scholarly journals Comparison of docking methods for carbohydrate binding in calcium-dependent lectins and prediction of the carbohydrate binding mode to sea cucumber lectin CEL-III

2008 ◽  
Vol 34 (4) ◽  
pp. 469-479 ◽  
Author(s):  
A. Nurisso ◽  
S. Kozmon ◽  
A. Imberty
Keyword(s):  
Sea Cucumber ◽  
Binding Mode ◽  
Carbohydrate Binding ◽  
Calcium Dependent

Genomic analysis of C-type lectins

2002 ◽  
Vol 69 ◽  
pp. 59-72 ◽  
Author(s):  
Kurt Drickamer ◽  
Andrew J. Fadden
Keyword(s):  
Biological Effects ◽  
Cell Signalling ◽  
Genomic Analysis ◽  
Binding Activity ◽  
Immunoglobulin Superfamily ◽  
Carbohydrate Binding ◽  
Carbohydrate Recognition ◽  
Calcium Dependent ◽  
Binding Domains ◽  
Carbohydrate Recognition Domains

Many biological effects of complex carbohydrates are mediated by lectins that contain discrete carbohydrate-recognition domains. At least seven structurally distinct families of carbohydrate-recognition domains are found in lectins that are involved in intracellular trafficking, cell adhesion, cell–cell signalling, glycoprotein turnover and innate immunity. Genome-wide analysis of potential carbohydrate-binding domains is now possible. Two classes of intracellular lectins involved in glycoprotein trafficking are present in yeast, model invertebrates and vertebrates, and two other classes are present in vertebrates only. At the cell surface, calcium-dependent (C-type) lectins and galectins are found in model invertebrates and vertebrates, but not in yeast; immunoglobulin superfamily (I-type) lectins are only found in vertebrates. The evolutionary appearance of different classes of sugar-binding protein modules parallels a development towards more complex oligosaccharides that provide increased opportunities for specific recognition phenomena. An overall picture of the lectins present in humans can now be proposed. Based on our knowledge of the structures of several of the C-type carbohydrate-recognition domains, it is possible to suggest ligand-binding activity that may be associated with novel C-type lectin-like domains identified in a systematic screen of the human genome. Further analysis of the sequences of proteins containing these domains can be used as a basis for proposing potential biological functions.

scholarly journals An Adhesive Interface for the Non-Clustered δ1 Protocadherin-1 Involved in Respiratory Diseases

2018 ◽  
Author(s):  
Debadrita Modak ◽  
Marcos Sotomayor
Keyword(s):  
Respiratory Diseases ◽  
Large Family ◽  
Binding Mode ◽  
Hantavirus Infection ◽  
Airway Epithelial ◽  
Binding Assays ◽  
Calcium Dependent ◽  
Classical Cadherins ◽  
Adhesive Proteins ◽  
Homophilic Adhesion

ABSTRACTCadherins form a large family of calcium-dependent adhesive proteins involved in morphogenesis, cell differentiation, and neuronal connectivity. Non-clustered δ1 protocadherins form a cadherin subgroup of proteins with seven extracellular cadherin (EC) repeats and cytoplasmic domains distinct from those of classical cadherins. The non-clustered δ1 protocadherins mediate homophilic adhesion and have been implicated in various diseases including asthma, autism, and cancer. Here we present X-ray crystal structures of Protocadherin-1 (PCDH1), a δ1-protocadherin member essential for New World hantavirus infection that is typically expressed in the brain, airway epithelium, skin keratinocytes, and lungs. The structures suggest a binding mode that involves antiparallel overlap of repeats EC1 to EC4. Mutagenesis combined with binding assays and biochemical experiments validated this mode of adhesion. Overall, these results reveal the molecular mechanism underlying adhesiveness of PCDH1 and δ1-protocadherins, also shedding light on PCDH1’s role in maintaining airway epithelial integrity, the loss of which causes respiratory diseases.

scholarly journals Circular Permutation Provides an Evolutionary Link between Two Families of Calcium-dependent Carbohydrate Binding Modules

2010 ◽  
Vol 285 (41) ◽  
pp. 31742-31754 ◽  
Author(s):  
Cedric Montanier ◽  
James E. Flint ◽  
David N. Bolam ◽  
Hefang Xie ◽  
Ziyuan Liu ◽  
...  
Keyword(s):  
Circular Permutation ◽  
Carbohydrate Binding ◽  
Calcium Dependent ◽  
Carbohydrate Binding Modules

scholarly journals SapL1: A New Target Lectin for the Development of Antiadhesive Therapy Against Scedosporium apiospermum

2020 ◽  
Author(s):  
Dania Martínez-Alarcón ◽  
Jean-Philippe Bouchara ◽  
Roland J. Pieters ◽  
Annabelle Varrot
Keyword(s):  
Biochemical Characterization ◽  
Present Report ◽  
Binding Mode ◽  
Host Cells ◽  
Titration Calorimetry ◽  
Carbohydrate Binding ◽  
Scedosporium Apiospermum ◽  
X Ray Crystallography ◽  
Opportunistic Fungal Pathogen

AbstractScedosporium apiospermum is an emerging opportunistic fungal pathogen responsible for life-threatening infections in immunocompromised patients. This fungus exhibits limited susceptibility to all current antifungals and, due its emerging character, its pathogeny and virulence factors remain largely unknown. Carbohydrate binding proteins such as lectins are involved in host-pathogen interactions and may constitute valuable therapeutic targets to inhibit microbial adhesion to the host cells by using carbohydrate mimics. However, such lectins are still unidentified in S. apiospermum. Here, we present the first report of the identification and characterization of a lectin from S. apiospermum named SapL1. SapL1 is homologous to the conidial surface lectin FleA from Aspergillus fumigatus known to be involved in the adhesion to host glycoconjugates present in human lung epithelium. The present report includes a detailed strategy to achieve SapL1 soluble expression in bacteria, its biochemical characterization, an analysis of its specificity and affinity by glycan arrays and isothermal titration calorimetry (ITC), as well as the structural characterization of its binding mode by X–ray crystallography. The information gathered here contribute to the understanding of glycosylated surface recognition by Scedosporium species and is essential for the design and development of antiadhesive glycodrugs targeting SapL1.

scholarly journals Structural and Biochemical Analyses of Glycoside Hydrolase Families 5 and 26 β-(1,4)-Mannanases from Podospora anserina Reveal Differences upon Manno-oligosaccharide Catalysis

2013 ◽  
Vol 288 (20) ◽  
pp. 14624-14635 ◽  
Author(s):  
Marie Couturier ◽  
Alain Roussel ◽  
Anna Rosengren ◽  
Philippe Leone ◽  
Henrik Stålbrand ◽  
...  
Keyword(s):  
Glycoside Hydrolase ◽  
Enzymatic Degradation ◽  
Plant Cell Wall ◽  
Biological Process ◽  
Binding Mode ◽  
Podospora Anserina ◽  
Carbohydrate Binding ◽  
Substrate Specificities ◽  
Biochemical Analyses ◽  
Classical Mode

The microbial deconstruction of the plant cell wall is a key biological process that is of increasing importance with the development of a sustainable biofuel industry. The glycoside hydrolase families GH5 (PaMan5A) and GH26 (PaMan26A) endo-β-1,4-mannanases from the coprophilic ascomycete Podospora anserina contribute to the enzymatic degradation of lignocellulosic biomass. In this study, P. anserina mannanases were further subjected to detailed comparative analysis of their substrate specificities, active site organization, and transglycosylation capacity. Although PaMan5A displays a classical mode of action, PaMan26A revealed an atypical hydrolysis pattern with the release of mannotetraose and mannose from mannopentaose resulting from a predominant binding mode involving the −4 subsite. The crystal structures of PaMan5A and PaMan26A were solved at 1.4 and 2.85 Å resolution, respectively. Analysis of the PaMan26A structure supported strong interaction with substrate at the −4 subsite mediated by two aromatic residues Trp-244 and Trp-245. The PaMan26A structure appended to its family 35 carbohydrate binding module revealed a short and proline-rich rigid linker that anchored together the catalytic and the binding modules.

Carbohydrate-binding modules from family 11: Understanding the binding mode of polysaccharides

2008 ◽  
Vol 108 (11) ◽  
pp. 2030-2040 ◽  
Author(s):  
N. F. Brás ◽  
N. M. F. S. A. Cerqueira ◽  
P. A. Fernandes ◽  
M. J. Ramos
Keyword(s):  
Binding Mode ◽  
Carbohydrate Binding ◽  
Carbohydrate Binding Modules

Calmodulin binds to the STAS domain of SLC26A5 prestin with a calcium-dependent, one-lobe, binding mode

2021 ◽  
pp. 107714
Author(s):  
Elisa Costanzi ◽  
Alice Coletti ◽  
Barbara Zambelli ◽  
Antonio Macchiarulo ◽  
Massimo Bellanda ◽  
...  
Keyword(s):  
Binding Mode ◽  
Calcium Dependent ◽  
Stas Domain

scholarly journals Phosphomannosyl-derivatized beads detect a receptor involved in lymphocyte homing.

1987 ◽  
Vol 104 (3) ◽  
pp. 713-723 ◽  
Author(s):  
T A Yednock ◽  
L M Stoolman ◽  
S D Rosen
Keyword(s):  
Selection Procedure ◽  
Blood Stream ◽  
Carbohydrate Binding ◽  
High Endothelial Venules ◽  
Vitro Assay ◽  
Flow Cytofluorometry ◽  
Calcium Dependent ◽  
Surface Probe ◽  
Mouse Lymphocytes

Recirculating lymphocytes initiate extravasation from the blood stream by binding to specialized high endothelial venules (HEV) within peripheral lymph nodes (PN) and other secondary lymphoid organs. We have previously reported that lymphocyte attachment to PN HEV is selectively inhibited by mannose-6-phosphate (M6P) and related carbohydrates (Stoolman, L. M., T. S. Tenforde, and S. D. Rosen, 1984, J. Cell Biol., 99:1535-1540). In the present study, we employ a novel cell-surface probe consisting of fluorescent beads derivatized with PPME, a M6P-rich polysaccharide. PPME beads directly identify a carbohydrate-binding receptor on the surface of mouse lymphocytes. In every way examined, lymphocyte attachment to PPME beads (measured by flow cytofluorometry) mimics the interaction of lymphocytes with PN HEV (measured in the Stamper-Woodruff in vitro assay): both interactions are selectively inhibited by the same panel of structurally related carbohydrates, are calcium-dependent, and are sensitive to mild treatment of the lymphocytes with trypsin. In addition, thymocytes and a thymic lymphoma, S49, bind poorly to PPME beads in correspondence to their weak ability to bind to HEV. When the S49 cell line was subjected to a selection procedure with PPME beads, the ability of the cells to bind PPME beads, as well as their ability to bind to PN HEV, increased six- to eightfold. We conclude that a carbohydrate-binding receptor on mouse lymphocytes, detected by PPME beads, is involved in lymphocyte attachment to PN HEV.

scholarly journals ERGIC-53 is a functional mannose-selective and calcium-dependent human homologue of leguminous lectins.

1996 ◽  
Vol 7 (3) ◽  
pp. 483-493 ◽  
Author(s):  
C Itin ◽  
A C Roche ◽  
M Monsigny ◽  
H P Hauri
Keyword(s):  
Secretory Pathway ◽  
Carbohydrate Binding ◽  
Dependent Manner ◽  
Calcium Dependent ◽  
New Class ◽  
Early Secretory Pathway ◽  
Sequence Homologies ◽  
Sorting Receptor ◽  
Lectin Family ◽  
Specificity Domain

Based on sequence homologies with leguminous lectins, the intermediate compartment marker ERGIC-53 was proposed to be a member of a putative new class of animal lectins associated with the secretory pathway. Independent, a promyelocytic protein, MR60, was purified by mannose-column chromatography, and a cDNA was isolated that matched MR60 peptide sequences. This cDNA was identical to that of ERGIC-53 and homologies with the animal lectin family of the galectins were noticed. Not all peptide sequences of MR60, however, were found in ERGIC-53, raising the possibility that another protein associated with ERGIC-53 may possess the lectin activity. Here, we provide the first direct evidence for a lectin function of ERGIC-53. Overexpressed ERGIC-53 binds to a mannose column in a calcium-dependent manner and also co-stains with mannosylated neoglycoprotein in a morphological binding assay. By using a sequential elution protocol we show that ERGIC-53 has selectivity for mannose and low affinity for glucose and GlcNAc, but no affinity for galactose. To experimentally address the putative homology of ERGIC-53 to leguminous lectins, a highly conserved protein family with an invariant asparagine essential for carbohydrate binding, we substituted the corresponding asparagine in ERGIC-53. This mutation, as well as a mutation affecting a second site in the putative carbohydrate recognition domain, abolished mannose-column binding and co-staining with mannosylated neoglycoprotein. These findings establish ERGIC-53 as a lectin and provide functional evidence for its relationship to leguminous lectins. Based on its monosaccharide specificity, domain organization, and recycling properties, we propose ERGIC-53 to function as a sorting receptor for glyco-proteins in the early secretory pathway.

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