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Protein-Carbohydrate Interactions
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Protein-Carbohydrate Interactions

A special issue of Molecules (ISSN 1420-3049). This special issue belongs to the section "Bioorganic Chemistry".

Deadline for manuscript submissions: closed (30 May 2017) | Viewed by 39720

Special Issue Editor

Prof. Dr. Roland J. Pieters

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Guest Editor
Division of Medicinal Chemistry and Chemical Biology, Utrecht Institute for Pharmaceutical Sciences, Faculty of Science, Utrecht University, Universiteitsweg 99, 3584 CG Utrecht, The Netherlands
Interests: protein-carbohydrate interactions; lectins; glycosidases; carbohydrate microarrays; multivalency; bacterial adhesion; viral adhesion; O-GlcNAcylation
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Protein–carbohydrate interactions play important roles in biological processes. On the surface of cells, carbohydrates communicate information to the outside, and, for example, are of importance in the immune system. In addition to on the cell surface, inside the cell, O-GlcNAcylation of proteins is of great importance in cell regulation. In most cases, the recognition of carbohydrates is performed by carbohydrate-recognizing proteins, such as lectins, but also antibodies and carbohydrate processing enzymes.  In many cases, protein carbohydrate recognition is responsible for disease, for example, through adhesion of microbial pathogens or toxins. In addition to this, carbohydrates and complementary proteins also provide opportunities to treat numerous diseases, for example, in the immune system and cancer.

In order to better understand the biology and communication aspects of protein carbohydrate recognition, new selective bioactive molecules need to be explored, such as enzyme inhibitors based on close transition state mimicry, bisubstrate inhibitors, and adhesion inhibitors. In addition to the better understanding such molecules will yield, medicinal applications may also come within reach. Thus far, few drugs based on carbohydrates have made it to market. Nevertheless, the hurdles, such as the lack of oral availability, renal excretion, and degradation and weak binding, have all been overcome in select cases.  Approaches, such as glycomimetics, prodrugs, and binding to plasma proteins, can help the drug properties of carbohydrate derivatives, while multivalency can enhance the binding affinities. In this Special Issue, we welcome contributions in all mentioned areas, as well as those reporting on novel tools to study protein–carbohydrate interactions, as well as the application of computational tools.

Prof. Dr. Roland Pieters
Guest Editor

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Keywords

  • protein–carbohydrate interactions
  • lectins
  • glycosidases
  • glycosyl transferases
  • glycobiology
  • glycomics
  • carbohydrate microarrays
  • multivalency
  • bacterial adhesion
  • viral adhesion

Published Papers (6 papers)

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Research

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11125 KiB  
Article
Engineering of a Potent Recombinant Lectin-Toxin Fusion Protein to Eliminate Human Pluripotent Stem Cells
by Hiroaki Tateno, Fumi Minoshima and Sayoko Saito
Molecules 2017, 22(7), 1151; https://0-doi-org.brum.beds.ac.uk/10.3390/molecules22071151 - 10 Jul 2017
Cited by 17 | Viewed by 4636
Abstract
The use of human pluripotent stem cells (hPSCs) such as human embryonic stem cells (hESCs) and human induced pluripotent stem cells (hiPSCs) in regenerative medicine is hindered by their tumorigenic potential. Previously, we developed a recombinant lectin-toxin fusion protein of the hPSC-specific lectin [...] Read more.
The use of human pluripotent stem cells (hPSCs) such as human embryonic stem cells (hESCs) and human induced pluripotent stem cells (hiPSCs) in regenerative medicine is hindered by their tumorigenic potential. Previously, we developed a recombinant lectin-toxin fusion protein of the hPSC-specific lectin rBC2LCN, which has a 23 kDa catalytic domain (domain III) of Pseudomonas aeruginosa exotoxin A (rBC2LCN-PE23). This fusion protein could selectively eliminate hPSCs following its addition to the cell culture medium. Here we conjugated rBC2LCN lectin with a 38 kDa domain of exotoxin A containing domains Ib and II in addition to domain III (PE38). The developed rBC2LCN-PE38 fusion protein could eliminate 50% of 201B7 hPSCs at a concentration of 0.003 μg/mL (24 h incubation), representing an approximately 556-fold higher activity than rBC2LCN-PE23. Little or no effect on human fibroblasts, human mesenchymal stem cells, and hiPSC-derived hepatocytes was observed at concentrations lower than 1 μg/mL. Finally, we demonstrate that rBC2LCN-PE38 selectively eliminates hiPSCs from a mixed culture of hiPSCs and hiPSC-derived hepatocytes. Since rBC2LCN-PE38 can be prepared from soluble fractions of E. coli culture at a yield of 9 mg/L, rBC2LCN-PE38 represents a practical reagent to remove human pluripotent stem cells residing in cultured cells destined for transplantation. Full article
(This article belongs to the Special Issue Protein-Carbohydrate Interactions)
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1313 KiB  
Article
L1210 Cells Overexpressing ABCB1 Drug Transporters Are Resistant to Inhibitors of the N- and O-glycosylation of Proteins
by Lucia Pavlikova, Mario Seres, Milan Hano, Viera Bohacova, Ivana Sevcikova, Tomas Kyca, Albert Breier and Zdena Sulova
Molecules 2017, 22(7), 1104; https://0-doi-org.brum.beds.ac.uk/10.3390/molecules22071104 - 03 Jul 2017
Cited by 6 | Viewed by 4703
Abstract
Overexpression of P-glycoprotein (P-gp, drug transporter) in neoplastic cells is the most frequently observed molecular cause of multidrug resistance. Here, we show that the overexpression of P-gp in L1210 cells leads to resistance to tunicamycin and benzyl 2-acetamido-2-deoxy-α-d-galactopyranoside (GalNAc-α-O-benzyl). [...] Read more.
Overexpression of P-glycoprotein (P-gp, drug transporter) in neoplastic cells is the most frequently observed molecular cause of multidrug resistance. Here, we show that the overexpression of P-gp in L1210 cells leads to resistance to tunicamycin and benzyl 2-acetamido-2-deoxy-α-d-galactopyranoside (GalNAc-α-O-benzyl). Tunicamycin induces both glycosylation depression and ubiquitination improvement of P-gp. However, the latter is not associated with large increases in molecular mass as evidence for polyubiquitination. Therefore, P-gp continues in maturation to an active membrane efflux pump rather than proteasomal degradation. P-gp-positive L1210 cells contain a higher quantity of ubiquitin associated with cell surface proteins than their P-gp-negative counterparts. Thus, P-gp-positive cells use ubiquitin signaling for correct protein folding to a higher extent than P-gp-negative cells. Elevation of protein ubiquitination after tunicamycin treatment in these cells leads to protein folding rather than protein degradation, resulting at least in the partial lack of cell sensitivity to tunicamycin in L1210 cells after P-gp expression. In contrast to tunicamycin, to understand why P-gp-positive cells are resistant to GalNAc-α-O-benzyl, further research is needed. Full article
(This article belongs to the Special Issue Protein-Carbohydrate Interactions)
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14083 KiB  
Article
Sites for Dynamic Protein-Carbohydrate Interactions of O- and C-Linked Mannosides on the E. coli FimH Adhesin
by Mohamed Touaibia, Eva-Maria Krammer, Tze C. Shiao, Nao Yamakawa, Qingan Wang, Anja Glinschert, Alex Papadopoulos, Leila Mousavifar, Emmanuel Maes, Stefan Oscarson, Gerard Vergoten, Marc F. Lensink, René Roy and Julie Bouckaert
Molecules 2017, 22(7), 1101; https://0-doi-org.brum.beds.ac.uk/10.3390/molecules22071101 - 03 Jul 2017
Cited by 22 | Viewed by 7191
Abstract
Antagonists of the Escherichia coli type-1 fimbrial adhesin FimH are recognized as attractive alternatives for antibiotic therapies and prophylaxes against acute and recurrent bacterial infections. In this study α-d-mannopyranosides O- or C-linked with an alkyl, alkene, alkyne, thioalkyl, amide, [...] Read more.
Antagonists of the Escherichia coli type-1 fimbrial adhesin FimH are recognized as attractive alternatives for antibiotic therapies and prophylaxes against acute and recurrent bacterial infections. In this study α-d-mannopyranosides O- or C-linked with an alkyl, alkene, alkyne, thioalkyl, amide, or sulfonamide were investigated to fit a hydrophobic substituent with up to two aryl groups within the tyrosine gate emerging from the mannose-binding pocket of FimH. The results were summarized into a set of structure-activity relationships to be used in FimH-targeted inhibitor design: alkene linkers gave an improved affinity and inhibitory potential, because of their relative flexibility combined with a favourable interaction with isoleucine-52 located in the middle of the tyrosine gate. Of particular interest is a C-linked mannoside, alkene-linked to an ortho-substituted biphenyl that has an affinity similar to its O-mannosidic analog but superior to its para-substituted analog. Docking of its high-resolution NMR solution structure to the FimH adhesin indicated that its ultimate, ortho-placed phenyl ring is able to interact with isoleucine-13, located in the clamp loop that undergoes conformational changes under shear force exerted on the bacteria. Molecular dynamics simulations confirmed that a subpopulation of the C-mannoside conformers is able to interact in this secondary binding site of FimH. Full article
(This article belongs to the Special Issue Protein-Carbohydrate Interactions)
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6331 KiB  
Article
Complex Coacervation of Soy Proteins, Isoflavones and Chitosan
by Yu-Hsuan Hsiao, Sheng-Yang Hsia, Yin-Ching Chan and Jung-Feng Hsieh
Molecules 2017, 22(6), 1022; https://0-doi-org.brum.beds.ac.uk/10.3390/molecules22061022 - 20 Jun 2017
Cited by 9 | Viewed by 7178
Abstract
In this study, the chitosan-induced coacervation of soy protein-isoflavone complexes in soymilk was investigated. Most of the soymilk proteins, including β-conglycinin (7S), glycinin (11S), and isoflavones, were found to coacervate into the soymilk pellet fraction (SPF) following the addition of 0.5% chitosan. The [...] Read more.
In this study, the chitosan-induced coacervation of soy protein-isoflavone complexes in soymilk was investigated. Most of the soymilk proteins, including β-conglycinin (7S), glycinin (11S), and isoflavones, were found to coacervate into the soymilk pellet fraction (SPF) following the addition of 0.5% chitosan. The total protein in the soymilk supernatant fraction (SSF) decreased from 18.1 ± 0.3 mg/mL to 1.6 ± 0.1 mg/mL, and the pH values decreased slightly, from 6.6 ± 0.0 to 6.0 ± 0.0. The results of SDS-PAGE revealed that the 7S α’, 7S α, 7S β, 11S A3, and 11S acidic subunits, as well as the 11S basic proteins in the SSF, decreased to 0.7 ± 0.5%, 0.2 ± 0.1%, 0.1 ± 0.0%, 0.2 ± 0.2%, 0.2 ± 0.2% and 0.3 ± 0.2%, respectively. We also found that isoflavones in the SSF, including daidzein, glycitein, and genistein, decreased to 9.6 ± 2.3%, 5.7 ± 0.9% and 5.9 ± 1.5%, respectively. HPLC analysis indicated that isoflavones mixed with soy proteins formed soy protein-isoflavone complexes and were precipitated into the SPF by 0.5% chitosan. Full article
(This article belongs to the Special Issue Protein-Carbohydrate Interactions)
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1503 KiB  
Article
Investigation of the Maillard Reaction between Polysaccharides and Proteins from Longan Pulp and the Improvement in Activities
by Miao-Miao Han, Yang Yi, Hong-Xun Wang and Fei Huang
Molecules 2017, 22(6), 938; https://0-doi-org.brum.beds.ac.uk/10.3390/molecules22060938 - 05 Jun 2017
Cited by 47 | Viewed by 6206
Abstract
The purpose of this study was to investigate the Maillard reaction between polysaccharides and proteins from longan pulp and the effects of reaction on their in vitro activities. The polysaccharide-protein mixtures of fresh longan pulp (LPPMs) were co-prepared by an alkali extraction–acid precipitation [...] Read more.
The purpose of this study was to investigate the Maillard reaction between polysaccharides and proteins from longan pulp and the effects of reaction on their in vitro activities. The polysaccharide-protein mixtures of fresh longan pulp (LPPMs) were co-prepared by an alkali extraction–acid precipitation method. They were then dry-heated under controlled conditions for monitoring the characterization of the Maillard reaction by the measurement of the free amino group content, ultraviolet-visible spectrum, Fourier transform infrared spectrum and molecular weight distribution. All the physicochemical analyses indicated the development of the Maillard reaction between polysaccharides and proteins. The in vitro activity evaluation indicated that the Maillard reaction could effectively enhance the antioxidant, antitumor and immunostimulating activities of LPPMs. The enhancement of 1,1-diphenyl-2-picrylhydrazyl radical scavenging activity and ferric reducing antioxidant power displayed both a positive correlation with the reaction time (p < 0.05). LPPMs dry-heated for three days obtained relatively strong inhibitory activity against HepG2 cells and SGC7901 cells, as well as strong immunostimulating effects on the nitric oxide production and tumor necrosis factor α secretion of macrophages. Maillard-type intermacromolecular interaction is suggested to be an effective and controllable method for improving the functional activities of polysaccharides and proteins from longan pulp. Full article
(This article belongs to the Special Issue Protein-Carbohydrate Interactions)
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Review

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4951 KiB  
Review
CH/π Interactions in Carbohydrate Recognition
by Vojtěch Spiwok
Molecules 2017, 22(7), 1038; https://0-doi-org.brum.beds.ac.uk/10.3390/molecules22071038 - 23 Jun 2017
Cited by 91 | Viewed by 8909
Abstract
Many carbohydrate-binding proteins contain aromatic amino acid residues in their binding sites. These residues interact with carbohydrates in a stacking geometry via CH/π interactions. These interactions can be found in carbohydrate-binding proteins, including lectins, enzymes and carbohydrate transporters. Besides this, many non-protein aromatic [...] Read more.
Many carbohydrate-binding proteins contain aromatic amino acid residues in their binding sites. These residues interact with carbohydrates in a stacking geometry via CH/π interactions. These interactions can be found in carbohydrate-binding proteins, including lectins, enzymes and carbohydrate transporters. Besides this, many non-protein aromatic molecules (natural as well as artificial) can bind saccharides using these interactions. Recent computational and experimental studies have shown that carbohydrate–aromatic CH/π interactions are dispersion interactions, tuned by electrostatics and partially stabilized by a hydrophobic effect in solvated systems. Full article
(This article belongs to the Special Issue Protein-Carbohydrate Interactions)
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