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Selected Publication:

Type of publication: Journal Article
Type of document: Full Paper

Year: 1997


Title: The role of structural domains in RIP II toxin model membrane binding.

Source: FEBS Lett (402), 1 91-93.

Authors Vetmeduni Vienna:

Pohl Elena

The interaction of plant toxin ricin and MLI binding subunits to liposomes containing monosialoganglioside (GM1), bearing a terminal galactose residue, has been examined as a possible receptor model, For the first time we demonstrate that ricin B-chain but not ricin provokes liposome aggregation at 10 M% GM1 concentration, whereas in the presence of either ricin A-chain or galactose the aggregation is inhibited, The B-subunit of plant toxin MLI from Viscum album has similar lectin specificity and activity but cannot aggregate GM1 liposomes, The ability of the B-chain to aggregate liposomes adds a new crucial step in the toxin transmembrane penetration mechanism, We demonstrate here possible ricin B-chain interactions with membranes proceeding via two sites, namely (a) a galactose-binding domain and (b) a hydrophobic interchain domain, In close contact with two phospholipid bilayers, ricin B-chain may determine the geometry of the fusion site, These events can provoke A-chain translocation which follows membrane fusion.

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