Canatoxin is a toxic protein isolated from the jackbean, Canavalia ensiformis. The toxin injected intraperitoneally is lethal for mice and rats; however, it is inactive if given orally. In this study, Manduca sexta (L.) (Lepidoptera), Schistocerca americana (Drury) (Orthoptera), Drosophila melanogaster (L.) (Diptera), Aedes aegypti (L.) (Diptera), Rhodnius prolixus (Stål) (Hemiptera), and Callosobruchus maculatus (F.) (Coleoptera) were fed on canatoxin-containing diets. No effects were seen in M. sexta, S. americana, D. melanogaster, or A. aegypti. No traces of canatoxin were found in their feces, suggesting that the protein was digested completely by these insects, which characteristically have a trypsin-based digestion. In contrast, canatoxin was lethal for insects displaying cathepsin-based digestion. Thus, for C. maculatus, a diet containing 0.25% wt:wt canatoxin caused complete inhibition of larval growth. When R. prolixus were fed on canatoxin, 2 effects were seen: impairment of water excretion and increased lethality 48-96 h after feeding. The lethal effect of canatoxin in R. prolixus was blocked partially or completely when the digestion of the toxin by R. prolixus midgut enzymes was impaired. The data showed that canatoxin is highly toxic when ingested by some species of insects but not affecting others, probably in correlation with the characteristics of the digestive process of the insect.
Download full-text PDF |
Source |
---|---|
http://dx.doi.org/10.1093/jee/90.2.340 | DOI Listing |
Toxins (Basel)
May 2023
Department of Agricultural Sciences, University of Naples Federico II, 80055 Portici, Italy.
Plants evolve to synthesize various natural metabolites to protect themselves against threats, such as insects, predators, microorganisms, and environmental conditions (such as temperature, pH, humidity, salt, and drought). Plant-derived toxic proteins are often secondary metabolites generated by plants. These proteins, including ribosome-inactivating proteins, lectins, protease inhibitors, α-amylase inhibitors, canatoxin-like proteins and ureases, arcelins, antimicrobial peptides, and pore-forming toxins, are found in different plant parts, such as the roots, tubers, stems, fruits, buds, and foliage.
View Article and Find Full Text PDFJ Biomol Struct Dyn
December 2023
Brain Institute-Instituto do Cérebro do Rio Grande do Sul (INSCER), Porto Alegre, RS, Brazil.
Ureases catalyze the hydrolysis of urea into carbamate and ammonia. Well-conserved proteins, most plant ureases are hexamers of a single chain subunit, like the most abundant isoform of the jack bean () urease (JBU). Canatoxin (CNTX) was originally isolated from these seeds as a neurotoxic protein, and later characterized as an isoform of JBU with lower molecular mass and enzyme activity.
View Article and Find Full Text PDFToxicology
April 2021
Laboratory of Neurotoxins, Brain Institute of Rio Grande do Sul (BraIns), Pontifícia Universidade Católica do Rio Grande do Sul, Porto Alegre, RS, Brazil; Graduate Program in Medicine and Health Sciences, School of Medicine, Pontifícia Universidade Católica do Rio Grande do Sul, Porto Alegre, RS, Brazil; Scholl of Medicine, Pontificía Universidade Católica do Rio Grande do Sul, Porto Alegre, RS, Brazil. Electronic address:
Ureases are microbial virulence factors either because of the enzymatic release of ammonia or due to many other non-enzymatic effects. Here we studied two neurotoxic urease isoforms, Canatoxin (CNTX) and Jack Bean Urease (JBU), produced by the plant Canavalia ensiformis, whose mechanisms of action remain elusive. The neurotoxins provoke convulsions in rodents (LD ∼2 mg/kg) and stimulate exocytosis in cell models, affecting intracellular calcium levels.
View Article and Find Full Text PDFJ Venom Res
September 2020
Centro Interdisciplinar de Pesquisa em Biotecnologia (CIPBiotec), Universidade Federal do Pampa (UNIPAMPA), Avenida Antônio Trilha 1847, Campus São Gabriel, São Gabriel 97300-000, RS, Brazil.
Ureases are metalloenzymes that hydrolyze urea to ammonia and carbamate. The main urease isoforms present in the seeds of (jack bean urease - JBU and canatoxin) exert a variety of biological activities. The insecticidal activity of JBU is mediated, at least in part, by jaburetox (Jbtx), a recombinant peptide derived from the JBU amino acid sequence.
View Article and Find Full Text PDFColloids Surf B Biointerfaces
September 2016
Graduate Program in Chemistry, Institute of Chemistry, Universidade Federal do Rio Grande do Sul, Porto Alegre, RS, Brazil. Electronic address:
Ureases are metalloenzymes that catalyze the hydrolysis of urea to ammonia and carbon dioxide. Jack bean (Canavalia ensiformis) produces three isoforms of urease (Canatoxin, JBU and JBURE-II). Canatoxin and JBU display several biological properties independent of their ureolytic activity, such as neurotoxicity, exocytosis-inducing and pro-inflammatory effects, blood platelets activation, insecticidal and antifungal activities.
View Article and Find Full Text PDFEnter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!