Synthetic mannosides act as acceptors for mycobacterial α1-6 mannosyltransferase

J.R. Brown, R.A. Field, A. Barker, M. Guy, R. Grewal, K.-H. Khoo, P.J. Brennan, G.S. Besra, D. Chatterjee

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A series of synthetic mannosides was screened in a cell-free system for their ability to act as acceptor substrates for mycobacterial mannosyltransferases. Evaluation of these compounds demonstrated the incorporation of [14C]Man from GDP-[14C]Man into a radiolabeled organic-soluble fraction and analysis by thin layer chromatography and autoradiography revealed the formation of two radiolabeled products. Each synthetic acceptor was capable of accepting one or two mannose residues, resulting in a major and a minor mannosylated product. Both products from each acceptor were isolated and their mass was confirmed by fast-atom bombardment–mass spectrometry (FABMS). Characterization of each mannosylated product by exo-glycosidase digestion, acetolysis and linkage analysis by gas chromatography–mass spectrometry of partially per-O-methylated alditols, revealed only α1-6-linked products. In addition, the antibiotic amphomycin selectively inhibited the formation of mannosylated products suggesting polyprenolmonophosphate-mannose (C35/50-P-Man) was the immediate mannose donor in all mannosylation reactions observed. The ability of synthetic disaccharides to act as acceptor substrates in this system, is most likely due to the action of a mycobacterial polyprenol-P-Man:mannan α1-6 mannosyltransferase involved in the biosynthesis of linear α1-6-linked lipomannan.

Manα1-6Manα1-O-decenyl and analogues thereof serve as substrates for M. smegmatis α1,6-mannosyltransferase involved in mycobacterial cell wall biosynthesis.

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Original languageUndefined
Pages (from-to)815-824
Number of pages10
JournalBioorganic and Medicinal Chemistry
Issue number4
Publication statusPublished - 25 Apr 2001

Research Beacons, Institutes and Platforms

  • Manchester Institute of Biotechnology

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