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Ricin A chain–B chain disulfide bond
- Molecular classification
- Other (disulfide linkage between protein subunits)
01
Overview
The **ricin A chain–B chain disulfide bond** is a single covalent linkage that joins the enzymatically active A chain (RTA) to the cell-binding B chain (RTB) of the heterodimeric plant toxin ricin[4][5]. Upon cellular uptake, reduction of this disulfide bond in the endoplasmic reticulum is a critical step that releases the A chain into the cytosol[3][4][5]. The free A chain then catalyzes the depurination of a specific adenine residue in the 28S rRNA of eukaryotic ribosomes, halting protein synthesis and leading to cell death[1][3][4]. The disulfide bond itself is not a therapeutic target, but its cleavage is essential for ricin's mechanism of action; thus, the term "ricin disulfide bond cleavage" refers to a step in ricin toxicity and not an independent receptor, enzyme, or molecular target.
- Other names
- Ricin interchain disulfideRicin A-B chain disulfide bond
02
Mechanism of action
Disulfide bond reduction releases the enzymatic A chain to enter the cytosol and inhibit protein synthesis[3][4][5].
03
Biological functions
Enables activation of ricin cytotoxicity via A chain release
04
Disease associations
Infection (as a biological warfare agent)Other (cell death due to ricin exposure)
05
Safety considerations
Extreme toxicity of ricin following cell entry and A chain activation[1][3][4]
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