P-42 グラム陰性菌Campylobacter jejuni由来N-結合型糖タンパク質糖鎖の立体選択的合成研究(ポスター発表の部)

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The N-linked glycan is the most conserved among eukaryotic glycoprotein glycans. Contrary to previous belief, certain prokaryotes are able to produce glycosylated proteins. A major non-flagellin antigenic glycoprotein designated PEB3 or Cj0289c has recently been identified in the pathogenic Gram-negative bacterium Campylobacter jejuni [1]. This glycoprotein has multiple glycosylation sites with novel glycans at Asn residues in the consensus sequence Asn-Xaa-Thr/Ser [2], as is the case in the eukaryotes. However, the novel N-glycan is composed of GalNAc-α(1,4)-GalNAc-α(1,4)-[Glc-β(1,3)-]GalNAc-α(1,4)-GalNAc-α(1,4)-GalNAc-α(1,3)-Bac-β(1), where Bac is bacillosamine (2,4-diacetamido-2,4,6-trideoxyglucopyranose). This N-linked glycan structure is distinct from eukaryotic glycoprotein glycans. The presence of this glycan on the surface of C. jejuni was shown to play a key role in enteric adhesion to host cells, and this adhesion constitutes the first step of virulence. A relationship between C. jejuni infection and Guillian Barr syndrome (GBS) has since been reported. Here, we report synthetic studies on a novel N-linked glycan from C. jejuni (Figure 1), including 1) development of our PFP strategy using pentafluoropropanoyl ester [3] for the stereoselective synthesis of GalNAc-α(1,4)-GalNAc repeating motifs [4], 2) its application to construction of a branched hexasaccharide Glc_1GalNAc_5 A [4], 3) syntheses of Bac [5] and 4) its transformation to N-asparagine-linked Bac B [5] using our methodology for the efficient formation of N-glycosidic linkage to Asn [6].
2006-09-15

P-42 グラム陰性菌Campylobacter jejuni由来N-結合型糖タンパク質糖鎖の立体選択的合成研究(ポスター発表の部)

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