Carbohydrate and domain architecture of an immature antibody glycoform exhibiting enhanced effector functions.

Journal article

Antibodies contain a conserved glycosylation site that has emerged as a target for the modulation of antibody effector functions. The crystal structure of a biosynthetic intermediate of human IgG1, bearing immature oligomannose-type glycans and reported to display increased antibody-dependent cellular cytotoxicity, demonstrates that glycan engineering can bias the Fc to an open conformation primed for receptor binding.

Authors: Crispin, M; Bowden, T; Coles, C; Harlos, K; Aricescu, A

• Publication status: Published
• Journal: Journal of molecular biology
• Volume: 387
• Issue: 5
• Pages: 1061-1066
• Publication date: 2009-04-01
• DOI: 10.1016/j.jmb.2009.02.033
• EISSN: 1089-8638
• ISSN: 0022-2836
• Language: English
• Keywords: Static Electricity; Carbohydrate Sequence; Immunoglobulin Fc Fragments; Immunoglobulin G; Recombinant Proteins; Models, Molecular; Antibody-Dependent Cell Cytotoxicity; Glycosylation; Oligosaccharides; Protein Structure, Tertiary; Crystallography, X-Ray; Humans; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization