Immunoglobulin Glycosylation – An Unexploited Potential for Immunomodulatory Strategies in Farm Animals

The function of antibodies, namely the identification and neutralization of pathogens, is mediated by their antigen binding site (Fab). In contrast, the subsequent signal transduction for activation of the immune system is mediated by the fragment crystallizable (Fc) region, which interacts with receptors or other components of the immune system, such as the complement system. This aspect of binding and interaction is more precise, readjusted by covalently attached glycan structures close to the hinge region of immunoglobulins (Ig). This fine-tuning of Ig and its actual state of knowledge is the topic of this review. It describes the function of glycosylation at Ig in general and the associated changes due to corresponding glycan structures. We discuss the functionality of IgG glycosylation during different physiological statuses, like aging, lactation and pathophysiological processes. Further, we point out what is known to date about Ig glycosylation in farm animals and how new achievements in vaccination may contribute to improved animal welfare.

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Faculty Opinions recommendation of Variants of the antibody herceptin that interact with HER2 and VEGF at the antigen binding site.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.1158476.618775 ◽

2009 ◽

Author(s):

Peter Colman ◽

Douglas Fairlie

Keyword(s):

Binding Site ◽

Antigen Binding ◽

Antigen Binding Site

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Uncommon structural motifs dominate the antigen binding site in human autoantibodies reactive with basement membrane collagen

Molecular Immunology ◽

10.1016/j.molimm.2016.07.004 ◽

2016 ◽

Vol 76 ◽

pp. 123-133 ◽

Cited By ~ 1

Author(s):

Mary H. Foster ◽

Elizabeth S. Buckley ◽

Benny J. Chen ◽

Kwan-Ki Hwang ◽

Amy G. Clark

Keyword(s):

Basement Membrane ◽

Binding Site ◽

Antigen Binding ◽

Antigen Binding Site ◽

Structural Motifs ◽

Basement Membrane Collagen ◽

Membrane Collagen

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A shared idiotype among human anti-Ro/SSA autoantibodies.

Journal of Experimental Medicine ◽

10.1084/jem.169.5.1583 ◽

1989 ◽

Vol 169 (5) ◽

pp. 1583-1588 ◽

Cited By ~ 5

Author(s):

K K Gaither ◽

J B Harley

Keyword(s):

Binding Site ◽

Heart Block ◽

Congenital Heart ◽

Congenital Heart Block ◽

Antigen Binding ◽

Normal Donor ◽

Neonatal Lupus ◽

Antigen Binding Site ◽

Fine Specificity ◽

Low Level

Idiotypes and antiidiotypes are thought to be important immune regulators and have provided clues for the origin and pathogenicity of autoantibodies. Many lupus and Sjögren's syndrome patients, as well as most neonatal lupus infants with congenital heart block or dermatitis, have antibodies to the ribonucleoprotein Ro/SSA, which is one of a group of RNA-protein autoantigens commonly found in human lupus sera. To characterize the fine specificity of anti-Ro/SSA antibodies, a rabbit antidiotypic serum was prepared against polyclonal affinity purified anti-Ro/SSA F(ab')2. The resulting antiidiotype, anti-Id-Rol, is specific for the F(ab')2 fraction of the anti-Ro/SSA immunogen and its binding to anti-Ro/SSA is inhibited by purified Ro/SSA. These data indicate that the Id-Rol epitope on anti-Ro/SSA is associated with the antigen binding site of these same antibodies. The Id-Rol idiotype was present by ELISA in 3 of 12 additional anti-Ro/SSA preparations from precipitin-positive donor sera and in anti-Ro/SSA from one normal donor with low level antibody. This is the first shared idiotype to be found in the human autoantibodies binding to this RNA-protein antigen. Idiotypic differences between anti-Ro/SSA autoantibodies have the potential to explain the variation in pathologic associations found in individuals who develop this autoantibody specificity.

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THE THREE-DIMENSIONAL STRUCTURE OF THE ANTIGEN BINDING SITE OF McPC 603 PROTEIN

The Immune System ◽

10.1016/b978-0-12-637150-5.50009-2 ◽

1974 ◽

pp. 7-14 ◽

Cited By ~ 6

Author(s):

E.A. Padlan ◽

D.M. Segal ◽

G.H. Cohen ◽

D.R. Davies ◽

S. Rudikoff ◽

...

Keyword(s):

Binding Site ◽

Three Dimensional ◽

Dimensional Structure ◽

Antigen Binding ◽

Antigen Binding Site ◽

Three Dimensional Structure

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The complement system

Oxford Textbook of Medicine ◽

10.1093/med/9780199204854.003.050102 ◽

2010 ◽

pp. 213-224

Author(s):

Marina Botto ◽

Mark J. Walport

Keyword(s):

Immune System ◽

Complement System ◽

Immune Complexes ◽

Innate Immune System ◽

Inflammatory Responses ◽

Antibody Responses ◽

Host Defence ◽

System P ◽

Dying Cells ◽

The Complement System

The complement system consists of over 20 distinct proteins and is an essential component of the innate immune system. It is a major effector mechanism of host defence against infection and inflammatory responses, has an important role in the physiological removal of immune complexes and dying cells, and plays an accessory role in the induction of antibody responses....

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