Recognition profile of Bauhinia purpurea agglutinin (BPA)

Wu, Albert M.; Wu, June H.; Liu, Jiahua; Singh, T. N.

doi:10.1016/j.lfs.2003.08.031

Cited by 35 publications

(24 citation statements)

References 52 publications

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“…Gal-specific lectins 1. T, Galβ1→3GalNAc (T a or T b )-Peanut, Bauhinia purpurea alba [10], Abrus precatorius [11], Agaricus bisporus [12], Sclerotium rolfsii [13], Artocarpus integrifolia (jacalin) [14], Artocarpus lakoocha [15], and Maclura pomifera [16], ricin [17] and Morus nigra (Morniga G) [18]. 2.…”

Section: Grouping Lectins Based On Recognition Of Monosaccharides Andmentioning

confidence: 99%

“…In this system, the amount of reagents required is greatly reduced (about 1,000-times) as compared to that needed for precipitation assays. When starting experiments with a new lectin, it is important to select a proper coating concentration of the target glycoform, because frequently with increasing coating concentration binding of the lectin increases to some point, and then strongly decreases [10,49,66]. Optimal binding usually occurred when solution used for coating contained the ligand at 0.2-2μg/ml concentration (10-100ng/50μl/well).…”

Section: Biotin/avidin Based Microtiter Plate Enzyme-linked Lectinosomentioning

confidence: 99%

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Lectins as tools in glycoconjugate research

et al. 2008

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Lectins are ubiquitous proteins of nonimmune origin, present in plants, microorganisms, animals and humans which specifically bind defined monosugars or oligosaccharide structures. Great progress has been made in recent years in understanding crucial roles played by lectins in many biological processes. Elucidation of carbohydrate specificity of human and animal lectins is of great importance for better understanding of these processes. Long before the role of carbohydrate-protein interactions had been explored, many lectins, mostly of plant origin, were identified, characterized and applied as useful tools in studying glycoconjugates. This review focuses on the specificity-based lectin classification and the methods of measuring lectin-carbohydrate interactions, which are used for determination of lectin specificity or for identification and characterization of glycoconjugates with lectins of known specificity. The most frequently used quantitative methods are shortly reviewed and the methods elaborated and used in our laboratories, based on biotinylated lectins, are described. These include the microtiter plate enzyme-linked lectinosorbent assay, lectinoblotting and lectin-glycosphingolipid interaction on thin-layer plates. Some chemical modifications of lectin ligands on the microtiter plates and blots (desialylation, Smith degradation, beta-elimination), which extend the applicability of these methods, are also described.

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Section: Grouping Lectins Based On Recognition Of Monosaccharides Andmentioning

confidence: 99%

Section: Biotin/avidin Based Microtiter Plate Enzyme-linked Lectinosomentioning

confidence: 99%

Lectins as tools in glycoconjugate research

et al. 2008

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“…Several techniques have been developed over the last few years for the study of carbohydrate-lectin interactions, ranging from hemagglutination [9], enzyme-linked lectinosorbent assays [10] or, more recently, microarrays [11]. In the latter case, different chemistries for attaching oligosaccharides to a solid matrix have been described [12], ranging from reductive amination (with ring opening of reducing-end monosaccharides), to oxime ligation (with equilibrium between ring-opened forms) [13], or to hydrazide (with predominantly β-cyclic forms) [14].…”

Section: Introductionmentioning

confidence: 99%

Neo-glycopeptides: the importance of sugar core conformation in oxime-linked glycoprobes for interaction studies

et al. 2008

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Carbohydrate binding proteins, such as lectins, are crucial in numerous biological recognition processes. While binding may be mediated by a single monosaccharide, several lectins have shown exquisite epimer and linkage recognition indicating that a larger structure is essential for optimal interaction. Several approaches have been described for their detailed study, including lectinosorbent assays, microarrays and surface plasmon resonance (SPR). Most of these approaches ignore that the aglycon-bound monosaccharide is often in a non-natural conformation that affects the occurring binding event. In this paper we demonstrate that oxime-bound glycans, employed in such approaches, occur predominantly in the open form (approximately 70%). Through the use of a secondary amine, the aglycon-bound monosaccharide in the resulting neo-glycopeptide probe is forced into the ring-form. Resulting structures were analyzed by means of nuclear magnetic resonance and differential derivatization experiments. The impact of ring closure was further demonstrated through interaction studies using SPR and various lectins with distinct binding specificities.

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“…Eine enorme Zahl verschiedener GalNAc bindender Lectine von Pflanzen und Tieren wurde verwendet, um die Expression des Tn-Antigens zu erforschen. Diese schließen die Pflanzenlectine Dolichos-biflorus-Agglutinin (DBA), [44] Marrubiumcandidissimum-Agglutinin, [45] Maclura-pomifera-Lectin (MPL), [46] Salvia-horminum-Agglutinin (SHA), [47] Salviasclarea-Agglutinin (SSA), [48] Salvia-bogotensis-Lectin, [49] Artocarpus-integrifolia-Lectin (Jacalin), [50] Bauhinia-purpurea-Agglutinin (BPA), [51,52] das B4-Isolectin von Vicia-villosaAgglutinin (VVA-B4), [53] Soja-hispida-Lectin, [54] Moluccellalaevis-Lectin (MLL) [55] und das aus Schnecken isolierte Helixpomatia-Agglutinin (HPA) ein. [48,56,57] Auch das Fehlen einer Bindung durch andere Lectine wurde genutzt, um die mög-liche Expression der Tn/STn-Antigene (STn-Antigen = Sialyl-Tn-Antigen; Neu5Aca2-6GalNAca1-O-Ser/Thr) zu untersuchen.…”

Section: Nachweis Des Tn-antigensunclassified

Das Tn‐Antigen – strukturell einfach und biologisch komplex

Otto

Cummings

2011

Angewandte Chemie

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Die Glycoproteine tierischer Zellen enthalten vielfältige Glycanstrukturen, die co‐ und/oder posttranslational an die Proteine angeheftet werden. Mehr als zwanzig verschiedene Bindungsarten von Glycanen an Proteine sind bekannt, doch sind N‐Glycane (gebunden an Asn) und O‐Glycane (gebunden an Ser/Thr) die häufigsten. Ein abnormes O‐Glycan, das bei Krebs und anderen menschlichen Erkrankungen auftritt, ist das Tn‐Antigen. Es hat eine einfache Struktur, bestehend aus einem N‐Acetyl‐D‐galactosamin, das α‐glycosidisch an einen Serin‐ oder Threoninrest gebunden ist. Das Tn‐Antigen war eines der ersten Glycokonjugate, die chemisch synthetisiert wurden. Es wird normalerweise von einer spezifischen Galactosyltransferase, der T‐Synthase, im Golgi‐Apparat modifiziert. Die Expression aktiver T‐Synthase hängt vom molekularen Chaperon Cosmc ab, dessen Gen auf dem X‐Chromosom liegt. Genmutationen, die die Funktion von T‐Synthase, Cosmc oder anderen an der O‐Glycosylierung beteiligten Faktoren beeinträchtigen, können zur Expression des Tn‐Antigens führen. Da dieses bei einer Reihe von Krankheiten auftritt, besteht großes Interesse, es für die Entwicklung von Impfstoffen und anderen therapeutischen Ansätzen zu nutzen.

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Recognition profile of Bauhinia purpurea agglutinin (BPA)

Cited by 35 publications

References 52 publications

Lectins as tools in glycoconjugate research

Lectins as tools in glycoconjugate research

Neo-glycopeptides: the importance of sugar core conformation in oxime-linked glycoprobes for interaction studies

Das Tn‐Antigen – strukturell einfach und biologisch komplex

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