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Originally published In Press as doi:10.1074/jbc.M006875200 on August 8, 2000

J. Biol. Chem., Vol. 275, Issue 43, 33890-33897, October 27, 2000
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Biosynthesis of the Galactan Component of the Mycobacterial Cell Wall*

Katarína MikusováDagger , Tetsuya Yagi§, Richard Stern, Michael R. McNeil, Gurdyal S. Besra, Dean C. Crick, and Patrick J. Brennan||

From the Department of Microbiology, Colorado State University, Fort Collins, Colorado 80523-1677

The structural core of the cell walls of Mycobacterium spp. consists of peptidoglycan bound by a linker unit (-alpha -L-Rhap-(1right-arrow3)-D-GlcNAc-P-) to a galactofuran, which in turn is attached to arabinofuran and mycolic acids. The sequence of reactions leading to the biogenesis of this complex starts with the formation of the linker unit on a polyprenyl-P to produce polyprenyl-P-P-GlcNAc-Rha (Mikusová, K., Mikus, M., Besra, G. S., Hancock, I., and Brennan, P. J. (1996) J. Biol. Chem. 271, 7820-7828). We now establish that formation of the galactofuran takes place on this intermediate with UDP-Galf as the Galf donor presented in the form of UDP-Galp and UDP-Galp mutase (the glf gene product) and is catalyzed by galactofuranosyl transferases, one of which, the Mycobacterium tuberculosis H37Rv3808c gene product, has been identified. Evidence is also presented for the growth of the arabinofuran on this polyprenyl-P-P-linker unit-galactan intermediate catalyzed by unidentified arabinosyl transferases, with decaprenyl-P-Araf or 5-P-ribosyl-PP as the Araf donor. The product of these steps, the lipid-linked-LU-galactan-arabinan has been partially characterized in terms of its heterogeneity, size, and composition. Biosynthesis of the major components of mycobacterial cell walls is proving to be extremely complex. However, partial definition of arabinogalactan synthesis, the site of action of several major anti-tuberculosis drugs, facilitates the present day thrust for new drugs to counteract multiple drug-resistant tuberculosis.

* This work was supported by NIAID, National Institutes of Health (NIH), Grants AI-18357 and AI-33706 and National Cooperative Drug Discovery Groups for the Treatment of Opportunistic Infections, NIAID, NIH, Grant AI-38087.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger Supported in part by Slovak Grant Agency Grant VEGA 1/4101/97. Present address: Dept. of Biochemistry, Faculty of Natural Sciences, Comenius University, Mlynská dolina CH-1, 842 15 Bratislava, Slovakia.

§ Supported initially by the Japan Health Sciences Foundation.

Present address: School of Microbiological, Immunological, and Virological Sciences, The Medical School, University of Newcastle upon Tyne, Newcastle upon Tyne NE2 4HH, United Kingdom.

|| To whom correspondence should be addressed. Tel.: 970-491-6700; Fax: 970-491-1815; E-mail: pbrennan@cvmbs.colostate.edu.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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