Investigating bacterial N-linked glycosylation: synthesis and glycosyl acceptor activity of the undecaprenyl pyrophosphate-linked bacillosamine.
The chemical synthesis and biological activity of undecaprenyl pyrophosphate bacillosamine (Und-PP-Bac), an obligatory intermediate in the asparagine-linked glycosylation pathway of Campylobacter jejuni, are reported. The key transformation involves the coupling of bacillosamine phosphate and undecaprenyl phosphate. The synthetic Und-PP-Bac can be used to investigate the activity of the enzyme PglA, which catalyzes the first glycosyl transfer in substrate biosynthesis for N-linked protein glycosylation in the pathogenic gram-negative bacterium. The availability of this synthetic substrate makes it possible to access polyprenyl-linked oligosaccharides, such as the GalNAc-alpha-1,3-bacillosamine-alpha-1-PP-Und intermediate, that will enable exploration of the remaining enzymes in the prokaryotic glycosylation pathway. Study of the bacterial glycosylation system will provide insight into the corresponding eukaryotic process, which is currently poorly understood.
Weerapana
Eranthie
E
Department of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA.
Glover
Kerney Jebrell
KJ
Chen
Mark M
MM
Imperiali
Barbara
B
D016123:Campylobacter jejuni; D002236:Carbohydrate Conformation; D002240:Carbohydrate Sequence; D006031:Glycosylation; D016695:Glycosyltransferases / Q000737:chemistry; D006595:Hexosamines / Q000138:chemical synthesis* / Q000737:chemistry*; D006868:Hydrolysis; D008969:Molecular Sequence Data; D011106:Polyisoprenyl Phosphates / Q000737:chemistry*
D006595:Hexosamines; D011106:Polyisoprenyl Phosphates; C088139:undecaprenyl pyrophosphate; C013920:4-deoxyneosamine C; D016695:Glycosyltransferases