Proteomics

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Desulfovibrio marinus single-subunit oligosaccharyltransferase and its human IgG substrates


ABSTRACT: Glycoproteomics data about glycan attachment of human IgG catalyzed by a previously uncharacterized single-subunit oligosaccharyltransferase (ssOST) from the bacterium Desulfovibrio marinus, namely DmPglB.

INSTRUMENT(S): Orbitrap Eclipse

ORGANISM(S): Escherichia Coli (ncbitaxon:562) Homo Sapiens (ncbitaxon:9606) Desulfovibrio Marinus (ncbitaxon:370038)

SUBMITTER: Matthew P. DeLisa   Parastoo Azadi  

PROVIDER: MSV000098017 | MassIVE | Wed May 28 09:54:00 BST 2025

SECONDARY ACCESSION(S): PXD064379

REPOSITORIES: MassIVE

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Publications


Human immunoglobulin G (IgG) antibodies are a major class of biotherapeutics and undergo N-linked glycosylation in their Fc domain, which is critical for immune functions and therapeutic activity. Hence, technologies for producing authentically glycosylated IgGs are in high demand. Previous attempts to engineer Escherichia coli for this purpose have met limited success due in part to the lack of oligosaccharyltransferase (OST) enzymes that can install N-glycans at the conserved N297 site in the  ...[more]

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