A Detailed Lectin Analysis of IgG Glycosylation, Demonstrating Disease Specific Changes in Terminal Galactose and N-acetylglucosamine

Bond, Angela; Alavi, Azita; Axford, John S.; Bourke, B; Bruckner, F E; Kerr, M. A.; Maxwell, J. D.; Tweed, Karen; Weldon, Michael; Youinou, Pierre; Hay, Frank C.

doi:10.1006/jaut.1996.0104

Cited by 80 publications

(57 citation statements)

References 22 publications

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“…Altered glycosylation is known to have important consequences for pathogenesis (3,7), as well as insect resistance (37). In some cases, modifications of specific carbohydrates mask recognition epitopes used by pathogens (41).…”

Section: Discussionmentioning

confidence: 99%

Altered Glycosylation of 63- and 68-Kilodalton Microvillar Proteins in Heliothis virescens Correlates with Reduced Cry1 Toxin Binding, Decreased Pore Formation, and Increased Resistance to Bacillus thuringiensis Cry1 Toxins

Jurat-Fuentes¹,

Gould

Adang

2002

Appl Environ Microbiol

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The binding and pore formation abilities of Cry1A and Cry1Fa Bacillus thuringiensis toxins were analyzed by using brush border membrane vesicles (BBMV) prepared from sensitive (YDK) and resistant (YHD2) strains of Heliothis virescens.125 I-labeled Cry1Aa, Cry1Ab, and Cry1Ac toxins did not bind to BBMV from the resistant YHD2 strain, while specific binding to sensitive YDK vesicles was observed. Binding assays revealed a reduction in Cry1Fa binding to BBMV from resistant larvae compared to Cry1Fa binding to BBMV from sensitive larvae. In agreement with this reduction in binding, neither Cry1A nor Cry1Fa toxin altered the permeability of membrane vesicles from resistant larvae, as measured by a light-scattering assay. Ligand blotting experiments performed with BBMV and 125 I-Cry1Ac did not differentiate sensitive larvae from resistant larvae. Iodination of BBMV surface proteins suggested that putative toxin-binding proteins were exposed on the surface of the BBMV from resistant insects. BBMV protein blots probed with the N-acetylgalactosamine-specific lectin soybean agglutinin (SBA) revealed altered glycosylation of 63-and 68-kDa glycoproteins but not altered glycosylation of known Cry1 toxin-binding proteins in YHD2 BBMV. The F1 progeny of crosses between sensitive and resistant insects were similar to the sensitive strain when they were tested by toxin-binding assays, light-scattering assays, and lectin blotting with SBA. These results are evidence that a dramatic reduction in toxin binding is responsible for the increased resistance and cross-resistance to Cry1 toxins observed in the YHD2 strain of H. virescens and that this trait correlates with altered glycosylation of specific brush border membrane glycoproteins.

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Section: Discussionmentioning

confidence: 99%

Altered Glycosylation of 63- and 68-Kilodalton Microvillar Proteins in Heliothis virescens Correlates with Reduced Cry1 Toxin Binding, Decreased Pore Formation, and Increased Resistance to Bacillus thuringiensis Cry1 Toxins

Jurat-Fuentes¹,

Gould

Adang

2002

Appl Environ Microbiol

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“…[44][45][46] Moreover, high serum levels of these IgG glycoforms are associated with further autoimmune diseases, including Crohn's disease, juvenile onset chronic arthritis, SLE complicated by Sjo¨gren's syndrome and tuberculosis. [47][48][49] The presence of agalactosyl glycoforms in RA has been shown to be associated with lowered galactosyltransferase (GTase) activity. 50 Inflammation in the joints was once thought to be mediated by MBL binding to clustered IgG-G0 and IgG-G0 ICs, which had been deposited in the synovial tissue, subsequently initiating the MBLdependent pathway of complement activation.…”

Section: Galactosylationmentioning

confidence: 99%

Sweet but dangerous – the role of immunoglobulin G glycosylation in autoimmunity and inflammation

Biermann

Griffante

Podolska

et al. 2016

Lupus

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Glycosylation is well-known to modulate the functional capabilities of immunoglobulin G (IgG)-mediated cellular and humoral responses. Indeed, highly sialylated and desialylated IgG is endowed with anti-and pro-inflammatory activities, respectively, whereas fully deglycosylated IgG is a rather lame duck, with no effector function besides toxin neutralization. Recently, several studies revealed the impact of different glycosylation patterns on the Fc part and Fab fragment of IgG in several autoimmune diseases, including systemic lupus erythematosus (SLE) and rheumatoid arthritis (RA). Here, we provide a synoptic update summarizing the most important aspects of antibody glycosylation, and the current progress in this field. We also discuss the therapeutic options generated by the modification of the glycosylation of IgG in a potential treatment for chronic inflammatory diseases. Lupus (2016) 25, 934-942.

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“…They correlate with the disease activity and fall during remission periods (Rook et al, 1991). High levels of desialylated IgG-G0 are also characteristic for other disorders: Crohn's disease, SLE complicated by Sjogren's syndrome, and tuberculosis (Parekh et al, 1985(Parekh et al, , 1989Bond et al, 1997). The enzyme EndoS from Streptococcus pyogenes that cleaves IgG glycan between two GlcNAc residues, was used for ''making autoantibodies safe'' (Scanlan et al, 2008).…”

Section: Discussionmentioning

confidence: 99%

Antibody‐mediated sialidase activity in blood serum of patients with multiple myeloma

Bilyy

Tomin

Mahorivska

et al. 2010

J of Molecular Recognition

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Cell surface sialylation is known to be tightly connected with tumorigenicity, invasiveness, metastatic potential, clearance of aged cells, while the sialylation of IgG molecules determines their anti-inflammatory properties. Four sialidases - hydrolytic enzymes responsible for cleavage of sialic residues - were described in different cellular compartments. However, sialidases activity in body fluids, and specifically in blood serum, remains poorly studied. Here, we characterize first known IgG antibodies possessing sialidase-like activity in blood serum of multiple myeloma (MM) patients. Ig fractions were precipitated with ammonium sulfate (50% of saturation) from blood serum of 12 healthy donors and 14 MM patients, and screened for the presence of sialidase activity by using 4-MUNA (2'-(4-methylumbelliferyl)-α-D-N-acetylneuraminic acid) as substrate. High level of sialidase activity was detected in the MM patients, but not in healthy donors. Subsequent antibody purification by protein-G affinity chromatography and HPLC size exclusion chromatography at acidic conditions demonstrated that sialidase activity was attributable to IgG molecules. Sialidase activity was also specific for (Fab)(2) fragment of IgG and blocked by sialidase inhibitor DANA. Sialidase activity of IgG molecule was also confirmed by in gel assay for cleavage of sialidase substrate. Kinetic parameters of the catalysis reaction were described by Michaelis-Menten equation with K(m) = 44.4-108 µM and k(cat) = 2.7-23.1 min(-1). The action of IgG possessing sialidase-like activity towards human red blood cells resulted in a subsequent increase in their agglutination by the peanut agglutinin, that confirms their desialylation by the studied IgG. This is the first demonstration of the intrinsic sialidase activity of IgG isolated from blood serum of MM patients.

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A Detailed Lectin Analysis of IgG Glycosylation, Demonstrating Disease Specific Changes in Terminal Galactose and N-acetylglucosamine

Cited by 80 publications

References 22 publications

Altered Glycosylation of 63- and 68-Kilodalton Microvillar Proteins in Heliothis virescens Correlates with Reduced Cry1 Toxin Binding, Decreased Pore Formation, and Increased Resistance to Bacillus thuringiensis Cry1 Toxins

Altered Glycosylation of 63- and 68-Kilodalton Microvillar Proteins in Heliothis virescens Correlates with Reduced Cry1 Toxin Binding, Decreased Pore Formation, and Increased Resistance to Bacillus thuringiensis Cry1 Toxins

Sweet but dangerous – the role of immunoglobulin G glycosylation in autoimmunity and inflammation

Antibody‐mediated sialidase activity in blood serum of patients with multiple myeloma

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