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Marine Drugs
Special Issues
Marine Glycomics 2nd Edition
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Marine Glycomics 2nd Edition

A special issue of Marine Drugs (ISSN 1660-3397).

Deadline for manuscript submissions: 30 April 2024 | Viewed by 10943

Special Issue Editors

Dr. Marco Gerdol

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Guest Editor
Department of Life Sciences, University of Trieste, Via Licio Giorgieri 5, 34127 Trieste, Italy
Interests: antimicrobial peptides; bivalves; defense peptides; immunity; molecular evolution
Special Issues, Collections and Topics in MDPI journals
Dr. Yuki Fujii

E-Mail Website
Guest Editor
Graduate School of Pharmaceutical Sciences, Nagasaki International University, 2825-7 Huis Ten Bosch, Sasebo, Nagasaki 859-3298, Japan
Interests: glycobiology; apoptosis; biochemistry; marine biology; marine lectin
Special Issues, Collections and Topics in MDPI journals
Prof. Dr. Yasuhiro Ozeki

E-Mail Website
Guest Editor
School of Sciences, Yokohama City University, 22-2, Seto, Kanazawa-Ku, Yokohama 236-0027, Japan
Interests: glycobiology; lectins; marine invertebrates
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Following the success of our 1st Special Issue on the topic of “Marine Glycomics, https://www.mdpi.com/journal/marinedrugs/special_issues/Marine_Glycomics”, we would like to renew the call for a 2nd Special Issue, which will welcome the submission of original manuscripts dealing with the theme of marine glycomics. Although these may include classic glycobiology approaches, studies which make use of bioinformatics for genomic or transcriptomic analyses aimed at the discovery of novel glycan-binding molecules are also welcome.

In the early stages of life and biological evolution, living organisms assembled a limited number of molecules in a bricolage fashion and used them to develop novel biological properties and adapt to new environments. As a fundamental molecule of life, carbohydrates have been exploited as glycans, acquiring a key role as structural determinants in cell-cell recognition processes.

In light of their importance in all living systems, understanding the biological role played by glycan-related molecules in the marine environment has a great potential, both for elucidating the impressive biodiversity of marine organisms and for discovering new drugs. Therefore, glycomics approaches may be focused on giant viruses, archaea, bacteria, protists, algae, fungi, and animals to discover new glycan-related molecules.

These studies might refine the importance of weak molecular interactions via carbohydrate–carbohydrate recognition, a fundamental biological reaction. Along with the elucidation of the biological activities of novel marine glycans, another desirable aim of marine glycomics studies would be to clarify the crucial physiological roles played by lectins in carbohydrate-protein interactions.

The investigation of the correlation between the physiological functions of these molecules and drug efficacy through simulations also represents a sustainable perspective for the design of next-generation drugs based on marine glycan-related molecules, which may be applied in the therapy and diagnostics of cancer, as well as of infectious or lifestyle diseases.

Original research manuscripts, comprehensive review papers, and future perspective articles are all welcome in this Special Issue.

Dr. Marco Gerdol
Dr. Yuki Fujii
Prof. Dr. Yasuhiro Ozeki
Guest Editors

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Marine Drugs is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2900 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • cell signaling
  • deep-sea
  • glycomics
  • infections
  • lectins
  • oligosaccharides
  • origins of life
  • polysaccharides
  • structure of glycans
  • transcriptome

Published Papers (7 papers)

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Research

19 pages, 2783 KiB  
Article
Taxonomic Distribution and Molecular Evolution of Mytilectins
by Marco Gerdol, Daniela Eugenia Nerelli, Nicola Martelossi, Yukiko Ogawa, Yuki Fujii, Alberto Pallavicini and Yasuhiro Ozeki
Mar. Drugs 2023, 21(12), 614; https://doi.org/10.3390/md21120614 - 27 Nov 2023
Viewed by 1383
Abstract
R-type lectins are a widespread group of sugar-binding proteins found in nearly all domains of life, characterized by the presence of a carbohydrate-binding domain that adopts a β-trefoil fold. Mytilectins represent a recently described subgroup of β-trefoil lectins, which have been functionally characterized [...] Read more.
R-type lectins are a widespread group of sugar-binding proteins found in nearly all domains of life, characterized by the presence of a carbohydrate-binding domain that adopts a β-trefoil fold. Mytilectins represent a recently described subgroup of β-trefoil lectins, which have been functionally characterized in a few mussel species (Mollusca, Bivalvia) and display attractive properties, which may fuel the development of artificial lectins with different biotechnological applications. The detection of different paralogous genes in mussels, together with the description of orthologous sequences in brachiopods, supports the formal description of mytilectins as a gene family. However, to date, an investigation of the taxonomic distribution of these lectins and their molecular diversification and evolution was still lacking. Here, we provide a comprehensive overview of the evolutionary history of mytilectins, revealing an ancient monophyletic evolutionary origin and a very broad but highly discontinuous taxonomic distribution, ranging from heteroscleromorphan sponges to ophiuroid and crinoid echinoderms. Moreover, the overwhelming majority of mytilectins display a chimera-like architecture, which combines the β-trefoil carbohydrate recognition domain with a C-terminal pore-forming domain, suggesting that the simpler structure of most functionally characterized mytilectins derives from a secondary domain loss. Full article
(This article belongs to the Special Issue Marine Glycomics 2nd Edition)
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13 pages, 5649 KiB  
Article
Biochemical Insights into a Novel Family 2 Glycoside Hydrolase with Both β-1,3-Galactosidase and β-1,4-Galactosidase Activity from the Arctic
by Dianyi Li, Zheng Wang, Yong Yu, Huirong Li, Wei Luo, Bo Chen, Guoqing Niu and Haitao Ding
Mar. Drugs 2023, 21(10), 521; https://doi.org/10.3390/md21100521 - 29 Sep 2023
Viewed by 1035
Abstract
A novel GH2 (glycoside hydrolase family 2) β-galactosidase from Marinomonas sp. BSi20584 was successfully expressed in E. coli with a stable soluble form. The recombinant enzyme (rMaBGA) was purified to electrophoretic homogeneity and characterized extensively. The specific activity of purified rMaBGA was determined [...] Read more.
A novel GH2 (glycoside hydrolase family 2) β-galactosidase from Marinomonas sp. BSi20584 was successfully expressed in E. coli with a stable soluble form. The recombinant enzyme (rMaBGA) was purified to electrophoretic homogeneity and characterized extensively. The specific activity of purified rMaBGA was determined as 96.827 U mg−1 at 30 °C using ONPG (o-nitrophenyl-β-D-galactopyranoside) as a substrate. The optimum pH and temperature of rMaBGA was measured as 7.0 and 50 °C, respectively. The activity of rMaBGA was significantly enhanced by some divalent cations including Zn2+, Mg2+ and Ni2+, but inhibited by EDTA, suggesting that some divalent cations might play important roles in the catalytic process of rMaBGA. Although the enzyme was derived from a cold-adapted strain, it still showed considerable stability against various physical and chemical elements. Moreover, rMaBGA exhibited activity both toward Galβ-(1,3)-GlcNAc and Galβ-(1,4)-GlcNAc, which is a relatively rare occurrence in GH2 β-galactosidase. The results showed that two domains in the C-terminal region might be contributed to the β-1,3-galactosidase activity of rMaBGA. On account of its fine features, this enzyme is a promising candidate for the industrial application of β-galactosidase. Full article
(This article belongs to the Special Issue Marine Glycomics 2nd Edition)
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25 pages, 6042 KiB  
Article
Species-Specific N-Glycomes and Methylation Patterns of Oysters Crassostrea gigas and Ostrea edulis and Their Possible Consequences for the Norovirus–HBGA Interaction
by Audrey Auger, Shin-Yi Yu, Shih-Yun Guu, Agnès Quéméner, Gabriel Euller-Nicolas, Hiromune Ando, Marion Desdouits, Françoise S. Le Guyader, Kay-Hooi Khoo, Jacques Le Pendu, Frederic Chirat and Yann Guerardel
Mar. Drugs 2023, 21(6), 342; https://doi.org/10.3390/md21060342 - 02 Jun 2023
Viewed by 1459
Abstract
Noroviruses, the major cause of acute viral gastroenteritis, are known to bind to histo-blood group antigens (HBGAs), including ABH groups and Lewis-type epitopes, which decorate the surface of erythrocytes and epithelial cells of their host tissues. The biosynthesis of these antigens is controlled [...] Read more.
Noroviruses, the major cause of acute viral gastroenteritis, are known to bind to histo-blood group antigens (HBGAs), including ABH groups and Lewis-type epitopes, which decorate the surface of erythrocytes and epithelial cells of their host tissues. The biosynthesis of these antigens is controlled by several glycosyltransferases, the distribution and expression of which varies between tissues and individuals. The use of HBGAs as ligands by viruses is not limited to humans, as many animal species, including oysters, which synthesize similar glycan epitopes that act as a gateway for viruses, become vectors for viral infection in humans. Here, we show that different oyster species synthesize a wide range of N-glycans that share histo-blood A-antigens but differ in the expression of other terminal antigens and in their modification by O-methyl groups. In particular, we show that the N-glycans isolated from Crassostrea gigas and Ostrea edulis exhibit exquisite methylation patterns in their terminal N-acetylgalactosamine and fucose residues in terms of position and number, adding another layer of complexity to the post-translational glycosylation modifications of glycoproteins. Furthermore, modeling of the interactions between norovirus capsid proteins and carbohydrate ligands strongly suggests that methylation has the potential to fine-tune the recognition events of oysters by virus particles. Full article
(This article belongs to the Special Issue Marine Glycomics 2nd Edition)
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17 pages, 15021 KiB  
Article
A Genomic and Transcriptomic Analysis of the C-Type Lectin Gene Family Reveals Highly Expanded and Diversified Repertoires in Bivalves
by Amaro Saco, Hugo Suárez, Beatriz Novoa and Antonio Figueras
Mar. Drugs 2023, 21(4), 254; https://doi.org/10.3390/md21040254 - 20 Apr 2023
Cited by 6 | Viewed by 1505
Abstract
C-type lectins belong to a widely conserved family of lectins characterized in Metazoa. They show important functional diversity and immune implications, mainly as pathogen recognition receptors. In this work, C-type lectin-like proteins (CTLs) of a set of metazoan species were analyzed, revealing an [...] Read more.
C-type lectins belong to a widely conserved family of lectins characterized in Metazoa. They show important functional diversity and immune implications, mainly as pathogen recognition receptors. In this work, C-type lectin-like proteins (CTLs) of a set of metazoan species were analyzed, revealing an important expansion in bivalve mollusks, which contrasted with the reduced repertoires of other mollusks, such as cephalopods. Orthology relationships demonstrated that these expanded repertoires consisted of CTL subfamilies conserved within Mollusca or Bivalvia and of lineage-specific subfamilies with orthology only between closely related species. Transcriptomic analyses revealed the importance of the bivalve subfamilies in mucosal immunity, as they were mainly expressed in the digestive gland and gills and modulated with specific stimuli. CTL domain-containing proteins that had additional domains (CTLDcps) were also studied, revealing interesting gene families with different conservation degrees of the CTL domain across orthologs from different taxa. Unique bivalve CTLDcps with specific domain architectures were revealed, corresponding to uncharacterized bivalve proteins with putative immune function according to their transcriptomic modulation, which could constitute interesting targets for functional characterization. Full article
(This article belongs to the Special Issue Marine Glycomics 2nd Edition)
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11 pages, 3785 KiB  
Article
Structural Characterization and Effects on Insulin Resistance of a Novel Chondroitin Sulfate from Halaelurus burgeri Skin
by Shiwei Hu, Hongli Zhu, Sichun Chen, Xiaofeng Wan, Yishu Liu, Zhaocai Ren and Shuang Gao
Mar. Drugs 2023, 21(4), 221; https://doi.org/10.3390/md21040221 - 30 Mar 2023
Cited by 3 | Viewed by 1546
Abstract
Several studies have isolated chondroitin sulphate (CHS) from sharks’ jaws or cartilage. However, there has been little research on CHS from shark skin. In the present study, we extracted a novel CHS from Halaelurus burgeri skin, which has a novel chemical structure and [...] Read more.
Several studies have isolated chondroitin sulphate (CHS) from sharks’ jaws or cartilage. However, there has been little research on CHS from shark skin. In the present study, we extracted a novel CHS from Halaelurus burgeri skin, which has a novel chemical structure and bioactivity on improvement in insulin resistance. Results using Fourier transform–infrared spectroscopy (FT-IR), 1H-nuclear magnetic resonance spectroscopy (1H-NMR), and methylation analysis showed that the structure of the CHS was [4)-β-D-GlcpA-(1→3)-β-D-GlcpNAc-(1→]n with 17.40% of sulfate group concentration. Its molecular weight was 238.35 kDa, and the yield was 17.81%. Experiments on animals showed that this CHS could dramatically decrease body weight, reduce blood glucose and insulin levels, lower lipid concentrations both in the serum and the liver, improve glucose tolerance and insulin sensitivity, and regulate serum-inflammatory factors. These results demonstrated that the CHS from H. burgeri skin has a positive effect in reducing insulin resistance because of its novel structure, which provides a significant implication for the polysaccharide as a functional food. Full article
(This article belongs to the Special Issue Marine Glycomics 2nd Edition)
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12 pages, 5654 KiB  
Article
New Data on the Rhamnose-Binding Lectin from the Colonial Ascidian Botryllus schlosseri: Subcellular Distribution, Secretion Mode and Effects on the Cyclical Generation Change
by Giacomo Bovo and Loriano Ballarin
Mar. Drugs 2023, 21(3), 171; https://doi.org/10.3390/md21030171 - 08 Mar 2023
Cited by 1 | Viewed by 1463
Abstract
Botryllus schlosseri in a cosmopolitan ascidian, considered a reliable model organism for studies on the evolution of the immune system. B. schlosseri rhamnose-binding lectin (BsRBL) is synthesised by circulating phagocytes and behaves as an opsonin by interacting with foreign cells or particles and [...] Read more.
Botryllus schlosseri in a cosmopolitan ascidian, considered a reliable model organism for studies on the evolution of the immune system. B. schlosseri rhamnose-binding lectin (BsRBL) is synthesised by circulating phagocytes and behaves as an opsonin by interacting with foreign cells or particles and acting as a molecular bridge between them and the phagocyte surface. Although described in previous works, many aspects and roles of this lectin in Botryllus biology remain unknown. Here, we studied the subcellular distribution of BsRBL during immune responses using light and electron microscopy. In addition, following the hints from extant data, suggesting a possible role of BsRBL in the process of cyclical generation change or takeover, we investigated the effects of interfering with this protein, by injecting a specific antibody in the colonial circulation, starting one day before the generation change. Results confirm the requirement of the lectin for a correct generation change and open new queries on the roles of this lectin in Botryllus biology. Full article
(This article belongs to the Special Issue Marine Glycomics 2nd Edition)
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12 pages, 2528 KiB  
Article
A Comparative Study of Oncolytic Vaccinia Viruses Harboring Different Marine Lectins in Breast Cancer Cells
by Yanrong Zhou, Qianpeng Wang, Qi Ying, Xiaomei Zhang, Ting Ye, Kan Chen and Gongchu Li
Mar. Drugs 2023, 21(2), 77; https://doi.org/10.3390/md21020077 - 23 Jan 2023
Cited by 1 | Viewed by 1674
Abstract
Our previous studies demonstrated that arming vaccinia viruses with marine lectins enhanced the antitumor efficacy in several cancer cells. This study aims to compare the efficacy of oncolytic vaccinia viruses harboring Tachypleus tridentatus lectin (oncoVV-TTL), Aphrocallistes vastus lectin (oncoVV-AVL), white-spotted charr lectin (oncoVV-WCL), [...] Read more.
Our previous studies demonstrated that arming vaccinia viruses with marine lectins enhanced the antitumor efficacy in several cancer cells. This study aims to compare the efficacy of oncolytic vaccinia viruses harboring Tachypleus tridentatus lectin (oncoVV-TTL), Aphrocallistes vastus lectin (oncoVV-AVL), white-spotted charr lectin (oncoVV-WCL), and Asterina pectinifera lectin (oncoVV-APL) in breast cancer cells (BC). These results indicated that oncoVV-AVL elicited the highest anti-tumor effect, followed by oncoVV-APL, while oncoVV-TTL and oncoVV-WCL had lower effects in BC. Further studies showed that apoptosis and replication may work together to enhance the cytotoxicity of oncoVV-lectins in a cell-type dependent manner. TTL/AVL/APL/WCL may mediate multiple pathways, including ERK, JNK, Hippo, and PI3K pathways, to promote oncoVV replication in MDA-MB-231 cells. In contrast, these pathways did not affect oncoVV-TTL/AVL/APL/WCL replication in MCF-7 cells, suggesting that the mechanisms of recombinant viruses in MCF-7 (ER+, PR+) and MDA-MB-231 (TNBC) cells were significantly different. Based on this study, we hypothesized that ER or PR may be responsible for the differences in promoting viral replication and inducing apoptosis between MCF-7 and MDA-MB-231 cells, but the specific mechanism needs to be further explored. In addition, small-molecule drugs targeting key cellular signaling pathways, including MAPK, PI3K/Akt, and Hippo, could be conjunction with oncoVV-AVL to promote breast cancer therapy, and key pathway factors in the JNK and PI3K pathways may be related to the efficacy of oncoVV-APL/TTL/WCL. This study provides a basis for applying oncolytic vaccinia virus in breast carcinoma. Full article
(This article belongs to the Special Issue Marine Glycomics 2nd Edition)
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