Sequencing of chondroitin sulfate oligosaccharides using a novel exolyase from a marine bacterium that degrades hyaluronan and chondroitin sulfate/dermatan sulfate

2017 ◽  
Vol 474 (22) ◽  
pp. 3831-3848 ◽  
Author(s):  
Wenshuang Wang ◽  
Xiaojuan Cai ◽  
Naihan Han ◽  
Wenjun Han ◽  
Kazuyuki Sugahara ◽  
...  
Keyword(s):  
Chondroitin Sulfate ◽  
Marine Bacterium ◽  
Dermatan Sulfate ◽  
Specific Activity ◽  
Structural Complexity ◽  
Complex Structures ◽  
Biological Functions ◽  
Chemical Structures ◽  
Lyase Activity ◽  
Sugar Chains

Glycosaminoglycans (GAGs) are a family of chemically heterogeneous polysaccharides that play important roles in physiological and pathological processes. Owing to the structural complexity of GAGs, their sophisticated chemical structures and biological functions have not been extensively studied. Lyases that cleave GAGs are important tools for structural analysis. Although various GAG lyases have been identified, exolytic lyases with unique enzymatic property are urgently needed for GAG sequencing. In the present study, a putative exolytic GAG lyase from a marine bacterium was recombinantly expressed and characterized in detail. Since it showed exolytic lyase activity toward hyaluronan (HA), chondroitin sulfate (CS), and dermatan sulfate (DS), it was designated as HCDLase. This novel exolyase exhibited the highest activity in Tris–HCl buffer (pH 7.0) at 30°C. Especially, it showed a specific activity that released 2-aminobenzamide (2-AB)-labeled disaccharides from the reducing end of 2-AB-labeled CS oligosaccharides, which suggest that HCDLase is not only a novel exolytic lyase that can split disaccharide residues from the reducing termini of sugar chains but also a useful tool for the sequencing of CS chains. Notably, HCDLase could not digest 2-AB-labeled oligosaccharides from HA, DS, or unsulfated chondroitin, which indicated that sulfates and bond types affect the catalytic activity of HCDLase. Finally, this enzyme combined with CSase ABC was successfully applied for the sequencing of several CS hexa- and octasaccharides with complex structures. The identification of HCDLase provides a useful tool for CS-related research and applications.

scholarly journals Chondroitin Sulfate/Dermatan Sulfate-Protein Interactions and Their Biological Functions in Human Diseases: Implications and Analytical Tools

2021 ◽  
Vol 9 ◽  
Author(s):  
Bin Zhang ◽  
Lianli Chi
Keyword(s):  
Cell Surface ◽  
Chondroitin Sulfate ◽  
Protein Interactions ◽  
Dermatan Sulfate ◽  
Interaction Analysis ◽  
Structural Complexity ◽  
Protein Characterization ◽  
Biological Functions ◽  
Gag Protein ◽  
Core Proteins

Chondroitin sulfate (CS) and dermatan sulfate (DS) are linear anionic polysaccharides that are widely present on the cell surface and in the cell matrix and connective tissue. CS and DS chains are usually attached to core proteins and are present in the form of proteoglycans (PGs). They not only are important structural substances but also bind to a variety of cytokines, growth factors, cell surface receptors, adhesion molecules, enzymes and fibrillary glycoproteins to execute series of important biological functions. CS and DS exhibit variable sulfation patterns and different sequence arrangements, and their molecular weights also vary within a large range, increasing the structural complexity and diversity of CS/DS. The structure-function relationship of CS/DS PGs directly and indirectly involves them in a variety of physiological and pathological processes. Accumulating evidence suggests that CS/DS serves as an important cofactor for many cell behaviors. Understanding the molecular basis of these interactions helps to elucidate the occurrence and development of various diseases and the development of new therapeutic approaches. The present article reviews the physiological and pathological processes in which CS and DS participate through their interactions with different proteins. Moreover, classic and emerging glycosaminoglycan (GAG)-protein interaction analysis tools and their applications in CS/DS-protein characterization are also discussed.

scholarly journals Investigation of Action Pattern of a Novel Chondroitin Sulfate/Dermatan Sulfate 4-O-Endosulfatase

2020 ◽  
Author(s):  
Wenshuang Wang ◽  
Cédric Przybylski ◽  
Xiaojuan Cai ◽  
Chrystel Lopin-Bon ◽  
Runmiao Jiao ◽  
...  
Keyword(s):  
Chondroitin Sulfate ◽  
Marine Bacterium ◽  
Catalytic Mechanism ◽  
Dermatan Sulfate ◽  
Structural Characteristics ◽  
Action Pattern ◽  
Substrate Specificities ◽  
Substrate Size ◽  
Function Relationship ◽  
Relationship Of

Recently, a novel CS/DS 4-O-endosulfatase was identified from a marine bacterium and its catalytic mechanism was investigated further (Wang, W., et.al (2015) J. Biol. Chem. 290, 7823-7832; Wang, S., et.al (2019) Front. Microbiol. 10:1309). In the study herein, we provide new insight about the structural characteristics of substrate which determine the activity of this enzyme. The substrate specificities of the 4-O-endosulfatase were probed by using libraries of structure-defined CS/DS oligosacccharides issued from synthetic and enzymatic sources. We found that this 4-O-endosulfatase effectively remove the 4-O-sulfate of disaccharide sequences GlcUAβ1-3GalNAc(4S) or GlcUAβ1-3GalNAc(4S,6S) in all tested hexasaccharides. The sulfated GalNac residue is resistant to the enzyme when adjacent uronic residues are sulfated as shown by the lack of enzymatic desulfation of GlcUAβ1-3GalNAc(4S) connected to a disaccharide GlcUA(2S)β1-3GalNAc(6S) in an octasaccharide. The 3-O-sulfation of GlcUA was also shown to hinder the action of this enzyme. The 4-O-endosulfatase exhibited an oriented action from the reducing to the non-reducing whatever the saturation or not of the non-reducing end. Finally, the activity of the 4-O-endosulfatase decreases with the increase of substrate size. With the deeper understanding of this novel 4-O-endosulfatase, such chondroitin sulfate (CS)/dermatan sulfate (DS) sulfatase is a useful tool for exploring the structure-function relationship of CS/DS.

The chondroitin sulfate/dermatan sulfate 4-O-endosulfatase from marine bacterium Vibrio sp FC509 is a dimeric species: Biophysical characterization of an endosulfatase

Biochimie ◽  
2016 ◽  
Vol 131 ◽  
pp. 85-95 ◽  
Author(s):  
José L. Neira ◽  
Encarnación Medina-Carmona ◽  
José G. Hernández-Cifre ◽  
Laia Montoliu-Gaya ◽  
Ana Cámara-Artigás ◽  
...  
Keyword(s):  
Chondroitin Sulfate ◽  
Marine Bacterium ◽  
Dermatan Sulfate ◽  
Biophysical Characterization

scholarly journals Cloning and Characterization of a Novel Chondroitin Sulfate/Dermatan Sulfate 4-O-Endosulfatase from a Marine Bacterium

2015 ◽  
Vol 290 (12) ◽  
pp. 7823-7832 ◽  
Author(s):  
Wenshuang Wang ◽  
Wenjun Han ◽  
Xingya Cai ◽  
Xiaoyu Zheng ◽  
Kazuyuki Sugahara ◽  
...  
Keyword(s):  
Chondroitin Sulfate ◽  
Marine Bacterium ◽  
Dermatan Sulfate

scholarly journals Research and Application of Chondroitin Sulfate/Dermatan Sulfate-Degrading Enzymes

2020 ◽  
Vol 8 ◽  
Author(s):  
Wenshuang Wang ◽  
Liran Shi ◽  
Yong Qin ◽  
Fuchuan Li
Keyword(s):  
Chondroitin Sulfate ◽  
Dermatan Sulfate ◽  
Structural Complexity ◽  
Medical Application ◽  
Composition Analysis ◽  
Biological Processes ◽  
Functional Studies ◽  
Degrading Enzymes ◽  
Site Of Action ◽  
Basic Studies

Chondroitin sulfate (CS) and dermatan sulfate (DS) are widely distributed on the cell surface and in the extracellular matrix in the form of proteoglycan, where they participate in various biological processes. The diverse functions of CS/DS can be mainly attributed to their high structural variability. However, their structural complexity creates a big challenge for structural and functional studies of CS/DS. CS/DS-degrading enzymes with different specific activities are irreplaceable tools that could be used to solve this problem. Depending on the site of action, CS/DS-degrading enzymes can be classified as glycosidic bond-cleaving enzymes and sulfatases from animals and microorganisms. As discussed in this review, a few of the identified enzymes, particularly those from bacteria, have wildly applied to the basic studies and applications of CS/DS, such as disaccharide composition analysis, the preparation of bioactive oligosaccharides, oligosaccharide sequencing, and potential medical application, but these do not fulfill all of the needs in terms of the structural complexity of CS/DS.

Isolation of a chondroitin sulfate-dermatan sulfate proteoglycan from bovine aorta

1975 ◽  
Vol 171 (1) ◽  
pp. 361-369 ◽  
Author(s):  
Kenneth C. Ehrlich ◽  
Bhandaru Radhakrishnamurthy ◽  
Gerald S. Berenson
Keyword(s):  
Chondroitin Sulfate ◽  
Dermatan Sulfate ◽  
Sulfate Proteoglycan ◽  
Dermatan Sulfate Proteoglycan

scholarly journals Analysis of a large food chemical database: chemical space, diversity, and complexity

F1000Research ◽  
2018 ◽  
Vol 7 ◽  
pp. 993 ◽  
Author(s):  
J. Jesús Naveja ◽  
Mariel P. Rico-Hidalgo ◽  
José L. Medina-Franco
Keyword(s):  
Natural Products ◽  
Chemical Space ◽  
Structural Complexity ◽  
Chemical Diversity ◽  
Chemical Structures ◽  
Novel Approach ◽  
Chemical Database ◽  
Protein Interactome ◽  
Limited Basis ◽  
Future Direction

Background: Food chemicals are a cornerstone in the food industry. However, its chemical diversity has been explored on a limited basis, for instance, previous analysis of food-related databases were done up to 2,200 molecules. The goal of this work was to quantify the chemical diversity of chemical compounds stored in FooDB, a database with nearly 24,000 food chemicals. Methods: The visual representation of the chemical space of FooDB was done with ChemMaps, a novel approach based on the concept of chemical satellites. The large food chemical database was profiled based on physicochemical properties, molecular complexity and scaffold content. The global diversity of FooDB was characterized using Consensus Diversity Plots. Results: It was found that compounds in FooDB are very diverse in terms of properties and structure, with a large structural complexity. It was also found that one third of the food chemicals are acyclic molecules and ring-containing molecules are mostly monocyclic, with several scaffolds common to natural products in other databases. Conclusions: To the best of our knowledge, this is the first analysis of the chemical diversity and complexity of FooDB. This study represents a step further to the emerging field of “Food Informatics”. Future study should compare directly the chemical structures of the molecules in FooDB with other compound databases, for instance, drug-like databases and natural products collections. An additional future direction of this work is to use the list of 3,228 polyphenolic compounds identified in this work to enhance the on-going polyphenol-protein interactome studies.

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