Effects of Sialic Acid Substitutions on Recognition by Sambucus nigra Agglutinin and Maackia amurensis Hemagglutinin

2002 ◽  
Vol 303 (1) ◽  
pp. 98-104 ◽  
Author(s):  
Els C.M. Brinkman-Van der Linden ◽  
Justin L. Sonnenburg ◽  
Ajit Varki
Keyword(s):  
Sialic Acid ◽  
Sambucus Nigra ◽  
Maackia Amurensis ◽  
Sambucus Nigra Agglutinin

scholarly journals α2,6-Linked sialic acid acts as a receptor for Feline calicivirus

2007 ◽  
Vol 88 (1) ◽  
pp. 177-186 ◽  
Author(s):  
Amanda D. Stuart ◽  
T. David K. Brown
Keyword(s):  
Sialic Acid ◽  
Adhesion Molecule ◽  
Sodium Periodate ◽  
Metabolic Inhibitors ◽  
Feline Calicivirus ◽  
Sambucus Nigra ◽  
Virus Binding ◽  
Maackia Amurensis ◽  
The Family

Feline calicivirus (FCV) is a major causative agent of respiratory disease in cats. It is also one of the few cultivatable members of the family Caliciviridae. It has recently been reported that FCV binding is in part due to interaction with junction adhesion molecule-A. This report describes the characterization of additional receptor components for FCV. Chemical treatment of cells with sodium periodate showed that FCV recognized carbohydrate moieties on the surface of permissive cells. Enzymic treatment with Vibrio cholerae neuraminidase demonstrated that sialic acid was a major determinant of virus binding. Further characterization using linkage-specific lectins from Maackia amurensis and Sambucus nigra revealed that FCV recognized sialic acid with an α2,6 linkage. Using various proteases and metabolic inhibitors, it was shown that α2,6-linked sialic acid recognized by FCV is present on an N-linked glycoprotein.

The content of immunomodulatory glycoepitopes in seminal plasma glycoproteins of fertile and infertile men

2019 ◽  
Vol 31 (3) ◽  
pp. 579
Author(s):  
Anna Kałuża ◽  
Mirosława Ferens-Sieczkowska ◽  
Beata Olejnik ◽  
Justyna Kołodziejczyk ◽  
Mariusz Zimmer ◽  
...  
Keyword(s):  
Sialic Acid ◽  
Seminal Plasma ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Specific Antigen ◽  
Mass Spectrometry Analysis ◽  
Spectrometry Analysis ◽  
Ulex Europaeus ◽  
Maackia Amurensis ◽  
Sambucus Nigra Agglutinin

According to a concept of fetoembryonic defence, protein–carbohydrate interaction may be involved in the regulation of maternal immunity that prevents rejection of allograft spermatozoa, embryo and fetus. In the present study we focussed on the evaluation of the expression of glycoepitopes that may be of crucial importance in this process: LewisY (LeY) and LewisX (LeX) as well as terminal sialylation. Polyacrylamide gel electrophoresis with sodium dodecyl sulphate was used to separate seminal plasma samples of fertile (n=10) and infertile (n=103) men; these were then probed with lectins specific to fucose (Lotus tetragonolobus agglutinin and Ulex europaeus agglutinin) and sialic acid (Sambucus nigra agglutinin and Maackia amurensis agglutinin). Differential expression of α2,3-bound sialic acid was found in six out of seven analysed bands, whereas differences in the other analysed glycoepitopes were found in fewer numbers of bands. Mass spectrometry analysis focussed on the identification of proteins carrying glycans with immunomodulatory epitopes, including fibronectin, lactoferrin, clusterin, zinc-α2-glycoprotein, prostate acid phosphatase and prostate-specific antigen; these should be submitted to further detailed analysis.

scholarly journals Purification and partial characterization of a novel lectin from elder (Sambucus nigra L.) fruit

1991 ◽  
Vol 278 (3) ◽  
pp. 667-671 ◽  
Author(s):  
L Mach ◽  
W Scherf ◽  
M Ammann ◽  
J Poetsch ◽  
W Bertsch ◽  
...  
Keyword(s):  
Sialic Acid ◽  
Amino Acid ◽  
Carbohydrate Specificity ◽  
Sambucus Nigra ◽  
Acid Glycoprotein ◽  
High Affinity ◽  
Sambucus Nigra Agglutinin ◽  
Sds Page ◽  
Molecular Masses

A previously unknown haemagglutinin, named Sambucus nigra agglutinin-III (SNA-III), has been purified from the fruit of the elder (Sambucus nigra). Whereas elder bark agglutinin I (SNA-I) is highly specific for terminal alpha 2,6-linked sialic acid residues, SNA-III displays a high affinity for oligosaccharides containing exposed N-acetylgalactosamine and galactose residues. Different N-terminal sequences and the amino acid composition distinguish the fruit lectin from elder bark agglutinin II (SNA-II), which shows a similar carbohydrate specificity. The 40-fold higher affinity of SNA-III for asialofetuin than for human asialo-alpha 1-acid glycoprotein and human asialotransferrin respectively suggests a preference for O-linked glycans. SNA-III occurs mainly as a monomeric glycoprotein, but tends to form di- and oligo-meric aggregates. This aggregation seems to mediate the multivalent interaction, leading to agglutination. SDS/PAGE revealed two major polypeptides with apparent molecular masses of 32 and 33 kDa respectively. This heterogeneity is probably a result of proteolysis in the C-terminal region. Binding to concanavalin A and susceptibility to peptide: N-glycosidase F indicated the presence of N-glycosidically linked oligosaccharides.

scholarly journals Carbohydrate characterization of purified thyroxine-binding globulin by lectin blot and isoelectric focusing

2003 ◽  
Vol 22 (4) ◽  
pp. 319-323 ◽  
Author(s):  
Ivana Petrovic ◽  
Svetlana Savin-Zegarac ◽  
Ivona Baricevic ◽  
Dubravka Cvejic
Keyword(s):  
Sialic Acid ◽  
Isoelectric Focusing ◽  
Blot Analysis ◽  
Wheat Germ ◽  
Sambucus Nigra ◽  
Thyroxine Binding Globulin ◽  
Sambucus Nigra Agglutinin ◽  
Lectin Blot ◽  
Wheat Germ Lectin

The structure of carbohydrate moiety of purified thyroxine-binding globulin (TBG) was examined by lectin blot and isoelectric focusing (IEF). In lectin blot, TBG reacted positively with the following lectins: Sambucus nigra agglutinin (SNA I), Ricinus commuais agglutinin (RCA I), wheat germ lectin (WGA), phytoheamagglutinin (PHA) and pea lectin (PSA). The obtained results indicate that purified TBG contains N-linked oligosaccharide chains consisting of mannose, galactose, N-acetylglucosamine and sialic acid. Isoelectric focusing of TBG at pl 4.2-4.6 revealed three bands, which confirmed that isolated TBG had retained its structure with?out desialylation. Lectin blot analysis and IEF can be considered to be useful tools in the study of TBG glycosylation.

scholarly journals Increased Sialylation of Anti-Thomsen-Friedenreich Antigen (CD176) Antibodies in Patients with Gastric Cancer: A Diagnostic and Prognostic Potential

2014 ◽  
Vol 2014 ◽  
pp. 1-11 ◽  
Author(s):  
Oleg Kurtenkov ◽  
Jelena Izotova ◽  
Kersti Klaamas ◽  
Boris Sergeyev
Keyword(s):  
Gastric Cancer ◽  
Sialic Acid ◽  
Cancer Detection ◽  
Disease Stage ◽  
Sambucus Nigra ◽  
Serum Samples ◽  
Specific Antibodies ◽  
Sambucus Nigra Agglutinin ◽  
Moderate Sensitivity ◽  
And Gender

Aim. To study whether alterations in the sialylation of antibodies (Ab) specific to the Thomsen-Friedenreich (TF) glycotope have a diagnostic and prognostic potential in gastric cancer.Methods. Serum samples were taken from patients with gastric carcinoma(n=142)and controls(n=61). The level of TF-specific antibodies and their sialylation was detected using ELISA with synthetic TF-polyacrylamide conjugate as antigen and sialic acid-specificSambucus nigra agglutinin(SNA).Results. The level of TF-specific IgM was significantly decreased in cancer compared with controls(P≤0.001). Cancer patients showed a higher level of SNA binding to anti-TF IgM and IgA(P≤0.001)irrespective of disease stage, tumor morphology, and gender. Changes in the SNA/Ab index demonstrated moderate sensitivity (66–71%) and specificity (60–73%) for stomach cancer. The best diagnostic accuracy (100%) was achieved in 29% patients with high SNA binding and low anti-TF IgM level. This subset of patients demonstrated the poorest survival.Conclusion. Our findings are the first evidence that the increased sialylation of TF-specific Abs combined with a low level of anti-TF IgM is strongly linked to gastric cancer and patients survival, which can be used as a novel biomarker for cancer detection and prognosis.

scholarly journals Increase of MAL-II Binding Alpha2,3-Sialylated Glycan Is Associated with 5-FU Resistance and Short Survival of Cholangiocarcinoma Patients

Medicina ◽  
2019 ◽  
Vol 55 (12) ◽  
pp. 761 ◽  
Author(s):  
Sasiprapa Wattanavises ◽  
Atit Silsirivanit ◽  
Kanlayanee Sawanyawisuth ◽  
Ubon Cha’on ◽  
Sakda Waraasawapati ◽  
...  
Keyword(s):  
Cell Lines ◽  
Bile Ducts ◽  
Lectin Histochemistry ◽  
Positive Staining ◽  
Sambucus Nigra ◽  
Short Survival ◽  
Maackia Amurensis ◽  
Sambucus Nigra Agglutinin ◽  
Maackia Amurensis Lectin ◽  
Chemosensitivity Assays

Background and objectives: Sialylation plays important roles in tumor progression. Our present study aimed to demonstrate the alteration of sialylation and its role in cholangiocarcinoma (CCA). Materials and Methods: The α2,3- and α2,6-sialylation in CCA tissue was analyzed by lectin-histochemistry using Maackia amurensis lectin-II (MAL-II) and Sambucus nigra agglutinin (SNA). CCA cell lines were treated with the pan-sialylation inhibitor 3Fax-peracetyl-Neu5Ac (3F-Sia) followed by proliferation and chemosensitivity assays. Results: MAL-II binding α2,3-Sialylated Glycan (MAL-SG) and SNA binding α2,6-Sialylated Glycan (SNA-SG) were both elevated in CCA compared with hyperplastic/dysplastic (HP/DP) and normal bile ducts (NBD). The positive staining for MAL-SG or SNA-SG were found in 82% (61/74) of the CCA cases. Higher expression of MAL-SG in CCA was associated with shorter survival of the patients. The median survival of patients with high and low MAL-SG were 167 and 308 days, respectively, with overall survival of 233 days, suggesting the involvement of MAL-SG in CCA progression. MAL-SG expression of CCA cell lines was markedly decreased after treatment with 3F-Sia for 48 to 72 h. While proliferation of CCA cells were not affected by 3F-Sia treatment, their susceptibility to 5-fluorouracil (5-FU) was significantly enhanced. These results suggest that sialylation is involved in the development of 5-FU resistance and the sialylation inhibitor 3F-Sia can be used as a chemosensitizer for CCA. Conclusions: Sialylation is critically involved in the development of chemoresistance of CCA, and sialylation inhibitors may be used as a chemosensitizer in CCA treatment.

scholarly journals The investigation of the changes in the surface glycoconjugates using two different spheroid models of breast cancer cells and availability assessment of these spheroid models for rapid diagnosis

2021 ◽  
Vol 38 (3) ◽  
pp. 266-271
Author(s):  
Yosun MATER ◽  
Günnur DEMİRCAN
Keyword(s):  
Breast Cancer ◽  
Cell Culture ◽  
Sialic Acid ◽  
Cancer Cell ◽  
Breast Cancer Cell ◽  
Wheat Germ Agglutinin ◽  
Wheat Germ ◽  
Sialic Acids ◽  
Maackia Amurensis ◽  
Maackia Amurensis Lectin

The importance of early cancer diagnosis has led to development of many different diagnostic methods. In this context, the studies investigating the presence and amount of sugar residues to use as indicators in the identification of cancer cell type have become prominent. In the present study, sialic acids found on the membrane surfaces of ER (+) MCF-7 and ER (-) MDA-MB-231 breast cancer cell lines were labeled using three-dimensional (3D) cell culture (Spheroid) model as the closest method to the patient sample, thus its natural environment, among the cell culture methods. These sugar units that play a role in regulation of important immune characteristics such as recognition, binding and metastasis were made visualizable by applying fluorescent-labeled lectins such as FITC-(Wheat Germ Agglutinin) specifically binding to sialic acid units (GlcNAc, Neu5Ac) including particularly ß-GlcNAc and FITC-(Maackia Amurensis-Lectin-1) specifically binding to Galß4GlcNAc type sialic acids. These glycan units were specifically labeled with FITC-(Maackia Amurensis-Lectin-1) and FITC- (Wheat Germ Agglutinin) and radiation intensities were analyzed relatively. The two different breast cancer cell cultures were compared with respect to change in the amounts of sialic acid residues containing α-2,3- and α-2,6 bonds using fluorescent-labeled lectins. In the present study, we have performed a precise, accurate and rapid determination of the sugar content in the different breast cancer cell surface lines by means of fluorescent-labeled lectins and carried out a relative comparison between the micrographs.

Sialic Acid-Binding Motif of Maackia amurensis Lectins

1997 ◽  
Vol 121 (4) ◽  
pp. 756-761 ◽  
Author(s):  
K. Yamamoto ◽  
Y. Konami ◽  
T. Irimura
Keyword(s):  
Sialic Acid ◽  
Binding Motif ◽  
Maackia Amurensis ◽  
Sialic Acid Binding
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