{"entity": "publication", "iuid": "c3946fe3e96345d4879afb8cce47d2b4", "timestamp": "2026-08-10T23:04:50.648Z", "links": {"self": {"href": "https://publications.scilifelab.se/publication/c3946fe3e96345d4879afb8cce47d2b4.json"}, "display": {"href": "https://publications.scilifelab.se/publication/c3946fe3e96345d4879afb8cce47d2b4"}}, "title": "Characterization of the ganglioside recognition profile of Escherichia coli heat-labile enterotoxin LT-IIc.", "authors": [{"family": "Zalem", "given": "Dani", "initials": "D"}, {"family": "Juh\u00e1s", "given": "Martin", "initials": "M"}, {"family": "Terrinoni", "given": "Manuela", "initials": "M"}, {"family": "King-Lyons", "given": "Natalie", "initials": "N"}, {"family": "Lebens", "given": "Michael", "initials": "M"}, {"family": "Varrot", "given": "Annabelle", "initials": "A"}, {"family": "Connell", "given": "Terry D", "initials": "TD"}, {"family": "Teneberg", "given": "Susann", "initials": "S", "orcid": "0000-0003-1957-9553", "researcher": {"href": "https://publications.scilifelab.se/researcher/76e79099e3fe4398a6b030896efb7308.json"}}], "type": "journal article", "published": "2022-04-21", "journal": {"title": "Glycobiology", "issn": "1460-2423", "volume": "32", "issue": "5", "pages": "391-403", "issn-l": "0959-6658"}, "abstract": "The heat-labile enterotoxins of Escherichia coli and cholera toxin of Vibrio cholerae are related in structure and function. Each of these oligomeric toxins is comprised of one A polypeptide and five B polypeptides. The B-subunits bind to gangliosides, which are followed by uptake into the intoxicated cell and activation of the host's adenylate cyclase by the A-subunits. There are two antigenically distinct groups of these toxins. Group I includes cholera toxin and type I heat-labile enterotoxin of E. coli; group II contains the type II heat-labile enterotoxins of E. coli. Three variants of type II toxins, designated LT-IIa, LT-IIb and LT-IIc have been described. Earlier studies revealed the crystalline structure of LT-IIb. Herein the carbohydrate binding specificity of LT-IIc B-subunits was investigated by glycosphingolipid binding studies on thin-layer chromatograms and in microtiter wells. Binding studies using a large variety of glycosphingolipids showed that LT-IIc binds with high affinity to gangliosides with a terminal Neu5Ac\u03b13Gal or Neu5Gc\u03b13Gal, e.g. the gangliosides GM3, GD1a and Neu5Ac\u03b13-/Neu5Gc\u03b13--neolactotetraosylceramide and Neu5Ac\u03b13-/Neu5Gc\u03b13-neolactohexaosylceramide. The crystal structure of LT-IIc B-subunits alone and with bound LSTd/sialyl-lacto-N-neotetraose d pentasaccharide uncovered the molecular basis of the ganglioside recognition. These studies revealed common and unique functional structures of the type II family of heat-labile enterotoxins.", "doi": "10.1093/glycob/cwab133", "pmid": "34972864", "labels": {"Glycoproteomics and MS Proteomics": "Service"}, "xrefs": [{"db": "pmc", "key": "PMC9022906"}, {"db": "pii", "key": "6482028"}], "notes": [], "created": "2022-11-30T12:04:15.224Z", "modified": "2024-01-16T13:46:29.258Z"}