Immune recruitment or suppression by glycan engineering of endogenous and therapeutic antibodies

• Published in: Biochimica et biophysica acta Vol. 1860; no. 8; pp. 1655 - 1668
• Main Authors: Le, Ngoc Phuong Lan, Bowden, Thomas A., Struwe, Weston B., Crispin, Max
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.08.2016; Elsevier Pub. Co
• Subjects: antibodies; Antibody; autoimmunity; binding properties; blood serum; Effector function; engineering; Glycan; Glycosylation; Humans; Immunoglobulin Fc Fragments - genetics; Immunoglobulin Fc Fragments - metabolism; Immunoglobulin Fc Fragments - therapeutic use; immunoglobulin G; Immunoglobulin G - genetics; Immunoglobulin G - metabolism; Immunoglobulin G - therapeutic use; medicine; neoplasms; polysaccharides; Polysaccharides - genetics; Polysaccharides - metabolism; Protein Engineering - methods; receptors; Structure; Therapeutic antibodies; Glycosylation; Structure; Therapeutic antibodies; Antibody; Effector function; Glycan

Human serum IgG contains multiple glycoforms which exhibit a range of binding properties to effector molecules such as cellular Fc receptors. Emerging knowledge of how the Fc glycans contribute to the antibody structure and effector functions has opened new avenues for the exploitation of defined an...