The plant toxin ricin is transported retrogradely from the cell surface to the endoplasmic reticulum (ER) from where the enzymatically active part is retrotranslocated to the cytosol, presumably by the same mechanism as used by misfolded proteins. The ER degradation enhancing alpha-mannosidase I-like protein, EDEM, is responsible for directing aberrant proteins for ER-associated protein degrada...

Historically veterinarians have diagnosed accidental poisonings and identified possible terrorist events before they have come to the attention of public health authorities. There are many toxins that pose a threat to both humans and animals and the authors examine several of them here, namely, anthrax, tricothecenes, staphylococcal enterotoxin B, botulinum toxins, ricin, saxitoxin and dinoflag...

Abrin, ricin, viscumin, modeccin, and volkensin are very potent toxins derived from plants. They are glycoproteins composed of two polypeptide chains linked by a disulphide bridge. The A-chain is the enzymatic toxic moiety and B-chain is responsible for bonding to the target cell and internalization of toxin. The toxic part of the toxin molecule removes an adenine from a specific adenosine resi...

Ribosome-inactivating proteins (RIPs) are plant toxins that irreversibly damage ribosomes and other substrates, thus causing cell death. RIPs classified in type 1 RIPs, single-chain enzymatic proteins, 2 consisting of active A chains, similar to linked lectin B which enable the rapid internalization toxin into cell. For this reason, many very cytotoxic, ricin, volkensin stenodactylin being most...

Ricin is a type 2 ribosome-inactivating protein (RIP), containing a catalytic A chain and a lectin-like B chain. It inhibits protein synthesis by depurinating the N-glycosidic bond at α-sarcin/ricin loop (SRL) of the 28S rRNA, which thereby prevents the binding of elongation factors to the GTPase activation center of the ribosome. Here, we present the 1.6 Å crystal structure of Ricin A chain (R...

The plant toxin ricin is a lectin that binds to D-galactose or lactose moieties by multivalent interactions. In the present work, this avidity was used to develop a novel sandwich glyco-immunoassay using a carbohydrate microarray. For realization, 6-azidohexyl-lactose was immobilized on an alkyne silane surface by Cu(I) catalyzed click chemistry. This procedure is fast, and prevents any nonspec...

The fate of tetanus toxin (mol wt 150,000) subsequent to its retrograde axonal transport in peripheral sympathetic neurons of the rat was studied by both electron microscope autoradiography and cytochemistry using toxin-horseradish peroxidase (HRP) coupling products, and compared to that of nerve growth factor (NGF), cholera toxin, and the lectins wheat germ agglutinin (WGA), phytohaemagglutini...

Ricin toxin has been regarded as one of the most potent poisons in the plant kingdom, and there is no effective therapeutic countermeasure or licensed vaccine against it. Consequently, early detection of ricin intoxication is necessary. In this study, we took mice as test subjects, and used the technique of Matrix-assisted laser desorption/ionization time of flight mass spectrometry (MALDI-TOF/...

Plant and microbial toxins are considered bioterrorism threat agents because of their extreme toxicity and/or ease of availability. Additionally, some of these toxins are increasingly responsible for accidental food poisonings. The current study utilized an ELISA-based protein antibody microarray for the multiplexed detection of ten biothreat toxins, botulinum neurotoxins (BoNT) A, B, C, D, E, ...

Ricin is one of the most known toxic materials of plant origin. The 2007 Guinness World Records Book considers ricin the world's most potent plant toxin. It also possesses wide-ranging biological effects on higher organisms and it is a powerful inhibitor of cellular protein synthesis. Ricin is frequently therapeutically used in the construction of immunotoxins designed to kill specific target c...