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Glycan–Receptor Interaction 3.0
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Glycan–Receptor Interaction 3.0

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Biology".

Deadline for manuscript submissions: closed (31 October 2022) | Viewed by 6366

Special Issue Editor

Prof. Dr. Cheorl-Ho Kim

E-Mail Website
Guest Editor
1. Department of Biological Sciences, College of Science, Sungkyunkwan University, Seoburo 2066, Suwon 16419, Republic of Korea
2. Samsung Advanced Institute of Health Science and Technology (SAIHST), Sungkyunkwan University, Seoul 06351, Republic of Korea
Interests: glycobiology; sialobiology; sialyltransferase; N-glycan; O-glycan; glycolipid; sphingolipid; glycoprotein; surface sugar; ganglioside; sialic acid; Sialyl Le antigen; lectin; galectin; Siglec; ER-Golgi glycosylation; sugar–receptor interaction; innate immune; xenotransplantation; cell–cell interaction
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Cell surface carbohydrates attached to proteins and lipids are major components of the outer surface of mammalian cells. Changes to the surface glycosylation are important means of cell–cell interaction in fertilization, development, differentiation, growth, aging, adhesion, signal transduction, neurotransduction, immune systems, carcinogenesis, metastasis, and angiogenesis. Therefore, surface glycosylations are mainly located on the borders of cells to communicate through face-to-face recognition or carbohydrate glycan–receptor interaction. Because the glycans communicate with their counterparts, such as specific receptors through purely physical interactions, the synthesis and distribution of these components are under strict genetic control. These glycosylated proteins and lipids have been implicated in multicellular functional expression and society formation, which depends on cell type, tissue type, and organ type. Modifications of cellular glycosylation are also a common phenotypic change in malignancy, with a poor prognosis for the patients. Most of the carbohydrate tumor antigens are sialylated. As examples, the mucin-type Sialyl-Tn, Sialyl-Lewis X, and Sialyl-Lewis A antigens are increased in the N-linked and O-linked oligosaccharides of the carcinoma cell glycoproteins of cancers. In recent viral pandemics, it was recognized that human and avian influenza viruses bind sialic acid-based receptors. For example, a human-type is NeuAcα2-6Gal, while an avian-type is NeuAcα2-3Gal. From the recent human-type H3N2 virus, the evolutionary transition has been suggested in sialyl ligand–receptor interaction. Therefore, interaction between the influenza virus and sialic acid receptors is a current hot issue in glycan–receptor interaction. The changed glycans can regulate carbohydrate–carbohydrate, carbohydrate–protein, and carbohydrate–lipid interactions. Therefore, each glycan structure has been implicated as a face or signature of certain biological states in cells and organs. In tumors, the glycosylated antigens can be used as tumor markers for human cancer patients, especially for node-negative patients.

We invite researchers to contribute original and review articles regarding the interactions between glycans and proteins. Potential topics include, but are not limited to:

  • Glycosylation of N-/O-glycoproteins;
  • Sialylation of glycoproteins and glycolipids;
  • Lectin–glycan interaction;
  • Sialyltransferases;
  • Glycosylation in malignancy and cancers;
  • Xenoantigenic glycosylation in non-human mammals;
  • Sphingolipids in membranes;
  • ER-specific glycobiology;
  • Golgi-specific glycobiology;
  • Glycan-based cell differentiation and development;
  • Glycan antigens in stem cells;
  • Sialyl antigen–Lectin, Galectin, Siglec;
  • Sugar–receptor interaction;
  • Innate immunity;
  • Xenotransplantation;
  • Influenza virus and sialic acid receptors;
  • Sialic acids mimetics as drug design.

Prof. Dr. Cheorl-Ho Kim
Guest Editor

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. International Journal of Molecular Sciences is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. There is an Article Processing Charge (APC) for publication in this open access journal. For details about the APC please see here. 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

  • glycobiology
  • N-/O-glycan
  • glycosphingolipid
  • glycoprotein
  • ganglioside
  • surface glycan
  • lectin
  • galectin
  • siglec
  • ER–Golgi network
  • glycan–receptor interaction
  • innate immunity
  • xenotransplantation
  • cell–cell interaction
  • influenza virus sialic acid receptors

Published Papers (4 papers)

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Research

15 pages, 2002 KiB  
Article
Specific Signal Transduction of Constitutively Activating (D576G) and Inactivating (R476H) Mutants of Agonist-Stimulated Luteinizing Hormone Receptor in Eel
by Seung-Hee Choi, Munkhzaya Byambaragchaa, Dae-Jung Kim, Jong-Hyuk Lee, Myung-Hwa Kang and Kwan-Sik Min
Int. J. Mol. Sci. 2023, 24(11), 9133; https://doi.org/10.3390/ijms24119133 - 23 May 2023
Cited by 1 | Viewed by 810
Abstract
We investigated the mechanism of signal transduction using inactivating (R476H) and activating (D576G) mutants of luteinizing hormone receptor (LHR) of eel at the conserved regions of intracellular loops II and III, respectively, naturally occurring in mammalian LHR. The expression of D576G and R476H [...] Read more.
We investigated the mechanism of signal transduction using inactivating (R476H) and activating (D576G) mutants of luteinizing hormone receptor (LHR) of eel at the conserved regions of intracellular loops II and III, respectively, naturally occurring in mammalian LHR. The expression of D576G and R476H mutants was approximately 58% and 59%, respectively, on the cell surface compared to those of eel LHR-wild type (wt). In eel LHR-wt, cAMP production increased upon agonist stimulation. Cells expressing eel LHR-D576G, a highly conserved aspartic acid residue, exhibited a 5.8-fold increase in basal cAMP response; however, the maximal cAMP response by high-agonist stimulation was approximately 0.62-fold. Mutation of a highly conserved arginine residue in the second intracellular loop of eel LHR (LHR-R476H) completely impaired the cAMP response. The rate of loss in cell-surface expression of eel LHR-wt and D576G mutant was similar to the agonist recombinant (rec)-eel LH after 30 min. However, the mutants presented rates of loss higher than eel LHR-wt did upon rec-eCG treatment. Therefore, the activating mutant constitutively induced cAMP signaling. The inactivating mutation resulted in the loss of LHR expression on the cell surface and no cAMP signaling. These data provide valuable information regarding the structure–function relationship of LHR–LH complexes. Full article
(This article belongs to the Special Issue Glycan–Receptor Interaction 3.0)
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13 pages, 1221 KiB  
Article
The N-Linked Glycosylation Site N191 Is Necessary for PKA Signal Transduction in Eel Follicle-Stimulating Hormone Receptor
by Munkhzaya Byambaragchaa, Hong-Kyu Park, Dae-Jung Kim, Jong-Hyuk Lee, Myung-Hwa Kang and Kwan-Sik Min
Int. J. Mol. Sci. 2022, 23(21), 12792; https://doi.org/10.3390/ijms232112792 - 24 Oct 2022
Cited by 2 | Viewed by 1098
Abstract
The follicle-stimulating hormone receptor (FSHR) contains several N-linked glycosylation sites in its extracellular region. We conducted the present study to determine whether conserved glycosylated sites in eel FSHR are necessary for cyclic adenosine monophosphate (cAMP) signal transduction. We used site-directed mutagenesis to induce [...] Read more.
The follicle-stimulating hormone receptor (FSHR) contains several N-linked glycosylation sites in its extracellular region. We conducted the present study to determine whether conserved glycosylated sites in eel FSHR are necessary for cyclic adenosine monophosphate (cAMP) signal transduction. We used site-directed mutagenesis to induce four mutations (N120Q, N191Q, N272Q, and N288Q) in the N-linked glycosylation sites of eel FSHR. In the eel FSHR wild-type (wt), the cAMP response was gradually increased in a dose-dependent manner (0.01–1500 ng/mL), displaying a high response (approximately 57.5 nM/104 cells) at the Rmax level. Three mutants (N120Q, N272Q, and N288Q) showed a considerably decreased signal transduction as a result of high-ligand treatment, whereas one mutant (N191Q) exhibited a completely impaired signal transduction. The expression level of the N191Q mutant was only 9.2% relative to that of the eel FSHR-wt, indicating a negligible expression level. The expression levels of the N120Q and N272Q mutants were approximately 35.9% and 24% of the FSHG-wt, respectively. The N288Q mutant had an expression level similar to that of the eel FSHR-wt, despite the mostly impaired cAMP responsiveness. The loss of the cell surface agonist-receptor complexes was very rapid in the cells expressing eel FSHR-wt and FSHR-N288Q mutants. Specifically, the N191Q mutant was completely impaired by the loss of cell surface receptors, despite treatment with a high concentration of the agonist. Therefore, we suggest that the N191 site is necessary for cAMP signal transduction. This finding implies that the cAMP response, mediated by G proteins, is directly related to the loss of cell surface receptors as a result of high-agonist treatment. Full article
(This article belongs to the Special Issue Glycan–Receptor Interaction 3.0)
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28 pages, 3393 KiB  
Article
Identification and Characterization of the Larval Settlement Pheromone Protein Components in Adult Shells of Crassostrea gigas: A Novel Function of Shell Matrix Proteins
by Mary Grace Sedanza, Asami Yoshida, Hee-Jin Kim, Kenichi Yamaguchi, Kiyoshi Osatomi and Cyril Glenn Satuito
Int. J. Mol. Sci. 2022, 23(17), 9816; https://doi.org/10.3390/ijms23179816 - 29 Aug 2022
Cited by 2 | Viewed by 2017
Abstract
The global decline of natural oyster populations emphasizes the need to improve our understanding of their biology. Understanding the role of chemical cues from conspecifics on how oysters occupy appropriate substrata is crucial to learning about their evolution, population dynamics, and chemical communication. [...] Read more.
The global decline of natural oyster populations emphasizes the need to improve our understanding of their biology. Understanding the role of chemical cues from conspecifics on how oysters occupy appropriate substrata is crucial to learning about their evolution, population dynamics, and chemical communication. Here, a novel role of a macromolecular assembly of shell matrix proteins which act as Crassostrea gigas Settlement Pheromone Protein Components in adult shells is demonstrated as the biological cue responsible for gregarious settlement on conspecifics. A bioassay-guided fractionation approach aided by biochemical and molecular analyses reveals that Gigasin-6 isoform X1 and/or X2 isolated from adult shells is the major inducing cue for larval settlement and may also play a role in postlarva–larva settlement interactions. Other isolated Stains-all-stainable acidic proteins may function as a co-factor and a scaffold/structural framework for other matrix proteins to anchor within this assembly and provide protection. Notably, conspecific cue-mediated larval settlement induction in C. gigas presents a complex system that requires an interplay of different glycans, disulfide bonds, amino acid groups, and phosphorylation crosstalk for recognition. These results may find application in the development of oyster aquacultures which could help recover declining marine species and as targets of anti-fouling agents. Full article
(This article belongs to the Special Issue Glycan–Receptor Interaction 3.0)
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16 pages, 3177 KiB  
Article
Characterization of a C-Type Lectin Domain-Containing Protein with Antibacterial Activity from Pacific Abalone (Haliotis discus hannai)
by Mi-Jin Choi, Yeo Reum Kim, Nam Gyu Park, Cheorl-Ho Kim, Young Dae Oh, Han Kyu Lim and Jong-Myoung Kim
Int. J. Mol. Sci. 2022, 23(2), 698; https://doi.org/10.3390/ijms23020698 - 09 Jan 2022
Cited by 7 | Viewed by 1814
Abstract
Genes that influence the growth of Pacific abalone (Haliotis discus hannai) may improve the productivity of the aquaculture industry. Previous research demonstrated that the differential expression of a gene encoding a C-type lectin domain-containing protein (CTLD) was associated with a faster [...] Read more.
Genes that influence the growth of Pacific abalone (Haliotis discus hannai) may improve the productivity of the aquaculture industry. Previous research demonstrated that the differential expression of a gene encoding a C-type lectin domain-containing protein (CTLD) was associated with a faster growth in Pacific abalone. We analyzed this gene and identified an open reading frame that consisted of 145 amino acids. The sequence showed a significant homology to other genes that encode CTLDs in the genus Haliotis. Expression profiling analysis at different developmental stages and from various tissues showed that the gene was first expressed at approximately 50 days after fertilization (shell length of 2.47 ± 0.13 mm). In adult Pacific abalone, the gene was strongly expressed in the epipodium, gill, and mantle. Recombinant Pacific abalone CTLD purified from Escherichia coli exhibited antimicrobial activity against several Gram-positive bacteria (Bacillus subtilis, Streptococcus iniae, and Lactococcus garvieae) and Gram-negative bacteria (Vibrio alginolyticus and Vibrio harveyi). We also performed bacterial agglutination assays in the presence of Ca2+, as well as bacterial binding assays in the presence of the detergent dodecyl maltoside. Incubation with E. coli and B. subtilis cells suggested that the CTLD stimulated Ca2+-dependent bacterial agglutination. Our results suggest that this novel Pacific abalone CTLD is important for the pathogen recognition in the gastropod host defense mechanism. Full article
(This article belongs to the Special Issue Glycan–Receptor Interaction 3.0)
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