Proteomics

Dataset Information

0

Human Serum Immunoglobulin N-Glycosylation using nLC-MS/MS


ABSTRACT: Here we employ a nLC-MS/MS method to separate small amounts of purified immunoglobulins to characterize the N-glycan reportoire and site occupancy of bulk serum antibodies. Using this method, we have established, for the first time within individual donors, the N-linked glycan repotoire for bulk IgG1, IgG4, IgA1, IgA2 and IgM in healthy individuals. This is crucial for developing a platform to define disease-specific N-glycan signatures for different isotypes to help tune antibodes to induce protection.

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Blood Plasma

SUBMITTER: Kevin Chandler  

LAB HEAD: Catherine E Costello

PROVIDER: PXD010911 | Pride | 2019-01-24

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
20170828_IgG1_1_A.mgf Mgf
20170828_IgG1_1_A.pride.mgf.gz Mgf
20170828_IgG1_1_A.raw Raw
20170828_IgG1_1_A_Mascot_F020909.mzid.gz Mzid
20170828_IgG1_1_A_Mascot_F020909.pride.mztab.gz Mztab
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Publications

Multi-isotype Glycoproteomic Characterization of Serum Antibody Heavy Chains Reveals Isotype- and Subclass-Specific <i>N</i>-Glycosylation Profiles.

Chandler Kevin Brown KB   Mehta Nickita N   Leon Deborah R DR   Suscovich Todd J TJ   Alter Galit G   Costello Catherine E CE  

Molecular & cellular proteomics : MCP 20190118 4


Antibodies are critical glycoproteins that bridge the innate and adaptive immune systems to provide protection against infection. The isotype/subclass of the antibody, the co-translational <i>N</i>-glycosylation on the CH2 domain, and the remodeling of the <i>N</i>-linked glycans during passage through the ER and Golgi are the known variables within the Fc domain that program antibody effector function. Through investigations of monoclonal therapeutics, it has been observed that addition or remo  ...[more]

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