Modification of the glycolipid-binding specificity of vero cytotoxin by polymyxin B and other cyclic amphipathic peptides
| Autor: | S Head, K Ramotar, C Lingwood |
|---|---|
| Rok vydání: | 1990 |
| Předmět: |
medicine.drug_class
Polymyxin Protein subunit Bacterial Toxins Immunology Receptors Cell Surface In Vitro Techniques Biology Shiga Toxin 1 Microbiology Glycosphingolipids Melittin chemistry.chemical_compound Glycolipid medicine Polymyxins Polymyxin B chemistry.chemical_classification Globosides Trihexosylceramides Glycolipid binding Periplasmic space Melitten Cyclic peptide Infectious Diseases chemistry Biochemistry lipids (amino acids peptides and proteins) Parasitology Chromatography Thin Layer Research Article medicine.drug |
| Zdroj: | Infection and Immunity. 58:1532-1537 |
| ISSN: | 1098-5522 0019-9567 |
| DOI: | 10.1128/iai.58.6.1532-1537.1990 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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