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Site-specific analysis of CD16a and CD32a N-glycosylation from monocytes display donor variability which modulate affinity to IgG1 Fc

ABSTRACT: Glycopeptide mass spectra of CD16a and CD32a from isolated monocytes display donor and site variability. CD16a N-glycosylation composition affects the affinity of IgG1 Fc. Peptide coverage of CD16a was ~85% while CD32a was ~61%.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Homo Sapiens (ncbitaxon:9606)

SUBMITTER: Adam Barb

PROVIDER: MSV000084012 | MassIVE | Wed Jun 26 10:33:00 BST 2019

REPOSITORIES: MassIVE

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Site-specific N-glycan Analysis of Antibody-binding Fc γ Receptors from Primary Human Monocytes.

Roberts Jacob T JT Patel Kashyap R KR Barb Adam W AW

Molecular & cellular proteomics : MCP 20191230 2

FcγRIIIa (CD16a) and FcγRIIa (CD32a) on monocytes are essential for proper effector functions including antibody dependent cellular cytotoxicity (ADCC) and phagocytosis (ADCP). Indeed, therapeutic monoclonal antibodies (mAbs) that bind FcγRs with greater affinity exhibit greater efficacy. Furthermore, post-translational modification impacts antibody binding affinity, most notably the composition of the asparagine(N)-linked glycan at N162 of CD16a. CD16a is widely recognized as the key receptor f ...[more]

PMID: 31888963

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