Lectins plant toxins

Ricin toxin, found in the bean of the castor plant, Ricinis communis, is one of the most toxic and easily produced plant toxins. It is a lectin consisting of two polypeptide chains, the A-chain and the B-chain, linked by a disulfide bond. It is one of a group of dichain ribosome-inactivating proteins, which are specific for the depurination of a single adenosine in ribosomal ribonucleic acid (RNA).1 The active chain (ie, the A-chain) has the ability to modify catalytically the 28S subunit of... 

Crude chloroform-methanol-water (30 60 8, v/v) extracts of immunostainedTLC bands were analyzed without further purification by nanoelectrospray low-energy mass spectrometry. The authors showed that this effective PLC/MS-joined procedure offers a wide range of applications for any carbohydrate-binding agents such as bacterial toxins, plant lectins, and others. Phenyl-boronic acid (PBA) immobilized on stationary support phases can be put to similar applications. This technology, named boronate affinity chromatography (BAC), consists of a chemical reaction of 1,2- and 1,3-diols with the bonded-phase PBA to form a stable... 

Similarly to animal glycoproteins, plant glycoproteins having different roles have been isolated and studied enzymes, lectins, toxins, and storage... 

A group of plant lectins, such as abrin, ricin, and mod-eccin, are highly toxic to eukaryotic cells. Their mode of action consists of inhibition of protein synthesis by enzymatically inactivating the EF-2 binding region of the 60S ribosomal subunit, whereas the diphtheria toxin inactivates the EF-2 protein itself. Ricin is isolated from castor beans and has a molecular weight of 66,000. Like most plant and bacterial toxic proteins, ricin contains two... 

The 93- to 95-residue neurophysins act as carriers for vasopressin and ocytocin, forming specific complexes with them. Neurophysins contain 14 cysteine residues, which form seven disulfide bonds. There is a striking similarity in sequence between the neurophysins, snake venom toxins, a wheat germ lectin (agglutinin), a ragweed pollen allergen, and a small plant protein called hevein. On the basis of the alignment of cysteine residues, Drenth proposed that all of these proteins have a disulfide-linked core whose structure is shown in Fig. 30-16. 

In the late 1800s, Stillmark4 discovered that the beans of the castor plant contained a toxic protein, which he named ricin. He discovered that ricin caused agglutination of erythrocytes and precipitation of serum proteins. (The lectin properties of ricin and abrin [a closely related toxin from the bean of Abrus precatorius] and their use as tools for research were described in 1972 by Sharon and Lis.5)... 

Ricin is a 66-kilodalton (kd) globular protein that makes up 1% to 5% by weight of the bean of the castor plant, Ricinis communis. The toxic heterodimer consists of a 32-kd A-chain that is disulfide-bonded to a 32-kd B-chain.21 The toxin is stored in the matrix of the castor bean, together with a 120,000-d ricinus lectin.22 Both chains are glycoproteins containing mannose carbohydrate groups the two 32-kd chains must be associated for toxicity. 

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