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Glycobiology Advance Access originally published online on August 4, 2009
Glycobiology 2009 19(11):1235-1247; doi:10.1093/glycob/cwp116
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© The Author 2009. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org

AftD, a novel essential arabinofuranosyltransferase from mycobacteria

Henrieta Skovierová2, Gérald Larrouy-Maumus3,4, Jian Zhang2, Devinder Kaur2, Nathalie Barilone5, Jana Korduláková6, Martine Gilleron3,4, Stéphanie Guadagnini7, Martina Belanová6, Marie-Christine Prevost7, Brigitte Gicquel5, Germain Puzo3,4, Delphi Chatterjee2, Patrick J Brennan2, Jérôme Nigou3,4 and Mary Jackson1,2

2 Mycobacteria Research Laboratories, Department of Microbiology, Immunology and Pathology, Colorado State University, Fort Collins, CO 80523-1682, USA
3 CNRS, IPBS (Institut de Pharmacologie et de Biologie Structurale), Département Mécanismes Moléculaires des Infections Mycobactériennes, 205 route de Narbonne
4 Université de Toulouse, UPS, IPBS, F-31077 Toulouse
5 Unité de Génétique Mycobactérienne, Institut Pasteur, 25 rue du Docteur Roux, 75724 Paris Cedex 15, France
6 Department of Biochemistry, Faculty of Natural Sciences, Comenius University, Mlynska dolina CH-1, 84215 Bratislava, Slovak Republic
7 Plate-Forme de Microscopie Ultrastructurale, Institut Pasteur, 25 rue du Docteur Roux, 75724 Paris Cedex 15, France

1 To whom correspondence should be addressed: Tel: +1-970-491-3582; Fax: +1-970-491-1815; e-mail: Mary.Jackson{at}colostate.edu

Received on June 30, 2009; revised on July 23, 2009; accepted on July 26, 2009

Arabinogalactan (AG) and lipoarabinomannan (LAM) are the two major cell wall (lipo)polysaccharides of mycobacteria. They share arabinan chains made of linear segments of {alpha}-1,5-linked D-Araf residues with some {alpha}-1,3-branching, the biosynthesis of which offers opportunities for new chemotherapeutics. In search of the missing arabinofuranosyltransferases (AraTs) responsible for the formation of the arabinan domains of AG and LAM in Mycobacterium tuberculosis, we identified Rv0236c (AftD) as a putative membrane-associated polyprenyl-dependent glycosyltransferase. AftD is 1400 amino acid-long, making it the largest predicted glycosyltransferase of its class in the M. tuberculosis genome. Assays using cell-free extracts from recombinant Mycobacterium smegmatis and Corynebacterium glutamicum strains expressing different levels of aftD indicated that this gene encodes a functional AraT with {alpha}-1,3-branching activity on linear {alpha}-1,5-linked neoglycolipid acceptors in vitro. The disruption of aftD in M. smegmatis resulted in cell death and a decrease in its activity caused defects in cell division, reduced growth, alteration of colonial morphology, and accumulation of trehalose dimycolates in the cell envelope. Overexpression of aftD in M. smegmatis, in contrast, induced the accumulation of two arabinosylated compounds with carbohydrate backbones reminiscent of that of LAM and a degree of arabinosylation dependent on aftD expression levels. Altogether, our results thus indicate that AftD is an essential AraT involved in the synthesis of the arabinan domain of major mycobacterial cell envelope (lipo)polysaccharides.

Key words: arabinogalactan / arabinosyltransferase / lipoarabinomannan / Mycobacterium / tuberculosis


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