Engineering N-linked protein glycosylation with diverse O antigen lipopolysaccharide structures in Escherichia coli
AUTOR(ES)
Feldman, Mario F.
FONTE
National Academy of Sciences
RESUMO
Campylobacter jejuni has a general N-linked protein glycosylation system that can be functionally transferred to Escherichia coli. In this study, we engineered E. coli cells in a way that two different pathways, protein N-glycosylation and lipopolysaccharide (LPS) biosynthesis, converge at the step in which PglB, the key enzyme of the C. jejuni N-glycosylation system, transfers O polysaccharide from a lipid carrier (undecaprenyl pyrophosphate) to an acceptor protein. PglB was the only protein of the bacterial N-glycosylation machinery both necessary and sufficient for the transfer. The relaxed specificity of the PglB oligosaccharyltransferase toward the glycan structure was exploited to create novel N-glycan structures containing two distinct E. coli or Pseudomonas aeruginosa O antigens. PglB-mediated transfer of polysaccharides might be valuable for in vivo production of O polysaccharides-protein conjugates for use as antibacterial vaccines.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=549450Documentos Relacionados
- Glycosylation site-binding protein is not required for N-linked glycoprotein synthesis.
- beta-Adrenergic receptor regulation of N-linked protein glycosylation in rat parotid acinar cells.
- N-Linked Protein Glycosylation Is Required for Full Competence in Campylobacter jejuni 81-176
- In vitro assembly of the undecaprenylpyrophosphate-linked heptasaccharide for prokaryotic N-linked glycosylation
- Regulation of the protein glycosylation pathway in yeast: structural control of N-linked oligosaccharide elongation.