An Example of Polyagglutinability Due to the Tn Antigen

Gunson, H. H.; Stratton, F.; Mullard, G. W.

doi:10.1111/j.1365-2141.1970.tb01445.x

Cited by 63 publications

(40 citation statements)

References 7 publications

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“…However, only SSA, DBA and GSA do not agglutinate the papain-treated Tn cells which have lost their Tn epitopes [27]. HPA, VVA, SBA and WFA still react with these cells at very low concentrations indicating their interaction with glycolipid antigens.…”

Section: Resultsmentioning

confidence: 99%

Comparison of the carbohydrate‐binding specificities of seven N‐acetyl‐D‐galactosamine‐recognizing lectins

Piller

Cartron

1990

European Journal of Biochemistry

125

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Seven plant lectins, Dolichos bijlorus agglutinin (DBA), Grijjfonia simplicifolia agglutinin (GSA, isolectin A4), Helix pomatia agglutinin (HPA), soybean (Glycine max) agglutinin (SBA), Salvia sclarea agglutinin (SSA), Vicia villosa agglutinin (VVA, isolectin B4) and Wistariafloribunda agglutinin (WFA), known to be specific for N-acetyl-D-galactosamine-(GalNAc) bearing glycoconjugates, have been compared by the binding of their radiolabelled derivatives, to eight well-characterized synthetic oligosaccharides immobilized via a spacer on an inert silica matrix (Synsorb). The eight oligosaccharides included the Forssman, the blood group A and the T antigens, as well as ctGalNAc coupled directly to the support (Tn antigen) and also structures with GalNAc linked a or /3 to positions 3 or 4 of an unsubstituted Gal. The binding studies clearly distinguished the lectins into aGalNAc-specific agglutinins like DBA, GSA and SSA, and lectins which recognize a-as well as P-linked GalNAc residues like HPA, VVA, WFA and SBA. HPA was the only lectin which bound to the P G a l l -+ 3aGalNAc-Synsorb adsorbent (T antigen) indicating that it also recognizes internal GalNAc residues. Among the aGalNAc-specific lectins, DBA strongly recognized blood group A structures while GSA displayed weaker recognition, and SSA bound only slightly to this affinity matrix. In addition, DBA and SSA were able to distinguish between GalNAc linked a1 -+ 3 and GalNAc linked a1 -+ 4, to the support, the latter being a much weaker ligand.These results were corroborated by the binding of the lectins to biological substrates as determined by their hemagglutination titers with native and enzyme-treated red blood cells carrying known GalNAc determinants, e.g. blood group A, and the Cad and Tn antigens. For SSA, the binding to the ctGalNAc matrix was inhibited by a number of glycopeptides and glycoproteins confirming the strong preference of this lectin for aGalNAc-Ser/ Thr-bearing glycoproteins.N-Acetyl-D-galactosamine (GalNAc) is an important constituent of the carbohydrate moieties of glycoproteins and glycolipids. Carbohydrate-binding proteins (lectins) which recognize this sugar residue were among the first to be studied in detail since these lectins were shown to agglutinate specifically blood group A erythrocytes ([l] binding of oligosaccharides having a terminal ct or PGalNAc linked in different positions to a or BGal, or a or PGalNAc. Some of these lectins have been used in immunocytochemistry since they are thought to bind specifically to defined carbohydrate structures (reviewed in [12]). Therefore it is of interest to compare, in the same analytical system, the binding specificities of lectins with similar recognition patterns in order to be able to choose the most appropriate lectin for a given purpose.Recently, two lectins have been purified from the seeds of Vicia villosa (VVA, isolectin B4) [13] and Salvia sclarea (SSA) [14] which were described as aGalNAc-specific and most interestingly both appeared to have a strong preference for the a...

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Section: Resultsmentioning

confidence: 99%

Comparison of the carbohydrate‐binding specificities of seven N‐acetyl‐D‐galactosamine‐recognizing lectins

Piller

Cartron

1990

European Journal of Biochemistry

125

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“…kaum aber von Neugeborenenseren [62]. Der dafür verantwortliche Antikörper Anti-Tn gehört zur IgM-Klasse und reagiert am stärksten in der Kälte [62][63][64]. Das Tn-Antigen ist normalerweise auf der Erythrozytenoberfläche nicht zugänglich und wird nur in seltenen Fällen freigelegt.…”

Section: Die Tn-polyagglutinabilität Und Das Erworbene A-ähnliche Antunclassified

“…Dies weist auf das Vorhandensein zweier unterschiedlicher Zellpopulationen hin. Die Tn-Polyagglutinabilität wird nicht vererbt, sondern tritt erst im Laufe des Lebens neu auf [62,63,67]. Typisch ist ihr langfristiges, zum Teil jahrelanges Fortbestehen, unabhängig von Infekten oder anderen äußeren Einflüssen [62,64].…”

Section: Die Tn-polyagglutinabilität Und Das Erworbene A-ähnliche Antunclassified

“…Durch die Tn-Polyagglutinabilität kann die Bestimmung der erythrozytären Blutgruppenantigene mit humanen und gegebenenfalls tierischen Testseren gestört werden. So kann aufgrund des Anti-Tn in polyklonalen Reagenzien zur AB0-Bestimmung die (scheinbare) Blutgruppe AB diagnostiziert werden, während im Serum die Isoagglutinine der wahren Blutgruppe des Patienten entsprechen [62,63,65]. Die von Sekretoren im Speichel ausgeschiedenen löslichen Blutgruppensubstanzen werden allerdings nicht von der Tn-Polyagglutinabilität beeinflußt [62,63,67].…”

Section: Die Tn-polyagglutinabilität Und Das Erworbene A-ähnliche Antunclassified

“…So kann aufgrund des Anti-Tn in polyklonalen Reagenzien zur AB0-Bestimmung die (scheinbare) Blutgruppe AB diagnostiziert werden, während im Serum die Isoagglutinine der wahren Blutgruppe des Patienten entsprechen [62,63,65]. Die von Sekretoren im Speichel ausgeschiedenen löslichen Blutgruppensubstanzen werden allerdings nicht von der Tn-Polyagglutinabilität beeinflußt [62,63,67]. Anti-A-haltige Seren zeigen oft etwas höhere Titer mit Tn-positiven 0-oder B-Erythrozyten als Seren von AB-Spendern [67,70].…”

Section: Die Tn-polyagglutinabilität Und Das Erworbene A-ähnliche Antunclassified

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Erworbene Veränderungen der erythrozytären AB0-Merkmale

Strobel¹

2000

Transfus Med Hemother

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Objective: Pathological changes of the ABO antigens on red blood cells are rare events, but they are important in blood group serology because of the risk of false results in ABO typing. This review is designed to show these pathological changes and the problems in ABO testing caused by them, especially if monoclonal reagents are used. Sources: Selected literature and own experiences. Results: The most relevant pathological changes of the ABO antigens are: 1) The depression of the A- and/or B-antigen on some or (nearly) all red blood cells of some patients with leukemia or myeolodysplastic syndrome. This change is caused by a reduced activity of ABH glycosyltransferases. 2) The acquired B-antigen in some pa-tients with gastrointestinal diseases and/or bacteremia. It is caused by a deacetylation of the A-antigen leading to a B-like antigen. 3) The ‘acquired A-like antigen’ in cases of Tn polyagglutinability which is caused by the cross-reactivity of some anti-A reagents with the Tn antigen. It has been found in cases of leukemia, but also in healthy persons. Conclusions: Although reagents of high quality are used for ABO typing, testing for ABO isoantibodies in the serum is still indispensable. Monoclonal antibodies that are cross-reactive with the acquired B-antigen or with Tn-positive red blood cells should not be used for ABO typing.

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Red Cell Antibodies Against Self‐Antigens, Bound Antigens and Induced Antigens

Klein¹,

Anstee²

2005

Mollison's Blood Transfusion in Clinical Medicine

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An Example of Polyagglutinability Due to the Tn Antigen

Cited by 63 publications

References 7 publications

Comparison of the carbohydrate‐binding specificities of seven N‐acetyl‐D‐galactosamine‐recognizing lectins

Comparison of the carbohydrate‐binding specificities of seven N‐acetyl‐D‐galactosamine‐recognizing lectins

Erworbene Veränderungen der erythrozytären AB0-Merkmale

Red Cell Antibodies Against Self‐Antigens, Bound Antigens and Induced Antigens

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