melitten and globotriaosylceramide

melitten has been researched along with globotriaosylceramide* in 1 studies

Other Studies

1 other study(ies) available for melitten and globotriaosylceramide

Article	Year
Modification of the glycolipid-binding specificity of vero cytotoxin by polymyxin B and other cyclic amphipathic peptides. Infection and immunity, 1990, Volume: 58, Issue:6 Polymyxin B, an amphipathic cyclic decapeptide produced by Bacillus polymyxa, is routinely used in the extraction of the components from the periplasmic space of gram-negative bacteria. Vero cytotoxin 1 (VT1) is an Escherichia coli-elaborated subunit toxin which binds to the glycolipid globotriosylceramide (Gal-alpha 1-4-Gal beta 1-4-Glc-ceramide [Gb3]) and has been strongly implicated in the etiology of the hemolytic uremic syndrome and hemorrhagic colitis. We now show by in vitro glycolipid-binding assays that in the presence of low concentrations of polymyxin B, globotetraosylceramide (GalNAc beta 1-3Gal alpha 1-4Gal beta 1-4Glc-ceramide [Gb4]) is also recognized by both the VT1 B (binding) subunit and holotoxin. Melittin, a 26-amino-acid cyclic peptide of similar amphipathic nature, produced the same effect, whereas a hydrophobic blocking agent did not. Triton X-100 did not increase binding of VT1 to Gb4 but prevented glycolipid binding in toto at concentrations above 0.5%. Caution is therefore advised in the analysis of VT1 glycolipid binding in the presence of amphipathic peptides. Topics: Bacterial Toxins; Chromatography, Thin Layer; Globosides; Glycosphingolipids; In Vitro Techniques; Melitten; Polymyxin B; Polymyxins; Receptors, Cell Surface; Shiga Toxin 1; Trihexosylceramides	1990

Article

Year

Modification of the glycolipid-binding specificity of vero cytotoxin by polymyxin B and other cyclic amphipathic peptides.

Infection and immunity, 1990, Volume: 58, Issue:6

Polymyxin B, an amphipathic cyclic decapeptide produced by Bacillus polymyxa, is routinely used in the extraction of the components from the periplasmic space of gram-negative bacteria. Vero cytotoxin 1 (VT1) is an Escherichia coli-elaborated subunit toxin which binds to the glycolipid globotriosylceramide (Gal-alpha 1-4-Gal beta 1-4-Glc-ceramide [Gb3]) and has been strongly implicated in the etiology of the hemolytic uremic syndrome and hemorrhagic colitis. We now show by in vitro glycolipid-binding assays that in the presence of low concentrations of polymyxin B, globotetraosylceramide (GalNAc beta 1-3Gal alpha 1-4Gal beta 1-4Glc-ceramide [Gb4]) is also recognized by both the VT1 B (binding) subunit and holotoxin. Melittin, a 26-amino-acid cyclic peptide of similar amphipathic nature, produced the same effect, whereas a hydrophobic blocking agent did not. Triton X-100 did not increase binding of VT1 to Gb4 but prevented glycolipid binding in toto at concentrations above 0.5%. Caution is therefore advised in the analysis of VT1 glycolipid binding in the presence of amphipathic peptides.

Topics: Bacterial Toxins; Chromatography, Thin Layer; Globosides; Glycosphingolipids; In Vitro Techniques; Melitten; Polymyxin B; Polymyxins; Receptors, Cell Surface; Shiga Toxin 1; Trihexosylceramides

1990