Molecular Aspects of Anti-Polysaccharide Antibody Responses

García-Ojeda, Pablo A.; Brorson, Kurt; Stein, Kathryn E.

doi:10.1201/9780203216514.ch4

Cited by 4 publications

(3 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The observed affinities of anti-carbohydrate antibodies are typically lower by factors of 103-105 than antibodies specific for protein or peptide antigens [53][54][55]. This is compensated by their initial expression as IgM and their observed class switching bias toward IgG3 in mice and IgG2 in humans, which tend to self-associate through their constant regions to form multivalent networks [56][57][58].…”

Section: Antibodies Against Aga and Agbmentioning

confidence: 98%

See 1 more Smart Citation

Mechanisms of Formation of Antibodies against Blood Group Antigens That Do Not Exist in the Body

Mironov,

Savin,

Zaitseva

et al. 2023

IJMS

View full text Add to dashboard Cite

The system of the four different human blood groups is based on the oligosaccharide antigens A or B, which are located on the surface of blood cells and other cells including endothelial cells, attached to the membrane proteins or lipids. After transfusion, the presence of these antigens on the apical surface of endothelial cells could induce an immunological reaction against the host. The final oligosaccharide sequence of AgA consists of Gal-GlcNAc-Gal (GalNAc)-Fuc. AgB contains Gal-GlcNAc-Gal (Gal)-Fuc. These antigens are synthesised in the Golgi complex (GC) using unique Golgi glycosylation enzymes (GGEs). People with AgA also synthesise antibodies against AgB (group A [II]). People with AgB synthesise antibodies against AgA (group B [III]). People expressing AgA together with AgB (group AB [IV]) do not have these antibodies, while people who do not express these antigens (group O [0; I]) synthesise antibodies against both antigens. Consequently, the antibodies are synthesised against antigens that apparently do not exist in the body. Here, we compared the prediction power of the main hypotheses explaining the formation of these antibodies, namely, the concept of natural antibodies, the gut bacteria-derived antibody hypothesis, and the antibodies formed as a result of glycosylation mistakes or de-sialylation of polysaccharide chains. We assume that when the GC is overloaded with lipids, other less specialised GGEs could make mistakes and synthesise the antigens of these blood groups. Alternatively, under these conditions, the chylomicrons formed in the enterocytes may, under this overload, linger in the post-Golgi compartment, which is temporarily connected to the endosomes. These compartments contain neuraminidases that can cleave off sialic acid, unmasking these blood antigens located below the acid and inducing the production of antibodies.

show abstract

Section: Antibodies Against Aga and Agbmentioning

confidence: 98%

“…Newborns may express only 50% of the adult levels of AgA and AgB [51,52]. In newborns up to 4 months old, the titre of AbA and AbB is low [51][52][53][54][55][56][57][58][59][60]. The number of AbA and AbB increases during the first year in humans, as in newborn and young rats and mice.…”

Section: Antibodies Against Aga and Agbmentioning

confidence: 99%

Mechanisms of Formation of Antibodies against Blood Group Antigens That Do Not Exist in the Body

Mironov,

Savin,

Zaitseva

et al. 2023

IJMS

View full text Add to dashboard Cite

show abstract

“…Polysaccharides carrying both negatively and positively charged substituents have been shown to interact with MHC class II species (Avci and Kasper, 2010), as have oxidative breakdown products of polysaccharides (Velez et al, 2009). Anti-carbohydrate antibodies are normally of low affinity, often of 10 3 -10 5 times less affinity than anti-peptide or -protein antibodies (Krause and Coligan, 1979; MacKenzie et al, 1996; Brorson et al, 2002). The low affinity is compensated for by a high avidity provided for by the decavalent configuration of the IgM antibody or self-associated IgG2 antibodies in humans (Greenspan et al, 1988; Cooper et al, 1991).…”

Section: General Aspects Of Glycoconjugates and Anti-carbohydrate Antmentioning

confidence: 99%

The Structural Complexity and Animal Tissue Distribution of N-Glycolylneuraminic Acid (Neu5Gc)-Terminated Glycans. Implications for Their Immunogenicity in Clinical Xenografting

Breimer

Holgersson

2019

Front. Mol. Biosci.

View full text Add to dashboard Cite

N -Glycolylneuraminic acid (Neu5Gc)-terminated glycans are present in all animal cells/tissues that are already used in the clinic such as bioprosthetic heart valves (BHV) as well as in those that potentially will be xenografted in the future to overcome end stage cell/organ failure. Humans, as a species lack this antigen determinant and can react with an immune response after exposure to Neu5Gc present in these products/cells/tissues. Genetically engineered source animals lacking Neu5Gc has been generated and so has animals that in addition lack the major αGal xenoantigen. The use of cells/tissues/organs from such animals may improve the long-term performance of BHV and allow future xenografting. This review summarizes the present knowledge regarding structural complexity and tissue distribution of Neu5Gc on glycans of cells/tissue/organs already used in the clinic or intended for treatment of end stage organ failure by xenografting. In addition, we briefly discuss the role of anti-Neu5Gc antibodies in the xenorejection process and how knowledge about Neu5Gc structural complexity can be used to design novel diagnostics for anti-Neu5Gc antibody detection.

show abstract

Chemical Biology Tools for Modulating and Visualizing Gram-Negative Bacterial Surface Polysaccharides

Zheng

Epstein

et al. 2021

ACS Chem. Biol.

View full text Add to dashboard Cite

Bacterial cells present a wide diversity of saccharides that decorate the cell surface and help mediate interactions with the environment. Many Gram-negative cells express O-antigens, which are long sugar polymers that makeup the distal portion of lipopolysaccharide (LPS) that constitutes the surface of the outer membrane. This review highlights chemical biology tools that have been developed in recent years to facilitate the modulation of O-antigen synthesis and composition, as well as related bacterial polysaccharide pathways, and the detection of unique glycan sequences. Advances in the biochemistry and structural biology of O-antigen biosynthetic machinery are also described, which provide guidance for the design of novel chemical and biomolecular probes. Many of the tools noted here have not yet been utilized in biological systems and offer researchers the opportunity to investigate the complex sugar architecture of Gram-negative cells.

show abstract

Molecular Aspects of Anti-Polysaccharide Antibody Responses

Cited by 4 publications

References 0 publications

Mechanisms of Formation of Antibodies against Blood Group Antigens That Do Not Exist in the Body

Mechanisms of Formation of Antibodies against Blood Group Antigens That Do Not Exist in the Body

The Structural Complexity and Animal Tissue Distribution of N-Glycolylneuraminic Acid (Neu5Gc)-Terminated Glycans. Implications for Their Immunogenicity in Clinical Xenografting

Chemical Biology Tools for Modulating and Visualizing Gram-Negative Bacterial Surface Polysaccharides

Contact Info

Product

Resources

About