Antibody Glycosylation and Inflammation

Shade, Kai-Ting C.; Anthony, Robert M.

doi:10.3390/antib2030392

Cited by 105 publications

(116 citation statements)

References 123 publications

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“…It is well-established that all IgG subclasses have a single N-linked glycan in the Fc, which is essential for IgG effector functions [34,35]. Each immunoglobulin class also has a unique glycosylation profile, which contribute to its activity, function and stability.…”

Section: Effect Of Antibody Glycosylation To Binding Activitymentioning

confidence: 99%

Biophysical characterization of antibodies with isothermal titration calorimetry

Frasca¹

2016

J Appl Bioanal

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REVIEWAntibodies play a key role in the immune response. Since antibodies bind antigens with high specificity and tight affinity, antibodies are an important reagent in experimental biology, assay development, biomedical research and diagnostics. Monoclonal antibodies are therapeutic drugs and used for vaccine development. Antibody engineering, biophysical characterization, and structural data have provided a deeper understanding of how antibodies function, and how to make better drugs. Isothermal titration calorimetry (ITC) is a label-free binding assay, which measures affinity, stoichiometry, and binding thermodynamics for biomolecular interactions. When thermodynamic data are used together with structural and kinetic data from other assays, a complete structure-activity-thermodynamics profile can be constructed. This review article describes ITC, and discusses several applications on how data from ITC provides insights into how antibodies function, guide antibody engineering, and aid design of new therapeutic drugs.

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Section: Effect Of Antibody Glycosylation To Binding Activitymentioning

confidence: 99%

Biophysical characterization of antibodies with isothermal titration calorimetry

Frasca¹

2016

J Appl Bioanal

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“…IgG1 molecules carry a single N-linked glycan located in the Fc region in each of their two heavy polypeptide chains. The presence or absence of glycosylation and the pattern of glycosylation influences antibody stability and function significantly, e.g., by affecting receptor binding and effector function [113]. Therefore, glycoengineering is often an essential prerequisite to provide antibodies with the desired therapeutic efficacy [114].…”

Section: Discussionmentioning

confidence: 99%

Cell-Free Synthesis Meets Antibody Production: A Review

Stech

Kubick

2015

Antibodies

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Engineered antibodies are key players in therapy, diagnostics and research. In addition to full size immunoglobulin gamma (IgG) molecules, smaller formats of recombinant antibodies, such as single-chain variable fragments (scFv) and antigen binding fragments (Fab), have emerged as promising alternatives since they possess different advantageous properties. Cell-based production technologies of antibodies and antibody fragments are well-established, allowing researchers to design and manufacture highly specific molecular recognition tools. However, as these technologies are accompanied by the drawbacks of being rather time-consuming and cost-intensive, efficient and powerful cell-free protein synthesis systems have been developed over the last decade as alternatives. So far, prokaryotic cell-free systems have been the focus of interest. Recently, eukaryotic in vitro translation systems have enriched the antibody production pipeline, as these systems are able to mimic the natural pathway of antibody synthesis in eukaryotic cells. This review aims to overview and summarize the advances made in the production of antibodies and antibody fragments in cell-free systems.

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“…The carbohydrate structures of ES-62 and immunoglobulin G share a common core of sugars consisting of N-acetylglucosamine conjugated to mannose, and then mannose linked to N-acetylglucosamine. 12,20 Whereas the phosphocholine in ES-62 is conjugated to N-type glycans, no such conjugation has been shown to exist in humans. Therefore the common antigenic structure between these glycoproteins must be the core sugars without phosphocholine.…”

Section: Discussionmentioning

confidence: 99%

“…Interestingly the carbohydrate moieties on immunoglobulin G are selectively attached to the CH2 domain in the Fc region at N-linked glycosylation site at asparagine-297. 20 To better understand the cross reactivity occurring between the polyclonal anti-ES-62 antiserum with the heavy chain of immunoglobulin G, a BLAST search was conducted. The reference immunoglobulin G heavy chain identified with KS (accession number AAH69016.1) was compared to the aminopeptidase ES-62 molecule (accession number AAC28365.1).…”

Section: Does An Es-62-like Molecule Exist In the Human Placenta?mentioning

confidence: 99%

Searching for a placental derived ES-62-like molecule to explain rheumatoid arthritis amelioration in pregnancy

Scoville¹,

Rasmussen

2014

Rheumatol Rep

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The majority of women with rheumatoid arthritis (RA) experience disease amelioration during pregnancy for unclear reasons. One possible explanation pursued and described here is whether the placenta produces a protein similar to the immunomodulating protein, ES-62, excreted by filarial nematodes. This protein has also been shown to reduce disease activity in animal models of RA. Eleven human placentas were prepared and a polyclonal anti-ES-62 antiserum was used to identify if any ES-62-like molecule exists from human placental tissues. Any bands identified were then excised from the gel and sent for mass spectrometry and protein identification. The antiserum showed consistent cross reactivity with the heavy chain from immunoglobulin G (IgG) from the eleven human placentas by mass spectrometry. No primary sequence homology between the heavy chain of IgG and ES-62 was identified. The placenta does not produce an ES-62-like molecule. However the binding of the antiserum to the Fc region of IgG suggests that this may be a possible mechanism for rheumatoid factor production in some patients with chronic filarial infections.

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Antibody Glycosylation and Inflammation

Cited by 105 publications

References 123 publications

Biophysical characterization of antibodies with isothermal titration calorimetry

Biophysical characterization of antibodies with isothermal titration calorimetry

Cell-Free Synthesis Meets Antibody Production: A Review

Searching for a placental derived ES-62-like molecule to explain rheumatoid arthritis amelioration in pregnancy

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