5g3l

Publication Abstract from PubMed

The structurally related AB5-type heat-labile enterotoxins of Escherichia coli and Vibrio cholerae are classified into two major types. The type I group includes cholera toxin and E. coli LT-I, while the type II subfamily comprises LT-IIa, LT-IIb and LT-IIc. The carbohydrate binding specificities of LT-IIa, LT-IIb and LT-IIc are distinctive from those of cholera toxin and E. coli LT-I. While CT and LT-I bind primarily to the GM1 ganglioside, LT-IIa binds to gangliosides GD1a, GD1b, and GM1, LT-IIb binds to the GD1a and GT1b gangliosides, and LT-IIc binds to GM1, GM2, GM3 and GD1a. These previous studies of the binding properties of type II B-subunits have been focused on ganglio core chain gangliosides. To further define the carbohydrate binding specificity of LT-IIb B-subunits, we have herein investigated its binding to a collection of gangliosides and non-acid glycosphingolipids with different core chains. A high affinity binding of LT-IIb B-subunits to gangliosides with neolacto core chain, as e.g Neu5Gcalpha3- and Neu5Acalpha3-neolactohexaosylceramide, and Neu5Gcalpha3- and Neu5Acalpha3-neolactooctaosylceramide was detected. An LT-IIb binding ganglioside was isolated from human small intestine and characterized as Neu5Acalpha3-neolactohexaosylceramide. The crystal structure of B-subunit of LT-IIb with the pentasaccharide moiety of Neu5Acalpha3-neolactotetraosylceramide (Neu5Ac-nLT: Neu5Acalpha3Galbeta4GlcNAcbeta3Galbeta4Glc) was determined providing the first information for sialic binding site in this sub-family, with clear differences with the one from CT and LT-I.

Biochemical and structural characterization of the novel sialic acid-binding site of Escherichia coli heat-labile enterotoxin LT-IIb.,Zalem D, Ribeiro JP, Varrot A, Lebens M, Imberty A, Teneberg S Biochem J. 2016 Aug 25. pii: BCJ20160575. PMID:27562297^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.