Immunology Faculty Member - Robert Anthony, PhD

Robert Anthony, PhD

Massachusetts General Hospital
Center for Immunology and Inflammatory Diseases
149 13th Street, Room 8.307
Charlestown, MA 02129
Tel: 617-724-4245
Fax: 617-726-5651

Regulation of Antibody Function by Glycosylation

Glycosylation is a post-translational modification resulting in attachment of sugar residues to proteins processed through the secretory pathway. This occurs at defined residues in the peptide backbone, and often supports appropriate folding and half-life of proteins. Antibodies are the preeminent effector proteins of the immune system, and are glycoproteins. IgG antibodies are the most predominant antibody class found in the circulation, and are essential in defense against many infections and cancers. A single, N-linked glycan is attached to the heavy chain of IgG antibodies in the constant domain. Studies over the last few years have demonstrated the composition of this glycan dictates IgG antibody effector function. IgE antibodies are the least common subclass in circulation, and are implicit in allergic diseases. My laboratory strives to dissect the role and regulation of glycosylation to the biology of IgG and IgE. We are examining the pathways triggered by sialylated IgG antibodies that result in an anti-inflammatory response, and modulating IgG sialylation in vivo to attenuate autoimmune inflammation. Further, we are dissecting how glycosylation of IgE impacts the magnitude of anaphylaxis. We have demonstrated
a single glycan on the IgE molecule that is an absolute requirement for IgE effector function. The overarching goals of my laboratory are to define the contribution of glycosylation to highly clinically relevant immunoglobulins, allowing for identification of novel disease biomarkers, refining immunotherapeutic approaches, and enable development of novel therapeutics that modulate immunoglobulin glycosylation in vivo.

Last Update: 8/6/2018


For a complete listing of publications click here.



a. Pagan J.D., Kitaoka M., and Anthony R.M. Engineered sialylation of pathogenic antibodies in vivo attenuates autoimmune disease. Cell, 2018 Jan 25;172(3):564-577. PMCID: PMC5849077
b. Shade K.T.C., Platzer B, Washburn N., Mani V., Bartsch Y.C., Conroy M., Pagan J.D., Bosques C., Mempel T.R., Fiebiger E., and Anthony R.M. A Single Glycan on IgE is Indispensable for Initiation of Anaphylaxis. J Exp Med. 2015 Apr 6;212(4):457-67. PMCID: PMC4387292
c. Anthony R.M.*, Kobayashi T.*, Wermeling F., and Ravetch J.V. Intravenous gamma globulin induces an innate Th2 response. *Contributed equally; Nature, 2011 Jun 19;475(7354):110-3. PMCID: PMC3694429.
d. Anthony R.M., Nimmerjahn F., Ashline D.J., Reinhold V. N., Paulson J.C., and Ravetch J.V. Recapitulation of intravenous immunoglobulin anti-inflammatory activity with a recombinant immunoglobulin G Fc. Science. 2008 Apr 18;320(5874):373-6; PMCID: PMC2409116

© 2016 President and Fellows
of Harvard College