Branch-specific sialylation of IgG-Fc glycans by ST6Gal-I.

Full Abstract

Sialylated forms of the Fc fragment of immunoglobulin G, produced by the human alpha2-6 sialyltransferase ST6Gal-I, were identified as potent anti-inflammatory mediators in a mouse model of rheumatoid arthritis and are potentially the active components in intravenous IgG anti-inflammatory therapies. The activities and specificities of hST6Gal-I are, however, poorly characterized. Here MS and NMR methodology demonstrates glycan modification occurs in a branch-specific manner with the alpha1-3Man branch of the complex, biantennary Fc glycan preferentially sialylated. Interestingly, this substrate preference is preserved when using a released glycan, suggesting that the apparent occlusion of glycan termini in Fc crystal structures does not dominate specificity.

Author information

Author/s: Barb, Adam W (AW); Brady, Evan K (EK); Prestegard, James H (JH);

Affiliation: Complex Carbohydrate Research Center, 315 Riverbend Road, University of Georgia, Athens, Georgia 30602, USA.

Grants: P41RR005351 (Agency:NCRR NIH HHS) ; R01GM033225 (Agency:NIGMS NIH HHS)

Journal and publication information

Publication Type: Journal Article; Research Support, N.I.H., Extramural

Journal: Biochemistry (Biochemistry), published in United States. (Language: eng)

Reference: 2009-Oct; vol 48 (issue 41) : pp 9705-7

Dates: Created 2009/10/13; Completed 2009/11/02;

PMID: 19772356, status: MEDLINE (last retrieval date: 11/2/2009, IMS Date: )

Sourced from the National Library of Medicine. Abstract text and other information may be subject to copyright.

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MeSH headings (categories)

This article was linked to the MESH Headings shown below.

Animals
Anti-Inflammatory Agents - therapeutic use
Arthritis, Rheumatoid - drug therapy; immunology
Crystallography, X-Ray
Disease Models, Animal
Immunoglobulin Fc Fragments - chemistry; immunology; metabolism; therapeutic use
Immunoglobulin G - chemistry; immunology; metabolism

Associated Chemicals: Anti-Inflammatory Agents (0) ; Immunoglobulin Fc Fragments (0) ; Immunoglobulin G (0) ; Polysaccharides (0) ; Sialyltransferases (EC 2.4.99.-) ; beta-D-galactoside alpha 2-6-sialyltransferase (EC 2.4.99.1)

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