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Klaus Apel - One of the best experts on this subject based on the ideXlab platform.
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systemic and local induction of an arabidopsis thionin gene by wounding and pathogens
Plant Journal, 1998Co-Authors: Alberto Vignutelli, Klaus Apel, Claus Wasternack, Holger BohlmannAbstract:Summary The Arabidopsis Thi2.1 thionin gene was cloned and sequenced. The promoter was fused to the uidA gene and stably transformed into Arabidopsis to study its regulation. GUS expression levels correlated with the steady-state levels of Thi2.1 mRNA, thus demonstrating that the promoter is sufficient for the regulation of the Thi2.1 gene. The sensitivity of the Thi2.1 gene to methyl jasmonate was found to be developmentally determined. Systemic and local expression could be induced by wounding and inoculation with Fusarium oxysporum f sp. matthiolae. A deletion analysis of the promoter identified a fragment of 325 bp upstream of the start codon, which appears to contain all the elements necessary for the regulation of the Thi2.1 gene. These results support the view that thionins are defence proteins, and indicate the possibility that resistance of Arabidopsis plants to necrotrophic fungal pathogens is mediated through the octadecanoid pathway.
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overexpression of an endogenous thionin enhances resistance of arabidopsis against fusarium oxysporum
The Plant Cell, 1997Co-Authors: Petra Epple, Klaus Apel, Holger BohlmannAbstract:Thionins are antimicrobial proteins that are thought to be involved in plant defense. Concordant with this view, we have recently shown that the Arabidopsis thionin Thi2.1 gene is inducible by phytopathogenic fungi. Here, we demonstrate that constitutive overexpression of this thionin enhances the resistance of the susceptible ecotype Columbia (Col-2) against attack by Fusarium oxysporum f sp matthiolae. Transgenic lines had a reduced loss of chlorophyll after inoculation and supported significantly less fungal growth on the cotyledons, as evaluated by trypan blue staining. Moreover, fungi on cotyledons of transgenic lines had more hyphae with growth anomalies, including hyperbranching, than on cotyledons of the parental line. No transcripts for pathogenesis-related PR-1, PR-5, or the pathogen-inducible plant defensin Pdf1.2 could be detected in uninoculated transgenic seedlings, indicating that all of the observed effects of the overexpressing lines are most likely the result of the toxicity of the THI2.1 thionin. Our findings strongly support the view that thionins are defense proteins.
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an arabidopsis thaliana thionin gene is inducible via a signal transduction pathway different from that for pathogenesis related proteins
Plant Physiology, 1995Co-Authors: Petra Epple, Klaus Apel, Holger BohlmannAbstract:Two cDNAs encoding thionin preproproteins have been isolated from Arabidopsis thaliana. The corresponding genes have been designated Thi2.1 and Thi2.2. Southern blot analysis suggests that A. thaliana most probably contains single genes for both thionins. Thi2.2 transcripts have a low basal level in seedlings and show circadian variation. Thi2.2 transcripts were also detected in rosette leaves. No potent elicitors have been found for the Thi2.2 gene. Transcripts of the Thi2.1 gene are not detectable in seedlings but are present in rosette leaves and at a very high level in flowers and in siliques. The expression of the Thi2.1 gene is highly inducible in seedlings by pathogens, silver nitrate, and methyl jasmonate, but not by salicylate, indicating that the gene is induced by a signal transduction pathway that is at least partly different from that for the pathogenesis-related proteins.
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specific and different expression patterns of two members of the leaf thionin multigene family of barley in transgenic tobacco
Plant Science, 1995Co-Authors: Sonke Holtorf, Klaus Apel, Holger BohlmannAbstract:Thionins are cysteine-rich, basic, and toxic proteins that are assumed to be involved in the defense against pathogens. Barley (Hordeum vulgare L. cv. Carina) contains a large gene family coding for leaf-specific thionins that comprises more than 50 genes per haploid genome. How the expression of these variants is regulated was not known. To address this question, we have cloned 2 of these thionin genes, BTH6 and BTH7, each belonging to one of 2 subgroups, and analysed their sequences. Both code for typical leaf thionin proteins. Their promoter regions have an identity of about 40% except for a region of 90 bp in the downstream region which has an identity of 80%. As reflected by these sequence differences, both promoters behave differently when placed in front of the uidA gene and analysed in transgenic tobacco plants. Whereas the BTH6 promoter is constitutively expressed in most tissues of transgenic tobacco plants except the roots, the BTH7 promoter is only active in the vascular strands of the stem and older leaves. The BTH6 promoter is highly active in the epidermis and in xylem elements whereas the BTH7 promoter shows very high activity in phloem elements. In addition, both promoters are differently regulated by light. The BTH7 promoter is only active in the light. The BTH6 promoter shows a differential regulation in seedlings, being active in the hypocotyl in darkness but not in the cotyledons and vice versa in the light. Our results indicate that the expression of the barley leaf thionin multigene family is regulated differentially at the transcriptional level.
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The Formation of Leaf Thionins and their Effecton the Viability of Isolated Protoplasts of Barley (Hordeum vulgare L.)
Journal of Plant Physiology, 1995Co-Authors: Klaus Apel, Horst BindingAbstract:Summary Thus far, reliable regeneration of plants from isolated protoplasts of cereals is restricted to embryogenicin vitro cultures as the starting material. In the present work we provide evidence that thionins released from the leaf material may contribute to the regeneration incompetence of barley leaf protoplasts. This conclusion is based on the following observations: Leaf thionins and their corresponding RNA are not found in young sexual embryos used for initiating embryogenic cultures or in embryogenic cells yielding regenerable protoplasts, but occur in significant amounts in non-regenerable callus and leaves; furthermore, wounding of leaves during the preparation of protoplasts induced a strong increase in leaf thionin mRNA. Improved stability and microcallus formation of leaf protoplasts were obtained when an antiserum against leaf thionins was added to the sample.
Holger Bohlmann - One of the best experts on this subject based on the ideXlab platform.
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arabidopsis thionin like genes are involved in resistance against the beet cyst nematode heterodera schachtii
Plant Physiology and Biochemistry, 2019Co-Authors: Bachar Almaghrabi, Adil Zahoor, Kausar Hussain Shah, Holger BohlmannAbstract:Abstract Plants express various antimicrobial peptides including thionins to protect themselves against pathogens. It was recently found that, in addition to four thionin genes, Arabidopsis contains 67 thionin-like (ThiL) genes including six pseudogenes. It is known that thionins have antimicrobial activity and are part of the plant defense system, however, nothing is known about ThiL genes. In this study, we present a bioinformatic analysis of the (ThiL) gene family in Arabidopsis. We identified 15 different motifs which positioned the ThiL peptides in four groups. A comparison of amino acid sequences showed that the ThiL peptides are actually more similar to the acidic domain of thionin proproteins than to the thionin domain. We selected 10 ThiL genes to study the expression and possible function in the Arabidopsis plant. RT-PCR and promoter:GUS fusions showed that most genes were expressed at a very low level but in several organs and at different developmental stages. Some genes were also expressed in syncytia induced by the beet cyst nematode Heterodera schachti in roots while others were downregulated in syncytia. Some overexpression lines supported lower number of nematodes that developed on the roots after inoculation. Two of the genes resulted in a strong hypersensitive response when infiltrated into leaves of Nicotiana benthamiana. These results indicate that ThiL genes might be involved in the response to biotic stress. ThiL genes have been expanded in the Brassicales and specifically the Brassicaceae. The most extreme example is the CRP2460 subfamily that contains 28 very closely related genes from Arabidopsis which are mostly the result of tandem duplications.
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isolation and characterization of a thionin proprotein processing enzyme from barley
Journal of Biological Chemistry, 2015Co-Authors: Stephan Plattner, Clemens Gruber, Stefan Widmann, Christian W. Gruber, Johannes Stadlmann, Friedrich Altmann, Holger BohlmannAbstract:Thionins are plant-specific antimicrobial peptides that have been isolated from the endosperm and leaves of cereals, from the leaves of mistletoes, and from several other plant species. They are generally basic peptides with three or four disulfide bridges and a molecular mass of similar to 5 kDa. Thionins are produced as preproproteins consisting of a signal peptide, the thionin domain, and an acidic domain. Previously, only mature thionin peptides have been isolated from plants, and in addition to removal of the signal peptide, at least one cleavage processing step between the thionin and the acidic domain is necessary to release the mature thionin. In this work, we identified a thionin proprotein-processing enzyme (TPPE) from barley. Purification of the enzyme was guided by an assay that used a quenched fluorogenic peptide comprising the amino acid sequence between the thionin and the acidic domain of barley leaf-specific thionin. The barley TPPE was identified as a serine protease (BAJ93208) and expressed in Escherichia coli as a strep tag-labeled protein. The barley BTH6 thionin proprotein was produced in E. coli using the vector pETtrx1a and used as a substrate. We isolated and sequenced the BTH6 thionin from barley to confirm the N and C terminus of the peptide in planta. Using an in vitro enzymatic assay, the recombinant TPPE was able to process the quenched fluorogenic peptide and to cleave the acidic domain at least at six sites releasing the mature thionin from the proprotein. Moreover, it was found that the intrinsic three-dimensional structure of the BTH6 thionin domain prevents cleavage of the mature BTH6 thionin by the TPPE.
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comparison of periplasmic and intracellular expression of arabidopsis thionin proproteins in e coli
Biotechnology Letters, 2013Co-Authors: Amjad Abbas, Stephan Plattner, Kausar Hussain Shah, Holger BohlmannAbstract:Thionins are antimicrobial plant peptides produced as preproproteins consisting of a signal peptide, the thionin domain, and a so-called acidic domain. Only thionin itself has been isolated from plants. To study the processing of the precursor, it has to be produced in a heterologous system. Since both domains contain several cysteines and, due to the known antimicrobial activity of the thionin, we tested the expression of all four Arabidopsis proproteins as fusion proteins. Periplasmic expression as fusion with maltose binding protein was not successful but cytoplasmic expression as His-tagged TRX fusion proteins with a TEV recognition sequence resulted in proteins of correct size. Use of the SHuffle strain C3030 further improved the expression. Fusion proteins inhibited growth of Escherichia coli. They could be cleaved by TEV protease, releasing authentic proproteins without any additional amino acid at the N-terminus.
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systemic and local induction of an arabidopsis thionin gene by wounding and pathogens
Plant Journal, 1998Co-Authors: Alberto Vignutelli, Klaus Apel, Claus Wasternack, Holger BohlmannAbstract:Summary The Arabidopsis Thi2.1 thionin gene was cloned and sequenced. The promoter was fused to the uidA gene and stably transformed into Arabidopsis to study its regulation. GUS expression levels correlated with the steady-state levels of Thi2.1 mRNA, thus demonstrating that the promoter is sufficient for the regulation of the Thi2.1 gene. The sensitivity of the Thi2.1 gene to methyl jasmonate was found to be developmentally determined. Systemic and local expression could be induced by wounding and inoculation with Fusarium oxysporum f sp. matthiolae. A deletion analysis of the promoter identified a fragment of 325 bp upstream of the start codon, which appears to contain all the elements necessary for the regulation of the Thi2.1 gene. These results support the view that thionins are defence proteins, and indicate the possibility that resistance of Arabidopsis plants to necrotrophic fungal pathogens is mediated through the octadecanoid pathway.
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overexpression of an endogenous thionin enhances resistance of arabidopsis against fusarium oxysporum
The Plant Cell, 1997Co-Authors: Petra Epple, Klaus Apel, Holger BohlmannAbstract:Thionins are antimicrobial proteins that are thought to be involved in plant defense. Concordant with this view, we have recently shown that the Arabidopsis thionin Thi2.1 gene is inducible by phytopathogenic fungi. Here, we demonstrate that constitutive overexpression of this thionin enhances the resistance of the susceptible ecotype Columbia (Col-2) against attack by Fusarium oxysporum f sp matthiolae. Transgenic lines had a reduced loss of chlorophyll after inoculation and supported significantly less fungal growth on the cotyledons, as evaluated by trypan blue staining. Moreover, fungi on cotyledons of transgenic lines had more hyphae with growth anomalies, including hyperbranching, than on cotyledons of the parental line. No transcripts for pathogenesis-related PR-1, PR-5, or the pathogen-inducible plant defensin Pdf1.2 could be detected in uninoculated transgenic seedlings, indicating that all of the observed effects of the overexpressing lines are most likely the result of the toxicity of the THI2.1 thionin. Our findings strongly support the view that thionins are defense proteins.
Rong Guo - One of the best experts on this subject based on the ideXlab platform.
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Comparative studies on adsorption behavior of Thionine on gold nanoparticles with different sizes.
Journal of colloid and interface science, 2008Co-Authors: Yuanhua Ding, Zhuqing Chen, Ju Xie, Rong GuoAbstract:Abstract The adsorption behavior of Thionine on gold nanoparticles of two different mean diameters, 18 and 5 nm, was compared by using UV–vis spectroscopy, fluorescence spectroscopy, Fourier transform infrared (FT-IR) spectroscopy, transmission electron microscopy (TEM), dynamic light scattering (DLS), and quantum chemical calculations. It is found that the addition of small particles makes the monomer peak of Thionine finally disappear, and the corresponding dimer peak is significantly increased. Small gold nanoparticles make the equilibrium between the monomer and H-type dimer forms of Thionine move largely toward the dimer forms. Due to the stronger binding between Thionine and small gold nanoparticles, the fluorescence quenching of Thionine by small particles is enhanced compared to large particles, and the quenching is both static and dynamic. TEM images indicate that the addition of Thionine results in a heavy clustering for small particles, and the resulting Thionine–gold nanoclusters of about 45 nm were obtained. Quantum chemical calculations, which were based on the density functional theory (DFT) at the B3LYP level, and infrared spectroscopic studies show that the nitrogen atoms of the NH 2 moieties of Thionine bind to the gold nanoparticle surfaces. For 18 and 5 nm particles, the surface-to-volume atomic ratios are about 0.0597 and 0.2148, respectively. The higher surface-to-volume atomic ratio and the higher surface free energy result in stronger binding of Thionine on small particle surfaces, which can be used to modulate the arrangement of dye molecules on particle surfaces, and thus control the properties of organic–inorganic nanocomposite materials.
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RETRACTED: Studies on interactions of Thionine with gold nanoparticles
Colloids and Surfaces A: Physicochemical and Engineering Aspects, 2006Co-Authors: Yuanhua Ding, Xumin Zhang, Xiaoxia Liu, Rong GuoAbstract:The interactions of Thionine with gold nanoparticles have been studied by using UV-vis absorption spectroscopy, fluorescence spectroscopy, transmission electron microscopy, and Fourier transform infrared spectroscopy. With addition of small amounts of gold nanoparticles, the absorption peak intensity of monomers of Thionine decreases significantly, whereas that of H-type dimers of Thionine increases. With further addition of gold nanoparticles, both the absorption peak intensities of the monomers and dimers of Thionine increase, and the increasing magnitude of the peak intensity of the dimers is larger than that of monomers. The addition of gold nanoparticles makes the equilibrium between the monomer and H-type dimer forms of Thionine move toward the dimer forms. Due to the binding between Thionine and gold nanoparticles, the fluorescence quenching of Thionine by gold nanoparticles is enhanced with increasing amounts of gold nanoparticles, and the quenching is both static and dynamic. TEM images show that the addition of Thionine results in the formation of gold clusters, and further support the spectral results. Infrared spectroscopic studies show that the nitrogen atoms of both the NH 2 moieties of Thionine strongly bind to the gold nanoparticle surfaces through the electrostatic interaction of Thionine with gold nanoparticles. For 3-6 nm particles, the number of adsorbed Thionine molecules per gold particle is about 1.21 x 10 3 . Thionine molecules can not only bind to a particle to form a compact monolayer via both the NH 2 moieties of Thionine, but also bind to two particles via their two NH 2 moieties, respectively.
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Adsorption Characteristics of Thionine on Gold Nanoparticles
Langmuir, 2006Co-Authors: Yuanhua Ding, Xumin Zhang, Xiaoxia Liu, Rong GuoAbstract:This paper was retracted on October 4, 2007 (Langmuir 2007, 23, 11342). Adsorption characteristics of Thionine on gold nanoparticles have been studied by using UV−vis absorption spectroscopy, fluorescence spectroscopy, transmission electron microscopy (TEM), cyclic voltammetry and Fourier transform infrared spectroscopy. With the increasing concentration of gold nanoparticles, the absorption peak intensity of H-type dimers of Thionine increases continuously, whereas that of monomers of Thionine first increases and then decreases. The addition of gold nanoparticles makes the equilibrium between the monomer and H-type dimer forms of Thionine move toward the dimer forms. Furthermore, the adsorption behavior of Thionine on gold nanoparticles is also influenced by temperature. TEM images show that the addition of Thionine results in an obvious aggregation, and further support the absorption spectral results. The fluorescence intensity of adsorbed Thionine is quenched by gold nanoparticles due to the electronic...
Francisco Garciaolmedo - One of the best experts on this subject based on the ideXlab platform.
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synthetic and structural studies on pyrularia pubera thionin a single residue mutation enhances activity against gram negative bacteria
FEBS Letters, 2003Co-Authors: Miquel Vilaperello, Francisco Garciaolmedo, Andrea Sanchezvallet, Antonio Molina, David AndreuAbstract:The thionin from Pyrularia pubera (Pp-TH), a 47-residue peptide with four internal disulfide bonds, was efficiently produced by chemical synthesis. Its antimicrobial activity in vitro against several representative pathogens (EC50=0.3–3.0 μM) was identical to that of natural Pp-TH. This peptide has a unique Asp32 instead of the consensus Arg found in other thionins of the same family. In order to evaluate the effect of this mutation, the Arg32 analogue (Pp-TH(D32R)) was also synthesized and showed a significant increase in antibiotic activity against several Gram-negative bacteria, whereas it retained the same activity against other pathogens. The overall structure of Pp-TH(D32R) was maintained, though a slight decrease in the helical content of the peptide was observed.
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processing of thionin precursors in barley leaves by a vacuolar proteinase
FEBS Journal, 1997Co-Authors: Alicia Romero, Jocefa M Alamillo, Francisco GarciaolmedoAbstract:Thionins are synthesized as precursors with a signal peptide and a long C-terminal acidic peptide that is post-translationally processed. A fusion protein including the maltose-binding protein from Eschrrichia coli (MalE), thionin DG3 froin barley leaves, and its acidic C-terminal peptide has been used to obtain antibodies that recognize both domains of the precursor. In barley leaf sections. mature thionins accuinulated in the vacuolar content, while the acidic peptide was not detected in any cell fraction. Brefeldin A and inonensin inhibited processing of the precursor but its export from the microsomal fraction was not inhibited. Both purified vacuoles aiid an acid (pH 5.5) extract from leaves processed the fusion protein into a MalE-thionin and an acidic peptide fragment. A 70-kDa proteinase that effected this cleavage was purified froin the acid extract. Processing of the fusion protein by both lysed vacuoles and the purified proteinase was inhibited by Zn2+ and by Cu2+, but not by inhibitors of the previously described vacuolar processing thiol or aspartic proteinases. In vivo processing of the thionin precursor in leaf sections was also inhibited by Zn+, and Cu2+, Variants of the fusion protein with altered processing sites that represented thme of thionin precursors from different taxa were readily processed by the proteinase, whereas changing the polarity of either the C-terminal or N-terminal residues of the processing site prevented cleavage by the proteinase.
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expression of the α thionin gene from barley in tobacco confers enhanced resistance to bacterial pathogens
Plant Journal, 1993Co-Authors: M J Carmona, Juan Jose Lopezfando, Antonio Molina, José A. Fernández, Francisco GarciaolmedoAbstract:Thionins are cysteine-rich, 5 kDa polypeptides which are toxic to plant pathogens in vitro. Expression of the gene encoding alpha-thionin from barley endosperm, under the 35S promoter from cauliflower mosaic virus, conferred to transgenic tobacco enhanced resistance to the bacterial plant pathogens Pseudomonas syringae pv. tabaci 153 and P. syringae pv. syringae. The barley alpha-thionin gene, which has two introns, was correctly spliced in tobacco. The alpha-thionin in transgenic plants had the expected mobility in the gradient, when separated by high- performance liquid chromatography, reacted with monospecific antibodies and showed the expected antibiotic properties in vitro
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extreme divergence of a novel wheat thionin generated by a mutational burst specifically affecting the mature protein domain of the precursor
Journal of Molecular Biology, 1992Co-Authors: A Castagnaro, Carmen Marana, Francisco GarciaolmedoAbstract:A new type of neutral thionin (type V), specifically expressed in developing wheat endosperm, has been found to be encoded by a set of single-copy genes located in the long arms of chromosomes 1A, 1B and 1D, within less than 10,000 base-pairs of those corresponding to the highly basic type-I thionins. Divergence between types I and V has occurred through a process of accelerated evolution that has affected the amino acid sequence of the mature thionin but not the precursor domains corresponding to the N-terminal signal peptide and the long C-terminal acidic peptide. This process involved a deletion and a non-synonymous nucleotide substitution rate equal to the synonymous rate in the thionin sequence.
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characterization and analysis of thionin genes
Characterization and analysis of thionin genes | En: Genes Involved in Plant Defense | pag. 283-302 | Springer Verlag | 1992, 1992Co-Authors: Francisco Garciaolmedo, M J Carmona, Juan Jose Lopezfando, A Castagnaro, Antonio Molina, J A Fernandez, C HernandezlucasAbstract:The general designation of thionins has been proposed for a family of homologous proteins that have been isolated from different tissues in a wide range of plant taxa and have been variously named purothionins, viscotoxins, crambins, etc. (see Garcia-Olmedo et al., 1989). The possible involvement of thionins in plant defense was first suggested, on the basis of their in vitro toxicity to plant pathogens, by Fernandez de Caleya et al., (1972). Those observations had been prompted by earlier reports concerning the antimicrobial properties of these polypeptides (Stuart and Harris, 1942; Balls and Harris, 1944). Work on the thionins, which has been actively pursued over the past half-century, has been recently reviewed in detail (Garcia-Olmedo et al., 1989). For this reason. earlier work will only be partially summarized in the present chapter, which will focus on recent developments concerning thionin genes and their potential role in plant defense mechanisms.
Valdirene Moreira Gomes - One of the best experts on this subject based on the ideXlab platform.
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thionin like peptide from capsicum annuum fruits mechanism of action and synergism with fluconazole against candida species
BMC Microbiology, 2016Co-Authors: Gabriel Bonan Taveira, Fernanda Gomes Trindade, Maura Da Cunha, Andre De Oliveira Carvalho, Rosana Rodrigues, Valdirene Moreira GomesAbstract:Background Thionins are a family of plant antimicrobial peptides (AMPs), which participate in plant defense system against pathogens. Here we describe some aspects of the CaThi thionin-like action mechanism, previously isolated from Capsicum annuum fruits. Thionin-like peptide was submitted to antimicrobial activity assays against Candida species for IC50 determination and synergism with fluconazole evaluation. Viability and plasma membrane permeabilization assays, induction of intracellular ROS production analysis and CaThi localization in yeast cells were also investigated.
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thionin like peptides from capsicum annuum fruits with high activity against human pathogenic bacteria and yeasts
Biopolymers, 2014Co-Authors: Gabriel Bonan Taveira, Luciana S Mathias, Olney Vieira Da Motta, Olga Lima Tavares Machado, Andre De Oliveira Carvalho, Andre Teixeiraferreira, Jonas Perales, Ilka M Vasconcelos, Rosana Rodrigues, Valdirene Moreira GomesAbstract:Plants defend themselves against pathogens with production of antimicrobial peptides (AMPs). Herein we describe the discovery of a new antifungal and antibacterial peptide from fruits of Capsicum annuum that showed similarity to an already well characterized family of plant AMPs, thionins. Other fraction composed of two peptides, in which the major peptide also showed similarity to thionins. Among the obtained fractions, fraction 1, which is composed of a single peptide of 7 kDa, was sequenced by Edman method and its comparative sequence analysis in database (nr) showed similarity to thionin-like peptides. Tests against microorganisms, fraction 1 presented inhibitory activity to the cells of yeast Saccharomyces cerevisiae, Candida albicans, and Candida tropicalis and caused growth reduction to the bacteria species Escherichia coli and Pseudomonas aeruginosa. Fraction 3 caused inhibitory activity only for C. albicans and C. tropicalis. This fraction was composed of two peptides of ∼7 and 10 kDa, and the main protein band correspondent to the 7 kDa peptide, also showed similarity to thionins. This plasma membrane permeabilization assay demonstrates that the peptides present in the fractions 1 and 3 induced changes in the membranes of all yeast strains, leading to their permeabilization. Fraction 1 was capable of inhibiting acidification of the medium of glucose-induced S. cerevisiae cells 78% after an incubation time of 30 min, and opposite result was obtained for C. albicans. Experiments demonstrate that the fraction 1 and 3 were toxic and induced changes in the membranes of all yeast strains, leading to their permeabilization. © 2013 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 102: 30–39, 2014.
