Specificity of human natural antibodies referred to as anti-Tn

Dobrochaeva, Kira; Khasbiullina, Nailya; Шилова, Н. В.; Антипова, Н. В.; Obukhova, Polina; Ovchinnikova, Tatiana V.; Galanina, Oxana; Blixt, Ola; Kunz, Horst; Filatov, Alexander; Knirel, Yuriy A.; LePendu, Jacques; Хайдуков, С. В.; Bovin, Nicolai V.

doi:10.1016/j.molimm.2020.02.005

Cited by 20 publications

(15 citation statements)

References 40 publications

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“…Only class G antibodies were eluted from the placenta, while IgMs were absent (IgAs were not investigated); this observation is in line with the previously published data, [39][40][41] however, in few studies, certain amounts of IgM and IgA were found in addition to predominant IgG. 42 Functional activity of IgG antibodies from healthy human placenta has been studied.…”

Section: Discussionsupporting

confidence: 84%

“…Apparently, Tn in patients with PE (similarly to certain carcinomas), unlike other antigens of the second type, is an aberrant antigen 54 . Human blood antibodies, commonly called ‘anti‐Tn’, represent a rather broad population of specific immunoglobulins, capable to recognize either the monosaccharide GalNAcα, or GalNAcα‐containing oligosaccharide, or glycopeptide, or even a spatial epitope, 40 but we have not yet studied which of these antigens are targets for placental antibodies.…”

Section: Discussionmentioning

confidence: 99%

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Repertoire of glycan‐binding placenta‐associated antibodies in healthy pregnancy and in pre‐eclampsia

et al. 2022

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A possible mechanism of the immune tolerance in pregnancy is production of blocking antibodies which reside in placenta and protect foetal allogeneic cells from the mother's immune system. Their epitope specificity, as well as the nature of the biomolecules masked by them, is unknown. For better understanding of this phenomenon, we attempted to characterize the specificity of antibodies isolated from placentas of women with healthy pregnancy and pre‐eclampsia (PE). It was found that: (1) the repertoire of placental antibodies is significantly less variable and qualitatively different from the peripheral blood; (2) with PE, the repertoire of placental antibodies is narrower than in healthy pregnancy; (3) some antibodies are found almost exclusively in the placenta, and some – only in the placenta of healthy women.

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Section: Discussionsupporting

confidence: 84%

Section: Discussionmentioning

confidence: 99%

Repertoire of glycan‐binding placenta‐associated antibodies in healthy pregnancy and in pre‐eclampsia

et al. 2022

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“…Moreover, like other glycan-specific antibodies, the anti-Tn reactivity in human serum antibodies is polyclonal in nature, exhibiting binding to an array of structurally similar glycans. In fact, human anti-Tn antibodies, including IgG and IgM isotypes, affinity-purified using terminal GalNAcα-containing matrix, demonstrate higher affinity for other glycan structures compared to terminal GalNAcα, including bacteria-derived products and cell-wall structures [ 128 ]. At least some of these antibodies clearly recognize tumor-associated Tn antigens [ 129 ].…”

Section: Other Types Of Autoantibodies Targeting Aberrantly Glycosylated Proteinsmentioning

confidence: 99%

Pathogenesis of IgA Nephropathy: Current Understanding and Implications for Development of Disease-Specific Treatment

Knoppová

Reily

King

et al. 2021

JCM

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IgA nephropathy, initially described in 1968 as a kidney disease with glomerular “intercapillary deposits of IgA-IgG”, has no disease-specific treatment and is a common cause of kidney failure. Clinical observations and laboratory analyses suggest that IgA nephropathy is an autoimmune disease wherein the kidneys are damaged as innocent bystanders due to deposition of IgA1-IgG immune complexes from the circulation. A multi-hit hypothesis for the pathogenesis of IgA nephropathy describes four sequential steps in disease development. Specifically, patients with IgA nephropathy have elevated circulating levels of IgA1 with some O-glycans deficient in galactose (galactose-deficient IgA1) and these IgA1 glycoforms are recognized as autoantigens by unique IgG autoantibodies, resulting in formation of circulating immune complexes, some of which deposit in glomeruli and activate mesangial cells to induce kidney injury. This proposed mechanism is supported by observations that (i) glomerular immunodeposits in patients with IgA nephropathy are enriched for galactose-deficient IgA1 glycoforms and the corresponding IgG autoantibodies; (ii) circulatory levels of galactose-deficient IgA1 and IgG autoantibodies predict disease progression; and (iii) pathogenic potential of galactose-deficient IgA1 and IgG autoantibodies was demonstrated in vivo. Thus, a better understanding of the structure–function of these immunoglobulins as autoantibodies and autoantigens will enable development of disease-specific treatments.

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“…For example, carbohydrate microarrays have been used to evaluate lectin binding and anticarbohydrate antibodies in the context of cancer and vaccine development. 47 − 51 In this study, a glycan microarray was constructed by exploiting covalent immobilization of glycan fragments and controls according to previously established procedures. 42 , 43 The six newly synthesized fragments were printed on the slide, together with native Sp 19F and 19A CPSs as controls.…”

Section: Resultsmentioning

confidence: 99%

Glycan Array Evaluation of Synthetic Epitopes between the Capsular Polysaccharides from Streptococcus pneumoniae 19F and 19A

et al. 2021

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Vaccination represents the most effective way to prevent invasive pneumococcal diseases. The glycoconjugate vaccines licensed so far are obtained from capsular polysaccharides (CPSs) of the most virulent serotypes. Protection is largely limited to the specific vaccine serotypes, and the continuous need for broader coverage to control the outbreak of emerging serotypes is pushing the development of new vaccine candidates. Indeed, the development of efficacious vaccine formulation is complicated by the high number of bacterial serotypes with different CPSs. In this context, to simplify vaccine composition, we propose the design of new saccharide fragments containing chemical structures shared by different serotypes as cross-reactive and potentially cross-protective common antigens. In particular, we focused on Streptococcus pneumoniae (Sp) 19A and 19F. The CPS repeating units of Sp 19F and 19A are very similar and share a common structure, the disaccharide ManNAc-β-(1→4)-Glc (A-B). Herein, we describe the synthesis of a small library of compounds containing different combinations of the common 19F/19A disaccharide. The six new compounds were tested with a glycan array to evaluate their recognition by antibodies in reference group 19 antisera and factor reference antisera (reacting against 19F or 19A). The disaccharide A-B, phosphorylated at the upstream end, emerged as a hit from the glycan array screening because it is strongly recognized by the group 19 antisera and by the 19F and 19A factor antisera, with similar intensity compared with the CPSs used as controls. Our data give a strong indication that the phosphorylated disaccharide A-B can be considered a common epitope among different Sp 19 serotypes.

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Specificity of human natural antibodies referred to as anti-Tn

Cited by 20 publications

References 40 publications

Repertoire of glycan‐binding placenta‐associated antibodies in healthy pregnancy and in pre‐eclampsia

Repertoire of glycan‐binding placenta‐associated antibodies in healthy pregnancy and in pre‐eclampsia

Pathogenesis of IgA Nephropathy: Current Understanding and Implications for Development of Disease-Specific Treatment

Glycan Array Evaluation of Synthetic Epitopes between the Capsular Polysaccharides from Streptococcus pneumoniae 19F and 19A

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