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Glycobiology Advance Access published online on December 12, 2007
Glycobiology, doi:10.1093/glycob/cwm134
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© The Author 2007. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org

Communications

Glucuronylation in Escherichia Coli for the Bacterial Synthesis of the Carbohydrate Moiety of Non-Sulfated HNK-1

Elif Yavuza, Sophie Drouillarda, Eric Samaina, Ian Robertsb and Bernard Priema

a Centre de Recherches sur les Macromolécules Végétales, 601 rue de la Chimie, BP 53X 38041 Grenoble, cedex 09 ( France) Fax: (33)476-547-203 E-mail: priem{at}cermav.cnrs.fr
b Faculty of Life Sciences, University of Manchester, Manchester, United Kingdoms

Received on October 31, 2007; accepted on December 4, 2007

We have previously reported the large scale synthesis of neolactotetraose (Galβ-4GlcNAcβ-3Galβ-4Glc) from lactose in engineered Escherichia coli cells (Priem et al. 2002). In the present study we analyzed the adaptation of this system to glucuronylated oligosaccharides. The catalytic domain of mouse glucuronyl transferase GlcAT-P was cloned and expressed in an engineered strain which performed the in vivo synthesis of neolactotetraose. Under these conditions, efficient glucuronylation of neolactotetraose was achieved, but some residual neolactotetraose was still present. Although E. coli K-12 has an indigenous UDP-glucose dehydrogenase, the yield of glucuronylated oligosaccharides was greatly improved by the additional expression of the orthologous gene kfiD from Escherichia coli K5. Glucuronylation of neolactohexaose and lactose was also observed. The final glucuronylated oligosaccharides are precursors of the brain carbohydrate motif HNK-1, involved in neural cell adhesion.

Key words: HNK-1 / glucuronyltransferase / UDP-glucose dehydrogenase / Escherichia coli / metabolic engineering.


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