A Guide to the Carbohydrate Specificities of Applied Lectins-2

Wu, Albert M.; Song, Shuh-Chyung; Tsai, Ming‐Shao; Herp, Anthony

doi:10.1007/978-1-4615-1267-7_37

Cited by 31 publications

(32 citation statements)

References 195 publications

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“…Previous investigations have identified a complex carbohydrate of ASOR, which is composed of the tri-and tetraantennary oligosaccharides containing Gal␤1,4GlcNAc-linked units at the nonreducing end (12,13). The Gal␤1,4GlcNAc sugar moiety is a core element of the blood group substance-related complex carbohydrates, being referred as type II sugar structures (17). There was no detectable antibody reactivity to agalacto-orosomucoid (AGOR), a degalactosyl derivative of ASOR, which differs from ASOR solely by the absence of the terminal galactosyl sugar residue.…”

Section: Experiments and Resultsmentioning

confidence: 99%

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Glycan arrays lead to the discovery of autoimmunogenic activity of SARS-CoV

Wang

2004

Physiological Genomics

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Wang, Denong, and Jiahai Lu. Glycan arrays lead to the discovery of autoimmunogenic activity of SARS-CoV. Physiol Genomics 18: 245-248, 2004. First published May 25, 2004 10.1152/ physiolgenomics.00102.2004.-Using carbohydrate microarrays, we characterized the carbohydrate binding activity of SARS-CoV neutralizing antibodies elicited by an inactivated SARS-CoV vaccine. In these antibodies, we detected undesired autoantibody reactivity specific for the carbohydrate moieties of an abundant human serum glycoprotein asialo-orosomucoid (ASOR). This observation provides important clues for the selection of specific immunologic probes to examine whether SARS-CoV expresses antigenic structures that mimic the host glycan. We found that lectin PHA-L (Phaseolus vulgaris L.), which is specific for a defined complex carbohydrate of ASOR, stained the SARS-CoV-infected cells specifically and intensively. Taken together, we present immunologic evidence that a carbohydrate structure of SARS-CoV shares antigenic similarity with host glycan complex carbohydrates. The experimental approaches we applied in this study are likely applicable for the identification of immunologic targets of other viral pathogens. microarray; carbohydrate; autoantigen; antibody and lectin; asialoorosomucoid SARS-COV IS A NEWLY IDENTIFIED human coronavirus that caused an outbreak of severe acute respiratory syndrome (SARS) (4,8,11). Although substantial efforts have been made to study the etiologic agent of the disease, the carbohydrate structures of SARS-CoV remain largely uncharacterized. In this study, we introduced a glycan array-based approach to probe the carbohydrate-based antigenic structures of SARS-CoV. More specifically, we constructed glycan arrays to display carbohydrate antigens of defined structures and then applied these tools to detect carbohydrate-specific antibody "fingerprints" that were elicited by a SARS vaccine. We reasoned that if SARS-CoV expressed antigenic carbohydrate structures, then immunizing animals using the whole virus-based vaccines would have the possibility to elicit antibodies specific for these structures. In addition, if SARS-CoV displayed a carbohydrate structure that mimics host cellular glycans, then vaccinated animals may develop antibodies with autoimmune reactivity to their corresponding cellular glycans. EXPERIMENTS AND RESULTSOur laboratory has established a practical bioarray platform for the construction of carbohydrate microarrays (14,16). Using this technology, we constructed a glycan array (Fig. 1, A and B) 1 to display a collection of 51 carbohydrate antigens, including both microbial polysaccharides and cellular glycan complex carbohydrates. Blood group substances A, B, O, Lewis, I, and i antigens, and their precursors and structural derivatives were specially included. These complex carbohydrates are covalently attached to cellular proteins by either Oor N-glycosylation linkages as protein posttranslational modifications or linked to a membrane-bound lipid molecule. Therefore, scanning the antibody...

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Section: Experiments and Resultsmentioning

confidence: 99%

“…D: image of glycan array II stained by lectin GS-1-B4 (Griffonia simplicifolia I-B4 agglutinin). This lectin was considered to be highly specific for Gal␣1,3Gal, a xentogenic epitope of porcine tissues (17). Distance between adjacent microspots is 375 m, center to center.…”

Section: Experiments and Resultsmentioning

confidence: 99%

Glycan arrays lead to the discovery of autoimmunogenic activity of SARS-CoV

Wang

2004

Physiological Genomics

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“…For example, the glycan chains attached to the membrane-associated glycoproteins (e.g., the CD phenotypic markers) vary considerably depending on the lymphocyte subsets (e.g., T cells, B cells, or NK cells) but also on the functional state of cells (growth, differentiation, activation/resting) [6,7]. Similarly, plant lectins display pronounced differences regarding their ability to recognize and bind complex N-glycans present on the lymphocyte surface [8]. In this respect, it should be kept in mind that lectins with a similar (nominal) specificity toward simple sugars (such as mannose or galactose) often can interact with a different set of N-glycans [9,10].…”

Section: Introductionmentioning

confidence: 99%

Two structurally identical mannose-specific jacalin-related lectins display different effects on human T lymphocyte activation and cell death

Benoist

Culerrier

Poiroux

et al. 2009

Journal of Leukocyte Biology

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Plant lectins displaying similar single sugar-binding specificity and identical molecular structure might present various biological effects. To explore this possibility, the effects on human lymphocytes of two mannose-specific and structurally closely related lectins, Morniga M from Morus nigra and artocarpin from Artocarpus integrifolia were investigated. In silico analysis revealed that Morniga M presents a more largely open carbohydrate-binding cavity than artocarpin, probably allowing interactions with a broader spectrum of carbohydrate moieties. In vitro, Morniga M interacted strongly with the lymphocyte surface and was uptaken quickly by cells. Morniga M and artocarpin triggered the proliferation and activation of human T and NK lymphocytes. A minority of B lymphocytes was activated in artocarpin-treated culture, whereas Morniga M favored the emergence of CD4ϩ CD8ϩ T lymphocytes. Moreover, cell death occurred in activated PBMC, activated T lymphocytes, and Jurkat T leukemia cells incubated with Morniga M only. The biological effects of both lectins were dependent on carbohydrate recognition. The Morniga M-induced cell death resulted, at least in part, from caspase-dependent apoptosis and FADD-dependent receptor-mediated cell death. Finally, Morniga M, but not artocarpin, triggered AICD of T lymphocytes. In conclusion, both lectins trigger lymphocyte activation, but only Morniga M induces cell death. In spite of similar in vitro mannose-binding specificities and virtually identical structure, only Morniga M probably interacts with carbohydrate moieties bound to molecules able to induce cell death. The present data suggest that subtle alterations in N-glycans can distinguish activation and cell death molecules at the lymphocyte surface.

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“…However, lectins with an exclusive or preferential specificity for Tn and T antigens are rather scarcely distributed among higher plants. A survey of plant lectins that were described as T or Tn specific is presented in Table 1 [11,12]. Hitherto, T or Tn specific lectins have been found in the families Amaranthaceae, Fabaceae, Lamiaceae, Moraceae and Orchidaceae.…”

Section: Overview Of Plant Lectins Described As Tn and T Specificmentioning

confidence: 99%