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Glycobiology Advance Access originally published online on August 4, 2006
Glycobiology 2006 16(11):1073-1081; doi:10.1093/glycob/cwl030
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© The Author 2006. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org

Arabinan-deficient mutants of Corynebacterium glutamicum and the consequent flux in decaprenylmonophosphoryl-D-arabinose metabolism

Luke J. Alderwick2, Lynn G. Dover2, Mathias Seidel3, Roland Gande3, Hermann Sahm3, Lothar Eggeling3 and Gurdyal S. Besra1,2

2 School of Biosciences, University of Birmingham, Edgbaston, Birmingham B15 2TT, UK; and 3 Institute for Biotechnologie 1, Research Centre Juelich, D-52425 Juelich, Germany

1 To whom correspondence should be addressed; e-mail: g.besra{at}bham.ac.uk

Received on June 8, 2006; revised on July 26, 2006; accepted on July 26, 2006

The arabinogalactan (AG) of Corynebacterianeae is a critical macromolecule that tethers mycolic acids to peptidoglycan, thus forming a highly impermeable cell wall matrix termed the mycolyl-arabinogalactan peptidoglycan complex (mAGP). The front line anti-tuberculosis drug, ethambutol (Emb), targets the Mycobacterium tuberculosis and Corynebacterium glutamicum arabinofuranosyltransferase Mt-EmbA, Mt-EmbB and Cg-Emb enzymes, respectively, which are responsible for the biosynthesis of the arabinan domain of AG. The substrate utilized by these important glycosyltransferases, decaprenylmonophosphoryl-D-arabinose (DPA), is synthesized via a decaprenylphosphoryl-5-phosphoribose (DPPR) synthase (UbiA), which catalyzes the transfer of 5-phospho-ribofuranose-pyrophosphate (pRpp) to decaprenol phosphate to form DPPR. Glycosyl compositional analysis of cell walls extracted from a C. glutamicum::ubiA mutant revealed a galactan core consisting of alternating ß(1->5)-Galf and ß(1->6)-Galf residues, completely devoid of arabinan and a concomitant loss of cell-wall-bound mycolic acids. In addition, in vitro assays demonstrated a complete loss of arabinofuranosyltransferase activity and DPA biosynthesis in the C. glutamicum::ubiA mutant when supplemented with p[14C]Rpp, the precursor of DPA. Interestingly, in vitro arabinofuranosyltransferase activity was restored in the C. glutamicum::ubiA mutant when supplemented with exogenous DP[14C]A substrate, and C. glutamicum strains deficient in ubiA, emb, and aftA all exhibited different levels of DPA biosynthesis.

Key words: arabinogalactan / Corynebacterium glutamicum / decaprenylmonophosphoryl-D-arabinose / mutants / Mycobacterium tuberculosis


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