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Marine Glycomics 2nd Edition

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

Deadline for manuscript submissions: closed (31 October 2024) | Viewed by 21205

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Dr. Marco Gerdol

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Department of Life Sciences, University of Trieste, Via Licio Giorgieri 5, 34127 Trieste, Italy
Interests: antimicrobial peptides; bivalves; defense peptides; immunity; molecular evolution
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Dr. Yuki Fujii

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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
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Prof. Dr. Yasuhiro Ozeki

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School of Sciences, Yokohama City University, 22-2, Seto, Kanazawa-Ku, Yokohama 236-0027, Japan
Interests: glycobiology; lectins; marine invertebrates
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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

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Published Papers (11 papers)

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Research

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18 pages, 3933 KiB

Open AccessArticle

Sulfated Polyhydroxysteroid Glycosides from the Sea of Okhotsk Starfish Henricia leviuscula spiculifera and Potential Mechanisms for Their Observed Anti-Cancer Activity against Several Types of Human Cancer Cells

by Alla A. Kicha, Dmitriy K. Tolkanov, Timofey V. Malyarenko, Olesya S. Malyarenko, Alexandra S. Kuzmich, Anatoly I. Kalinovsky, Roman S. Popov, Valentin A. Stonik, Natalia V. Ivanchina and Pavel S. Dmitrenok

Mar. Drugs 2024, 22(7), 294; https://doi.org/10.3390/md22070294 - 26 Jun 2024

Viewed by 1517

Abstract

Three new monosulfated polyhydroxysteroid glycosides, spiculiferosides A (1), B (2), and C (3), along with new related unsulfated monoglycoside, spiculiferoside D (4), were isolated from an ethanolic extract of the starfish Henricia leviuscula spiculifera collected in the Sea of Okhotsk. Compounds 1–3 contain two carbohydrate moieties, one of which is attached to C-3 of the steroid tetracyclic core, whereas another is located at C-24 of the side chain of aglycon. Two glycosides (2, 3) are biosides, and one glycoside (1), unlike them, includes three monosaccharide residues. Such type triosides are a rare group of polar steroids of sea stars. In addition, the 5-substituted 3-OSO₃-α-L-Araf unit was found in steroid glycosides from starfish for the first time. Cell viability analysis showed that 1–3 (at concentrations up to 100 μM) had negligible cytotoxicity against human embryonic kidney HEK293, melanoma SK-MEL-28, breast cancer MDA-MB-231, and colorectal carcinoma HCT 116 cells. These compounds significantly inhibited proliferation and colony formation in HCT 116 cells at non-toxic concentrations, with compound 3 having the greatest effect. Compound 3 exerted anti-proliferative effects on HCT 116 cells through the induction of dose-dependent cell cycle arrest at the G2/M phase, regulation of expression of cell cycle proteins CDK2, CDK4, cyclin D1, p21, and inhibition of phosphorylation of protein kinases c-Raf, MEK1/2, ERK1/2 of the MAPK/ERK1/2 pathway. Full article

(This article belongs to the Special Issue Marine Glycomics 2nd Edition)

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16 pages, 3543 KiB

Open AccessArticle

Multifunctional Cell Regulation Activities of the Mussel Lectin SeviL: Induction of Macrophage Polarization toward the M1 Functional Phenotype

by Yuki Fujii, Kenichi Kamata, Marco Gerdol, Imtiaj Hasan, Sultana Rajia, Sarkar M. A. Kawsar, Somrita Padma, Bishnu Pada Chatterjee, Mayuka Ohkawa, Ryuya Ishiwata, Suzuna Yoshimoto, Masao Yamada, Namiho Matsuzaki, Keita Yamamoto, Yuka Niimi, Nobumitsu Miyanishi, Masamitsu Konno, Alberto Pallavicini, Tatsuya Kawasaki, Yukiko Ogawa, Yasuhiro Ozeki and Hideaki Fujita Show full author list Hide full author list

Mar. Drugs 2024, 22(6), 269; https://doi.org/10.3390/md22060269 - 11 Jun 2024

Viewed by 2150

Abstract

SeviL, a galactoside-binding lectin previously isolated from the mussel Mytilisepta virgata, was demonstrated to trigger apoptosis in HeLa ovarian cancer cells. Here, we show that this lectin can promote the polarization of macrophage cell lines toward an M1 functional phenotype at low concentrations. The administration of SeviL to monocyte and basophil cell lines reduced their growth in a dose-dependent manner. However, low lectin concentrations induced proliferation in the RAW264.7 macrophage cell line, which was supported by the significant up-regulation of TOM22, a component of the mitochondrial outer membrane. Furthermore, the morphology of lectin-treated macrophage cells markedly changed, shifting from a spherical to an elongated shape. The ability of SeviL to induce the polarization of RAW264.7 cells to M1 macrophages at low concentrations is supported by the secretion of proinflammatory cytokines and chemokines, as well as by the enhancement in the expression of IL-6- and TNF-α-encoding mRNAs, both of which encode inflammatory molecular markers. Moreover, we also observed a number of accessory molecular alterations, such as the activation of MAP kinases and the JAK/STAT pathway and the phosphorylation of platelet-derived growth factor receptor-α, which altogether support the functional reprogramming of RAW264.7 following SeviL treatment. These results indicate that this mussel β-trefoil lectin has a concentration-dependent multifunctional role in regulating cell proliferation, phenotype, and death in macrophages, suggesting its possible involvement in regulating hemocyte activity in vivo. Full article

(This article belongs to the Special Issue Marine Glycomics 2nd Edition)

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11 pages, 2503 KiB

Open AccessArticle

Direct Degradation of Fresh and Dried Macroalgae by Agarivorans albus B2Z047

by Ya Gong, Dan-Dan Shang, Cheng-Lin Sun, Zong-Jun Du and Guan-Jun Chen

Mar. Drugs 2024, 22(5), 203; https://doi.org/10.3390/md22050203 - 28 Apr 2024

Viewed by 1268

Abstract

Marine macroalgae are increasingly recognized for their significant biological and economic potential. The key to unlocking this potential lies in the efficient degradation of all carbohydrates from the macroalgae biomass. However, a variety of polysaccharides (alginate, cellulose, fucoidan, and laminarin), are difficult to degrade simultaneously in a short time. In this study, the brown alga Saccharina japonica was found to be rapidly and thoroughly degraded by the marine bacterium Agarivorans albus B2Z047. This strain harbors a broad spectrum of carbohydrate-active enzymes capable of degrading various polysaccharides, making it uniquely equipped to efficiently break down both fresh and dried kelp, achieving a hydrolysis rate of up to 52%. A transcriptomic analysis elucidated the presence of pivotal enzyme genes implicated in the degradation pathways of alginate, cellulose, fucoidan, and laminarin. This discovery highlights the bacterium’s capability for the efficient and comprehensive conversion of kelp biomass, indicating its significant potential in biotechnological applications for macroalgae resource utilization. Full article

(This article belongs to the Special Issue Marine Glycomics 2nd Edition)

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19 pages, 2783 KiB

Open AccessFeature PaperArticle

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

Cited by 2 | Viewed by 2041

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 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

Open AccessArticle

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

Cited by 1 | Viewed by 1611

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 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

Open AccessArticle

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 - 2 Jun 2023

Cited by 5 | Viewed by 2110

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 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

Open AccessArticle

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 9 | Viewed by 2235

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 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

Open AccessArticle

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 4 | Viewed by 2120

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 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

Open AccessArticle

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 - 8 Mar 2023

Cited by 3 | Viewed by 1956

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 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

Open AccessArticle

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 3 | Viewed by 2137

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), 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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15 pages, 1765 KiB

Open AccessReview

Marine Lectins and Lectin-like Proteins as Promising Molecules Targeting Aberrant Glycosylation Signatures in Human Brain Tumors

by Ivan Buriak and Vadim Kumeiko

Mar. Drugs 2024, 22(12), 527; https://doi.org/10.3390/md22120527 - 22 Nov 2024

Viewed by 628

Abstract

Glycosylation is a ubiquitous and the most structurally diverse post-translational modification of proteins. High levels of phenotypic heterogeneity in brain tumors affect the biosynthetic pathway of glycosylation machinery, resulting in aberrant glycosylation patterns. Traditionally, unique glycocode readers, carbohydrate-binding proteins, have been used to identify differentially expressed carbohydrate determinants associated with the tumor cell surface. However, identifying novel distinctive glycosylation signatures in brain tumors requires the timely development of molecular tools capable of targeting them. We classified marine-derived lectins and lectin-like molecules according to their ability to cover aberrant glycosylation patterns in brain tumors to encourage exploration of the potential of these molecules for precision diagnostics and personalized therapy. Full article

(This article belongs to the Special Issue Marine Glycomics 2nd Edition)

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