Crystal structures of cholera toxin in complex with fucosylated receptors point to importance of secondary binding site.

ABSTRACT: Cholera is a life-threatening diarrhoeal disease caused by the human pathogen Vibrio cholerae. Infection occurs after ingestion of the bacteria, which colonize the human small intestine and secrete their major virulence factor - the cholera toxin (CT). The GM1 ganglioside is considered the primary receptor of the CT, but recent studies suggest that also fucosylated receptors such as histo-blood group antigens are important for cellular uptake and toxicity. Recently, a special focus has been on the histo-blood group antigen Lewis^x (Le^x), however, where and how the CT binds to Le^x remains unclear. Here we report the high-resolution crystal structure (1.5 Å) of the receptor-binding B-subunits of the CT bound to the Le^x trisaccharide, and complementa

SUBMITTER: Heim JB 

PROVIDER: S-EPMC6706398 | biostudies-literature | 2019 Aug

REPOSITORIES: biostudies-literature