Work

Tumor marker disaccharide D‐Gal‐β1,3‐GalNAc complexed to heat‐labile enterotoxin from Escherichia coli

Year: 1996

Type: article

Abstract: Heat-labile enterotoxin (LT) is part of the cholera toxin (CT) family and consists of a catalytic A subunit and a B pentamer that serves to recognize the oligosaccharide part of the GM1 ganglioside receptor. We report here the crystal structure of heat-labile enterotoxin in complex with the disaccharide portion of the Thomsen-Friedenreich (T-antigen) tumor marker. The toxin:carbohydrate complex is determined to 2.13 A resolution, yielding an R-factor of 18.5%. The T-antigen disaccharide, D-Gal-beta 1,3-GalNAc-Ser/Thr, is present in more than 85% of human carcinomas and monitoring its autoimmune response is used for the early detection of tumors. Insight into the molecular recognition of this tumor antigen by sugar binding proteins can benefit the development of a diagnostic tool for human carcinomas as well as a T-antigen directed anticancer drug delivery system.

Source: Protein Science

DOI: 10.1002/pro.5560050621

Authors: Focco Van Den Akker, Elles Steensma, Wim G. J. Hol

Institutions: University of Washington, University of Groningen, Wageningen University & Research, Howard Hughes Medical Institute

Language: English

Topic: Glycosylation and Glycoproteins Research

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

SDG: Good health and well-being

Open Access status: green

Funder: National Institute of Allergy and Infectious Diseases