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Article

Aglycosylated IgG variants expressed in bacteria that selectively bind FcgammaRI potentiate tumor cell killing by monocyte-dendritic cells.

Proceedings of the National Academy of Sciences of the United States of America - 12 Jan 2010

Jung Sang Taek, Reddy Sai T, Kang Tae Hyun, Borrok M Jack, Sandlie Inger, Tucker Philip W, Georgiou George

Abstract excerpt

The N-linked glycan of immunoglobulin G (IgG) is indispensable for the interaction of the Fc domain with Fcgamma receptors on effector cells and the clearance of target cells via antibody dependent cell-mediated cytotoxicity (ADCC). Escherichia coli expressed, aglycosylated Fc domains bind effector FcgammaRs poorly and cannot elicit ADCC. Using a novel bacterial display/flow cytometric library screening system we...

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Share to Antibodies, Monoclonal, Humanized
Share to Antibody-Dependent Cell Cytotoxicity

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Share to Receptors, IgG

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Source

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Identifiers

PMID: 20080725
DOI: 10.1073/pnas.0908590107
PMCID: PMC2818909

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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