifunctional peptide from green coconut water

et al. 2015

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a b s t r a c tMultifunctional and promiscuous antimicrobial peptides (AMPs) can be used as an efficient strategy to control pathogens. However, little is known about the structural properties of plant promiscuous AMPs without disulfide bonds. CD and NMR were used to elucidate the structure of the promiscuous peptide Cn-AMP1, a disulfide-free peptide isolated from green coconut water. Data here reported shows that peptide structure is transitory and could be different according to the microenvironment. In this regard, Cn-AMP1 showed a random coil in a water environment and an a-helical structure in the presence of SDS-d 25 micelles. Moreover, deuterium exchange experiments showed that Gly4, Arg5 and Met9 residues are less accessible to solvent, suggesting that flexibility and cationic charges seem to be essential for Cn-AMP1 multiple activities.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Structural insights into Cn‐AMP1, a short disulfide‐free multifunctional peptide from green coconut water

et al. 2015

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“…The link between loop 3 with operating centers of alpha-amylase in bruchids leads to preventing starch into the operating center of enzyme [14]. [26].…”

Section: Analyzing the Expression Of Recombinant Vrpdf1 Protein In T1mentioning

confidence: 99%

Expression analysis of recombinant Vigna radiata plant defensin 1 protein in transgenic tobacco plants

Thao¹,

Lan²,

Tường³

et al. 2017

J App Biol Biotech

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Bruchid resistance is regulated by defensin gene. Vigna radiata plant defensin 1 (VrPDF1) inhibits alpha-amylase activities in insect gut; therefore, insect will die of undigestion starch. VrPDF1 content in mungbean seeds is very low. Hence an increase in content of VrPDF1 in mungbean seeds leads to enhance alpha -amylase inhibition in larvae and bruchids, which is necessary for the study to improve bruchid resistance in mungbeans. This article presents the results of VrPDF1 gene expression in T1 generation transgenic tobacco seeds. It was confirmed that VrPDF1 gene was attached to genome of tobacco plants and translated to synthesize VrPDF1. Recombinant VrPDF1 protein was successfully expressed in seeds of four transgenic tobacco lines (T1 -7, T1-8, T1-10, T1-11), among which T1-10 line had the highest recombinant VrPDF1 content, reaching 8.57 g mg -1 total protein. The extract containing recombinant VrPDF1 from the transgenic tobacco lines effectively inhibited the activity of alpha-amylase from the intestine of larvae and weevils. However, the protein extract solution from T1 -10 line had the strongest inhibitory effect, so the activity of alpha-amylase was only 18.89% compared to controls. The analysis results of VrPDF1 gene expression in transgenic tobacco plants are fundamental to the transfer of pPhaso-dest-VrPDF1 vector into mungbean to improve bruchid resistance of mungbean and contribute to improving mungbean preservation.

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“…Thus, Cp-thionine II, identified in seeds of Vigna unguiculata, acts against Gram-positive and Gram-negative bacteria, Staphylococcus aureus, E. coli and Pseudomonas syringae [16]. Fabatins isolated from Vicia faba beans also inhibit the growth of various bacteria, but are inactive against yeast Saccharomyces cerevisiae and Candida albicans [17].…”

mentioning

confidence: 99%

“…There is both constitutive and inducible expression of genes, encoding plant defensins [11,14]. The main function of defensins is to inhibit fungal disease [8,11,15], but for some peptides there are antibacterial activity [16,17], inhibition of trypsin [18], and participation in the formation of resistance to heavy metals [19], cold stress [20,21], drought [22], salinity [23,24] and in developmental processes [25].…”

mentioning

confidence: 99%

PLANT DEFENSINS: BIOLOGICAL FUNCTION, MECHANISMS OF ACTION AND METHODS OF ANALYSIS (review)

Kulaeva¹,

Kliukova²,

Повыдыш³

et al. 2017

S-h. biol.

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A b s t r a c tOne of the actual problems of modern agriculture is crop loss due to various biotic and abiotic factors. In plants there is a multicomponent protection system, including the formation of protective barriers, activation the reaction of hypersensitivity and synthesis of antimicrobial peptides, which are low molecular weight compounds showing broad spectrum activity against fungi, bacteria and viruses. This group consists of several groups of peptides, including defensins, which are one of the most common classes of antimicrobial peptides and are detectable in all living organisms. Defensins are small (45-54 amino acids), cysteine-rich peptides involved in a different protective responses (B.P. Thomma et al., 2002). Genes which are coding plant defensins are expressed in different organs of plants, where their products are necessary for biotic and abiotic stresses. Thus, these peptides are extremely important in terms of getting crop lines that are resistant to pathogens and abiotic stresses. Defensins are characterized by a strong sequence variability that seems to correlate with a variety of mechanisms of action of these peptides that can induce pathogen's cell death by penetrating into a cell or by being on its surface (T.M. Shafee et al., 2016). Most of the plant defensins are characterized by the antifungal activity. Some defensins have antibacterial activity, which may be combined with activity against fungi. For a small number of plant defensins their participation in the processes of resistance to heavy metals, cold stress, drought, salinity, and in the development process is indicated. Modern approaches of molecular and computational biology allow an effective search for new forms of defensins activity by studying the wild, non-model plant objects. The development of next-generation sequencing methods («Next Generation Sequencing») make possible the intensive study of the transcriptomes of such objects. However, the correct annotation of the sequences of peptides, characterized by small size and high variability, can be done by usage the special programs, such as SPADA (Small Peptide Alignment Discovery Application) (P. Zhou et al., 2013). SPADA makes multiple sequence alignment of all known paralogous genes within a gene family and builds a predictive model for the search of new members of the same family. Prediction of newly identified active defensins and identification of conserved amino acids can also be performed by computational biology methods. An approach based on a multiple sequence alignment and subsequent cluster analysis allows dividing defensins into groups with similar functional activity (N.L. van der Weerden et al., 2013). Thus, the combination of modern methods of molecular and computational biology allows carrying out the study of this group of protective peptides with high efficiency.

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Identification of a cowpea γ‐thionin with bactericidal activity

Cited by 88 publications

References 63 publications

Structural insights into Cn‐AMP1, a short disulfide‐free multifunctional peptide from green coconut water

Structural insights into Cn‐AMP1, a short disulfide‐free multifunctional peptide from green coconut water

Expression analysis of recombinant Vigna radiata plant defensin 1 protein in transgenic tobacco plants

PLANT DEFENSINS: BIOLOGICAL FUNCTION, MECHANISMS OF ACTION AND METHODS OF ANALYSIS (review)

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