Enterolobin induces rat paw oedema independently of PAF-acether

Hc, Castro-Faria-Neto; Rs, Cordeiro; Martins, Marcos A. P.; Ac, Correia-Da-Silva; Pt, Bozza; Mv, Sousa; Morhy, Lauro

doi:10.1590/s0074-02761991000600029

Cited by 7 publications

(2 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In vitro proteolysis studies showed that Entrolobin is resistant to the digestion by larval gut enzymes of C. maculatus (Sousa et al, 1993). Enterolobin also induces inflammation upon injection in rats (Castro Faria Neto et al, 1991). Similar to other poreforming toxins, the oligomerization of enterolobin is promoted by low pH and high ionic strength (Fontes et al, 1997).…”

Section: Pore-forming Toxinsmentioning

confidence: 99%

Toxic proteins in plants

2015

View full text Add to dashboard Cite

Plants have evolved to synthesize a variety of noxious compounds to cope with unfavorable circumstances, among which a large group of toxic proteins that play a critical role in plant defense against predators and microbes. Up to now, a wide range of harmful proteins have been discovered in different plants, including lectins, ribosome-inactivating proteins, protease inhibitors, ureases, arcelins, antimicrobial peptides and pore-forming toxins. To fulfill their role in plant defense, these proteins exhibit various degrees of toxicity towards animals, insects, bacteria or fungi. Numerous studies have been carried out to investigate the toxic effects and mode of action of these plant proteins in order to explore their possible applications. Indeed, because of their biological activities, toxic plant proteins are also considered as potentially useful tools in crop protection and in biomedical applications, such as cancer treatment. Genes encoding toxic plant proteins have been introduced into crop genomes using genetic engineering technology in order to increase the plant's resistance against pathogens and diseases. Despite the availability of ample information on toxic plant proteins, very few publications have attempted to summarize the research progress made during the last decades. This review focuses on the diversity of toxic plant proteins in view of their toxicity as well as their mode of action. Furthermore, an outlook towards the biological role(s) of these proteins and their potential applications is discussed.

show abstract

Section: Pore-forming Toxinsmentioning

confidence: 99%

Toxic proteins in plants

2015

View full text Add to dashboard Cite

show abstract

“…Enterolobin was first purified by Sousa et al in 1989 [102]. Since enterolobin harbours insecticidal activities against larvae of the brucid Calosobruchus macullatus [102], and causes inflammation upon injection in rats [104], it may serve as a defence against potential herbivores. Three known outbreaks of intoxication have also been caused by E. contortisiliquum pods [105] consumed by cattle, leading to anorexia, depression, photosensitization, and abortion.…”

Section: Enterolobin From Seeds Of Enterolobium Contortisiliquum (Eukmentioning

confidence: 99%

Staphylococcal and Streptococcal Superantigens: Basic Biology of Conserved Protein Toxins

Larkin¹

2013

TOTNJ

View full text Add to dashboard Cite

Pore-forming toxins (PFTs) represent the largest known group of bacterial protein toxins to date. Membrane insertion and subsequent pore-formation occurs after initial binding to cell-surface receptor and oligomerization. Aerolysin, a toxin produced by the Gram-negative bacterium Aeromonas hydrophila and related species, belongs to the PFT group and shares a common mechanism of action involving -barrel structures resulting from the assembly ofhairpins from individual toxin monomers into a heptamer. Aerolysin is also the name given to structurally and mechanistically related toxins called the aerolysin-like toxin family. A universal characteristic of this toxin family involves the diverse life forms that synthesize these proteins throughout Nature. Examples include: 1) epsilon-toxin and septicum-alpha-toxin produced by anaerobic, Gram-positive Clostridium species; 2) enterolobin by the Brazilian tree Enterolobium contortisiliquum; 3) a mushroom toxin Laetiporus sulphureus lectin (LSL); 4) mosquitocidal toxins (Mtxs) from the Gram-positive bacteria Bacillus sphaericus and parasporine-2 from Bacillus thuringiensis; and 6) hydralysins from the tiny aquatic animal Chlorohydra viridis. The following review provides an overview of the different members within the aerolysin-like toxin family.

show abstract