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Literature summary for 2.4.99.18 extracted from

  • Feldman, M.F.; Wacker, M.; Hernandez, M.; Hitchen, P.G.; Marolda, C.L.; Kowarik, M.; Morris, H.R.; Dell, A.; Valvano, M.A.; Aebi, M.
    Engineering N-linked protein glycosylation with diverse O antigen lipopolysaccharide structures in Escherichia coli (2005), Proc. Natl. Acad. Sci. USA, 102, 3016-3021.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.4.99.18

Application

Application Comment Organism
medicine PglB-mediated transfer of poylsaccharides might be valuable for in vivo production of O-polysaccharides-protein congugates for use as antibacterial vaccines Campylobacter jejuni
medicine the relaxed specificity of the PglB oligosaccharyltransferase toward the glycan structure is exploited to create novel N-glycan structures containing two distinct Escherichia 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 Campylobacter jejuni

Cloned(Commentary)

Cloned (Comment) Organism
-
 Campylobacter jejuni
expression in Escherichia coli Campylobacter jejuni

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
dolichyl diphosphooligosaccharide + [protein]-L-asparagine Campylobacter jejuni PglB, the key enzyme of the Campylobacter jejuni N-glycosylation system, transfers O polysaccharide from a lipid carrier (undecaprenyl pyrophosphate) to an accept or protein. PglB is the only protein of the bacterial N-glycosylation machinery both necessary and sufficient for the transfer dolichyl diphosphate + [protein]-N-oligosaccharidyl-L-asparagine
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 ?
additional information Campylobacter jejuni key enzyme of Campylobacter jejuni N-glycosylation system, transfers O-polysaccharides from a lipid carrier (undecaprenyl pyrophosphate) to an acceptor protein. PglB is the only protein of the bacterial N-glycosylation machinery both necessary and sufficient for the transfer ?
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 ?

Organism

Organism UniProt Comment Textmining
Campylobacter jejuni
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-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
dolichyl diphosphooligosaccharide + [protein]-L-asparagine PglB, the key enzyme of the Campylobacter jejuni N-glycosylation system, transfers O polysaccharide from a lipid carrier (undecaprenyl pyrophosphate) to an accept or protein. PglB is the only protein of the bacterial N-glycosylation machinery both necessary and sufficient for the transfer Campylobacter jejuni dolichyl diphosphate + [protein]-N-oligosaccharidyl-L-asparagine
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 ?
dolichyl diphosphooligosaccharide + [protein]-L-asparagine PglB has relaxed specificity toward its lipid-linked glycan substrate. It can transfer its endogenous substrate, the heptasaccharide Glc(GalNAc)5Bac of Campylobacter jejuni, as well as different O antigen polysaccharides that are assembled by the rhamnosyltransferase (polymerase)-dependent mechanism on the lipid carrier undecaprenyl diphosphate Campylobacter jejuni dolichyl diphosphate + [protein]-N-oligosaccharidyl-L-asparagine
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 ?
additional information key enzyme of Campylobacter jejuni N-glycosylation system, transfers O-polysaccharides from a lipid carrier (undecaprenyl pyrophosphate) to an acceptor protein. PglB is the only protein of the bacterial N-glycosylation machinery both necessary and sufficient for the transfer Campylobacter jejuni ?
-
 ?
additional information PglB can transfer diverse oligosaccharides and polysaccharides from Escherichia coli and Pseudomonas aeruginosa to proteins, in addition to the Campylobacter jejuni glycan. PglB attaches O7 polysaccharides and Campylobacter jejuni oligosaccharides to the same Asn residue in AcrA Campylobacter jejuni ?
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 ?

Synonyms

Synonyms Comment Organism
PglB
-
 Campylobacter jejuni
PglB oligosaccharyltransferase
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 Campylobacter jejuni