Special Issue "Plant Toxins and Related Proteins: Pharmacology and Toxicology"

A special issue of Toxins (ISSN 2072-6651). This special issue belongs to the section "Plant Toxins".

Deadline for manuscript submissions: 31 March 2020.

Special Issue Editors

Prof. Dr. Maria Angeles Rojo
E-Mail Website
Guest Editor
Experimental Sciences, University of Europea Miguel de Cervantes, Valladolid, Spain
Interests: Lectins structure and function, Toxicology of lectins and ribosome-inactivating protein (RIPs), Toxicology of RNasas from plants, Interactions of lectins with food and intestinal mucosa, Hematology and parasitology
Prof. Dr. Manuel Garrosa
E-Mail Website
Guest Editor
Department of Cell Biology, Histology and Pharmacology, University of Valladolid, Valladolid, Spain
Interests: Ribosome-inactivating proteins (RIPs), Histotoxicity, Biology of aging, Nerve regeneration

Special Issue Information

Dear Colleagues,

For a long time, we have been interested in improving our knowledge about how plants can defend themselves against viruses, bacteria, fungi, nematodes, and other hazards like environmental changes that surround them. There are several reports in the literature describing plant proteins involved in defense mechanisms, such as lectins, ribosome-inactivating proteins (RIPs), inhibitors of proteolytic enzymes, and glycohydrolases, which have been supposedly developed as an evolutionary mechanism for self-protection. These proteins are substances produced as secondary metabolites, and since their action mechanisms are based on their chemical components, some of them share structural and functional properties.
Natural toxins are present in a wide variety of plants. Some of these plants are commonly consumed as food; therefore, eaten in a certain amount, they can be harmful to human or animal health and lead to disease. The toxicological effects following ingestion of plant toxins may range from acute small alterations (gastroenteritis, arrhythmias, etc.) to severe problems and death. Plant toxins act by altering specific mechanisms involving enzymes, receptors, and even genetic material in particular cells and tissues. Nevertheless, many aspects of their toxicity are still unknown and require particular attention, since their accidental consumption or use as biological weapons are possible. Furthermore, some plant protein toxins and plant toxin-related proteins have been used in targeted experimental therapy, especially for cancer treatment.
Focusing on plant toxins and related proteins, this Special Issue aims to highlight these substances, describe their characteristics and physiological and pathological effects, as well as their applicability in nutrition and medicine. Accordingly, articles that deal with these issues are welcome.

Prof. Dr. Maria Angeles Rojo
Prof. Dr. Manuel Garrosa
Guest Editors

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All papers will be peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a double-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Toxins is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2000 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • Plant toxins,
  • Lectins,
  • Pathology,
  • Recombinant plant toxins,
  • Immunotoxins,
  • Conjugates,
  • Toxicity in vitro and in vivo

Published Papers (3 papers)

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Research

Open AccessArticle
CCD Based Detector for Detection of Abrin Toxin Activity
Toxins 2020, 12(2), 120; https://doi.org/10.3390/toxins12020120 (registering DOI) - 14 Feb 2020
Abstract
Abrin is a highly potent and naturally occurring toxin produced in the seeds of Abrus precatorius (Rosary Pea) and is of concern as a potential bioterrorism weapon. There are many rapid and specific assay methods to detect this toxic plant protein, but few [...] Read more.
Abrin is a highly potent and naturally occurring toxin produced in the seeds of Abrus precatorius (Rosary Pea) and is of concern as a potential bioterrorism weapon. There are many rapid and specific assay methods to detect this toxic plant protein, but few are based on detection of toxin activity, critical to discern biologically active toxin that disables ribosomes and thereby inhibits protein synthesis, producing cytotoxic effects in multiple organ systems, from degraded or inactivated toxin which is not a threat. A simple and low-cost CCD detector system was evaluated with colorimetric and fluorometric cell-based assays for abrin activity; in the first instance measuring the abrin suppression of mitochondrial dehydrogenase in Vero cells by the MTT-formazan method and in the second instance measuring the abrin suppression of green fluorescent protein (GFP) expression in transduced Vero and HeLa cells. The limit of detection using the colorimetric assay was 10 pg/mL which was comparable to the fluorometric assay using HeLa cells. However, with GFP transduced Vero cells a hundred-fold improvement in sensitivity was achieved. Results were comparable to those using a more expensive commercial plate reader. Thermal inactivation of abrin was studied in PBS and in milk using the GFP-Vero cell assay. Inactivation at 100 °C for 5 min in both media was complete only at the lowest concentration studied (0.1 ng/mL) while treatment at 63 °C for 30 min was effective in PBS but not milk. Full article
(This article belongs to the Special Issue Plant Toxins and Related Proteins: Pharmacology and Toxicology)
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Open AccessArticle
Identification of Echinacea Purpurea (L.) Moench Root LysM Lectin with Nephrotoxic Properties
Toxins 2020, 12(2), 88; https://doi.org/10.3390/toxins12020088 - 28 Jan 2020
Abstract
Echinacea purpurea (L.) Moench (EP) is a well-studied plant used for health benefits. Even though there are a lot of data on EP secondary metabolites, its active proteins are not studied well enough. The aim of our experiment was to purify lectin fraction [...] Read more.
Echinacea purpurea (L.) Moench (EP) is a well-studied plant used for health benefits. Even though there are a lot of data on EP secondary metabolites, its active proteins are not studied well enough. The aim of our experiment was to purify lectin fraction from EP roots and evaluate its biological activity in vitro as well as its effect on kidney morphology in vivo. An EP root glycoprotein fraction was purified by affinity chromatography, identified by LC-MS/MS, and used for biological activity tests in vitro and in vivo. Identified glycoproteins were homologous with the LysM domain containing lectins from the Asteraceae plants Helianthus annuus L., Lactuca sativa L., Cynara cardunculus L. A purified fraction was tested by hemagglutination and hemagglutination inhibition (by carbohydrate reactions) in vitro. We purified the hemagglutinating active ~40 kDa size lactose, D-mannose, and D-galactose specific glycoproteins with two peptidoglycan binding LysM (lysine motif) domains. Purified LysM lectin was tested in vivo. Eight-week old Balb/C male mice (n = 15) were treated with 5 μg of the purified lectin. Injections were repeated four times per week. At the fifth experimental week, animals were sedated with carbon dioxide, then euthanized by cervical dislocation and their kidney samples were collected. Morphological changes were evaluated in hematoxylin and eosin stained kidney samples. The purified LysM lectin induced a statistically significant (p < 0.05) kidney glomerular vacuolization and kidney tubular necrosis (p < 0.001). Full article
(This article belongs to the Special Issue Plant Toxins and Related Proteins: Pharmacology and Toxicology)
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Open AccessArticle
LC-HRMS Screening and Identification of Novel Peptide Markers of Ricin Based on Multiple Protease Digestion Strategies
Toxins 2019, 11(7), 393; https://doi.org/10.3390/toxins11070393 - 05 Jul 2019
Cited by 1
Abstract
Both ricin and R. communis agglutinin (RCA120), belonging to the type II ribosome-inactivating proteins (RIPs-Ⅱ), are derived from the seeds of the castor bean plant. They share very similar amino acid sequences, but ricin is much more toxic than RCA120. It is urgently [...] Read more.
Both ricin and R. communis agglutinin (RCA120), belonging to the type II ribosome-inactivating proteins (RIPs-Ⅱ), are derived from the seeds of the castor bean plant. They share very similar amino acid sequences, but ricin is much more toxic than RCA120. It is urgently necessary to distinguish ricin and RCA120 in response to public safety. Currently, mass spectrometric assays are well established for unambiguous identification of ricin by accurate analysis of differentiated amino acid residues after trypsin digestion. However, diagnostic peptides are relatively limited for unambiguous identification of trace ricin, especially in complex matrices. Here, we demonstrate a digestion strategy of multiple proteinases to produce novel peptide markers for unambiguous identification of ricin. Liquid chromatography-high resolution MS (LC-HRMS) was used to verify the resulting peptides, among which only the peptides with uniqueness and good MS response were selected as peptide markers. Seven novel peptide markers were obtained from tandem digestion of trypsin and endoproteinase Glu-C in PBS buffer. From the chymotrypsin digestion under reduction and non-reduction conditions, eight and seven novel peptides were selected respectively. Using pepsin under pH 1~2 and proteinase K digestion, six and five peptides were selected as novel peptide markers. In conclusion, the obtained novel peptides from the established digestion methods can be recommended for the unambiguous identification of ricin during the investigation of illegal use of the toxin. Full article
(This article belongs to the Special Issue Plant Toxins and Related Proteins: Pharmacology and Toxicology)
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