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Glycobiology, 2002, Vol. 12, No. 5 319-327
© 2002 Oxford University Press

Lactobacillus helveticus glycosyltransferases: from genes to carbohydrate synthesis

Laure Jolly, John Newell, Ida Porcelli, Sébastien J.F. Vincent1 and Francesca Stingele2

Nestlé Research Center, Vers-chez-les-Blanc, CH-1000 Lausanne 26, Switzerland

Bioactive carbohydrates are crucial in mediating essential biological processes, and their biosynthesis is an essential aspect to develop for a global view of their biological functions. Lactic acid bacteria display an array of diverse and complex carbohydrates and, therefore, are of particular interest. Here we present the identification of a novel exocellular polysaccharide structure and the corresponding gene cluster from Lactobacillus helveticus NCC2745. The development of a glycosyltransferase-specific enzymatic assay allowed the assignment of sugar specificities, which as a general approach will for the future permit a faster and more direct characterization of glycosyltransferase specificities. A model of the biosynthesis of the repeating unit is proposed. EpsE is a phosphoglucosyltransferase initiating the repeating unit biosynthesis by linking a glucose residue to a membrane-associated lipophilic acceptor. EpsF elongates the carbohydrate chain by forming an {alpha}(1,3)-Glcp linkage onto the first Glcp, whereas EpsG adds a backbone {alpha}(1,6)-Galp onto {alpha}-Glcp and EpsH attaches a {alpha}(1,6)-Glcp branch onto the first glucose residue. Finally, EpsI would add a ß(1,6)-Galp linkage onto {alpha}-Glcp terminating the sidechain and EpsJ would terminate the synthesis of the polysaccharides’ repeating unit by forming a ß(1,3)-Galp linkage onto {alpha}-Galp.

1 To whom correspondence should be addressed

2 Present address: Neurim Pharmaceuticals SA, 18 Rte de Genève, CH-1280 Nyon, Switzerland


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