title: Immunoglobulin Glycosylation Effects in Allergy and Immunity.
abstract: OBJECTIVE
  The aim of this review will be to familiarize the reader with the general area of antibody (Ab) glycosylation and to summarize the known functional roles of glycosylation and how glycan structure can contribute to various disease states with emphasis on allergic disease.
  
  
  RESULTS
  Both immunoglobulin (Ig) isotype and conserved Fc glycosylation sites often dictate the downstream activity of an Ab where complexity and degree of glycosylation contribute to its ability to bind Fc receptors (FcRs) and activate complement. Most information on the effects of glycosylation center on IgG in cancer therapy and autoimmunity. In cancer therapy, glycosylation modifications that enhance affinity for activating FcRs are utilized to facilitate immune-mediated tumor cell killing. In autoimmunity, disease severity has been linked to alterations in the presence, location, and composition of Fc glycans. Significantly less is understood about the role of glycosylation in the setting of allergy and asthma. However, recent data demonstrate that glycosylation of IgE at the asparagine-394 site of Cε3 is necessary for IgE interaction with the high affinity IgE receptor but, surprisingly, glycosylation has no effect on IgE interaction with its low-affinity lectin receptor, CD23. Variations in the specific glycoform may modulate the interaction of an Ig with its receptors. Significantly more is known about the functional effects of glycosylation of IgG than for other Ig isotypes. Thus, the role of glycosylation is much better understood in the areas of autoimmunity and cancer therapy, where IgG is the dominant isotype, than in the field of allergy, where IgE predominates. Further work is needed to fully understand the role of glycan variation in IgE and other Ig isotypes with regard to the inhibition or mediation of allergic disease.
authors: Institute for Systemic Inflammation Research, University of Lübeck, Lübeck, Germany.
authors: Alexandra
authors: A
authors: Epp
authors: Immunology Graduate Program, Cincinnati Children's Hospital Medical Center and the University of Cincinnati College of Medicine, Cincinnati, OH, USA.
authors: Kathryn C
authors: KC
authors: Sullivan
authors: Division of Immunobiology, Cincinnati Children's Hospital Medical Center, Cincinnati, OH, USA.|Division of Infectious Diseases, Cincinnati Children's Hospital Medical Center, Cincinnati, OH, USA.|Department of Pediatrics, College of Medicine, University of Cincinnati, Cincinnati, OH, USA.
authors: Andrew B
authors: AB
authors: Herr
authors: Department of Pediatrics, College of Medicine, University of Cincinnati, Cincinnati, OH, USA. rick.strait@cchmc.org.|Division of Emergency Medicine, Cincinnati Children's Hospital, 3333 Burnet Ave, ML 2008, Cincinnati, OH, 45229, USA. rick.strait@cchmc.org.
authors: Richard T
authors: RT
authors: Strait
mesh_terms: D006031:Glycosylation; D006801:Humans; D006967:Hypersensitivity / Q000175:diagnosis*; D007136:Immunoglobulins / Q000276:immunology*
chemical_list: D007136:Immunoglobulins
keywords: Allergy; Asthma; Immunoglobulin glycosylation; Sialylation