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Glycobiology: The New Discoveries, Approaches, and Technical Developments

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

Deadline for manuscript submissions: 30 September 2024 | Viewed by 5210

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Dr. Sanja Dabelić

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Department of Biochemistry and Molecular Biology, Faculty of Pharmacy and Biochemistry, University of Zagreb, A. Kovacica 1, 10000 Zagreb, Croatia
Interests: glycobiology

Special Issue Information

Dear Colleagues,

Over the last few decades, our understanding of structure and function of carbohydrate has undergone an incredible transformation. From being considered molecules whose role is strictly energetical or structural, glycans are now recognized as complex and diverse structures involved in, and even crucial to, numerous biological processes. Given that the techniques and interest for investigating the structure, presence, and functions of glycans are progressing more and more, it is expected that we will, in the years ahead, discover many more of their roles—some "sweet or desirable", others "bitter or fatal". The growing field of glycobiology has a great impact, not only on our understanding of biological processes, but also on our potential to modulate them. This open access Special Issue will bring together original research and review articles on various aspects of glycobiology, highlighting new discoveries, approaches, and technical developments. The main focus of this issue is sharing significant works that advance our understanding of glycans’ roles and their impact on the structure and function of individual molecules, materials, cells, tissues, and organisms, as well as on the interplay between them.

This Special Issue welcomes original research papers, as well as critical or comprehensive reviews, that demonstrate or summarize significant advances in the glycobiology field.

Topics include, but are not limited to:

Novel tools and strategies for the analysis/synthesis/modulation of glycoconjugates.
Glycan structure, function, and biosynthesis.
Glycan-recognizing molecules.
Glycan structural and functional diversity across biological taxa.
Genetic basis of glycobiology.
Glycans in physiology, disorders, and diseases.
Carbohydrates in pharmacy, medicine, biotechnology, materials sciences and nanotechnology.

Dr. Sanja Dabelić
Guest Editor

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Keywords

glycans
lectins
glycoconjugates
glycosylation
genetic disorders of glycosylation
glycomics and glycoproteomics

Published Papers (6 papers)

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Research

14 pages, 12506 KiB

Open AccessArticle

Mannose-Binding Lectin Deposition in Membranous Nephropathy and Differentiation of Primary from Secondary Forms

by Irina Zdravkova, Eduard Tilkiyan and Desislava Bozhkova

Int. J. Mol. Sci. 2024, 25(14), 7659; https://doi.org/10.3390/ijms25147659 - 12 Jul 2024

Viewed by 131

Abstract

The differentiation between primary and secondary forms of membranous nephropathy (MN) is a cornerstone that is necessary for adequate decision making regarding the treatment options and behavior of each specific case. Kidney biopsy and antibody results can be controversial, and a unique biomarker has still not been found. Background and Objectives: We investigated the lack of mannose-binding lectin (MBL) deposition in patients with secondary MNs (sMNs) with the presence of IgG4 deposition in relation to the presence of MBL deposition in patients with primary MNs (pMNs). We also established a connection between the stage of MN and MBL deposition. Materials and Methods: Materials from 72 renal biopsies with proven MN were used for immunohistochemistry staining (IHC) for the phospholipase A2 receptor (PLA2R), immunoglobulin subtype IgG4, and MBL. Patients were separated into one of the following three groups: primary MN (pMN), idiopathic MN (iMN), and secondary MN (sMN). Serum antibodies for PLA2R and thrombospondin type-I-domain-containing 7A (THSD7A) were also used for the precise evaluation of the type of MN, as well as for detecting positivity for PLA2R using IHC. Which stage of MN was present in relation to the deposition of MBL was evaluated. Results: In total, 50 patients were positive for IgG4, 34 with pMN, 12 with iMN, and 4 with sMN. A total of 20 patients were positive for MBL, 14 with pMN and 6 with iMN; no MBL deposits were found in patients with sMN. MBL positivity was predominantly present in the first two stages of MN, with a gradual reduction in the later stages. Conclusions: The activation of the lectin–complement pathway occurs in the early stages of the disease and is associated with the deposition of IgG4; IgG4 deposition is present in sMN, but there is no MBL deposition. IgG4 cannot be used for the differentiation of primary from secondary MNs, but the lack of MBL can be used as a marker for sMN in the early stages of the disease. Full article

(This article belongs to the Special Issue Glycobiology: The New Discoveries, Approaches, and Technical Developments)

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15 pages, 3187 KiB

Open AccessArticle

Involvement of the GH38 Family Exoglycosidase α-Mannosidase in Strawberry Fruit Ripening

by Angela Méndez-Yáñez, Darwin Sáez, Francisca Rodríguez-Arriaza, Claudio Letelier-Naritelli, Felipe Valenzuela-Riffo and Luis Morales-Quintana

Int. J. Mol. Sci. 2024, 25(12), 6581; https://doi.org/10.3390/ijms25126581 - 14 Jun 2024

Viewed by 374

Abstract

Exoglycosidase enzymes hydrolyze the N-glycosylations of cell wall enzymes, releasing N-glycans that act as signal molecules and promote fruit ripening. Vesicular exoglycosidase α-mannosidase enzymes of the GH38 family (EC 3.2.1.24; α-man) hydrolyze N-glycans in non-reduced termini. Strawberry fruit (Fragaria × ananassa) is characterized by rapid softening as a result of cell wall modifications during the fruit ripening process. Enzymes acting on cell wall polysaccharides explain the changes in fruit firmness, but α-man has not yet been described in F. × ananassa, meaning that the indirect effects of N-glycan removal on its fruit ripening process are unknown. The present study identified 10 GH38 α-man sequences in the F. × ananassa genome with characteristic conserved domains and key residues. A phylogenetic tree built with the neighbor-joining method and three groups of α-man established, of which group I was classified into three subgroups and group III contained only Poaceae spp. sequences. The real-time qPCR results demonstrated that FaMAN genes decreased during fruit ripening, a trend mirrored by the total enzyme activity from the white to ripe stages. The analysis of the promoter regions of these FaMAN genes was enriched with ripening and phytohormone response elements, and contained cis-regulatory elements related to stress responses to low temperature, drought, defense, and salt stress. This study discusses the relevance of α-man in fruit ripening and how it can be a useful target to prolong fruit shelf life. Full article

(This article belongs to the Special Issue Glycobiology: The New Discoveries, Approaches, and Technical Developments)

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11 pages, 3118 KiB

Open AccessArticle

The Impact of Protein Glycosylation on the Identification of Patients with Pediatric Appendicitis

by Dalma Dojcsák, Flóra Farkas, Tamás Farkas, János Papp, Attila Garami, Béla Viskolcz and Csaba Váradi

Int. J. Mol. Sci. 2024, 25(12), 6432; https://doi.org/10.3390/ijms25126432 - 11 Jun 2024

Viewed by 881

Abstract

The identification of pediatric appendicitis is challenging due to the lack of specific markers thereby several factors are included in the diagnostic process such as abdominal pain, ultrasonography and altered laboratory parameters (C reactive protein, absolute neutrophil cell number and white blood cell number). The glycosylation pattern of serum N-glycome was analyzed in this study of 38 controls and 40 patients with pediatric appendicitis. The glycans were released by enzymatic deglycosylation followed by fluorescent labeling and solid-phase extraction. The prepared samples were analyzed by hydrophilic interaction liquid chromatography with fluorescence and mass-spectrometric detection. The generated data were analyzed by multiple statistical tests involving the most important laboratory parameters as well. Significant differences associated with the examined patient groups were revealed suggesting the potential use of glycosylation analysis supporting the detection of pediatric appendicitis. Full article

(This article belongs to the Special Issue Glycobiology: The New Discoveries, Approaches, and Technical Developments)

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12 pages, 2368 KiB

Open AccessArticle

Glycosylation and Characterization of Human Transferrin in an End-Stage Kidney Disease

by Goran Miljuš, Ana Penezić, Lucia Pažitná, Nikola Gligorijević, Marko Baralić, Aleksandra Vilotić, Miloš Šunderić, Dragana Robajac, Zorana Dobrijević, Jaroslav Katrlík and Olgica Nedić

Int. J. Mol. Sci. 2024, 25(9), 4625; https://doi.org/10.3390/ijms25094625 - 24 Apr 2024

Viewed by 773

Abstract

Chronic kidney disease (CKD) is a global health concern affecting approximately one billion individuals worldwide. End-stage kidney disease (ESKD), the most severe form of CKD, is often accompanied by anemia. Peritoneal dialysis (PD), a common treatment for ESKD, utilizes the peritoneum for solute transfer but is associated with complications including protein loss, including transferrin (Tf) a key protein involved in iron transport. This study investigated Tf characteristics in ESKD patients compared to healthy individuals using lectin microarray, spectroscopic techniques and immunocytochemical analysis to assess Tf interaction with transferrin receptors (TfRs). ESKD patients exhibited altered Tf glycosylation patterns, evidenced by significant changes in lectin reactivity compared to healthy controls. However, structural analyses revealed no significant differences in the Tf secondary or tertiary structures between the two groups. A functional analysis demonstrated comparable Tf-TfR interaction in both PD and healthy samples. Despite significant alterations in Tf glycosylation, structural integrity and Tf-TfR interaction remained preserved in PD patients. These findings suggest that while glycosylation changes may influence iron metabolism, they do not impair Tf function. The study highlights the importance of a glucose-free dialysis solutions in managing anemia exacerbation in PD patients with poorly controlled anemia, potentially offering a targeted therapeutic approach to improve patient outcomes. Full article

(This article belongs to the Special Issue Glycobiology: The New Discoveries, Approaches, and Technical Developments)

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14 pages, 1778 KiB

Open AccessArticle

Label-Free Liquid Chromatography–Mass Spectrometry Quantitation of Relative N- and O-Glycan Concentrations in Human Milk in Japan

by Toshiyuki Yamaguchi, Hirofumi Fukudome, Junichi Higuchi, Tomoki Takahashi, Yuta Tsujimori, Hiroshi M. Ueno, Yasuhiro Toba and Fumihiko Sakai

Int. J. Mol. Sci. 2024, 25(3), 1772; https://doi.org/10.3390/ijms25031772 - 1 Feb 2024

Viewed by 1153

Abstract

Human milk is abundant in carbohydrates and includes human milk oligosaccharides (HMOs) and N/O-glycans conjugated to proteins. HMO compositions and concentrations vary in individuals according to the maternal secretor status based on the fucosyltransferase 2 genotype; however, the profile of N/O-glycans remains uninvestigated because of the analytical complexity. Herein, we applied a label-free chromatography–mass spectrometry (LC–MS) technique to elucidate the variation in the composition and concentration of N/O-glycans in human milk. We used label-free LC–MS to relatively quantify 16 N-glycans and 12 O-glycans in 200 samples of Japanese human milk (1–2 months postpartum) and applied high performance anion exchange chromatography with pulsed amperometric detection to absolutely quantify the concentrations of 11 representative HMOs. Cluster analysis of the quantitative data revealed that O-glycans and several HMOs were classified according to the presence or absence of fucose linked to galactose while N-glycans were classified into a different group from O-glycans and HMOs. O-glycans and HMOs with fucose linked to galactose were more abundant in human milk from secretor mothers than from nonsecretor mothers. Thus, secretor status influenced the composition and concentration of HMOs and O-glycans but not those of N-glycans in human milk. Full article

(This article belongs to the Special Issue Glycobiology: The New Discoveries, Approaches, and Technical Developments)

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16 pages, 6669 KiB

Open AccessArticle

Sialyltransferase Mutations Alter the Expression of Calcium-Binding Interneurons in Mice Neocortex, Hippocampus and Striatum

by Senka Blažetić, Vinko Krajina, Irena Labak, Barbara Viljetić, Valentina Pavić, Vedrana Ivić, Marta Balog, Ronald L. Schnaar and Marija Heffer

Int. J. Mol. Sci. 2023, 24(24), 17218; https://doi.org/10.3390/ijms242417218 - 7 Dec 2023

Viewed by 939

Abstract

Gangliosides are major glycans on vertebrate nerve cells, and their metabolic disruption results in congenital disorders with marked cognitive and motor deficits. The sialyltransferase gene St3gal2 is responsible for terminal sialylation of two prominent brain gangliosides in mammals, GD1a and GT1b. In this study, we analyzed the expression of calcium-binding interneurons in primary sensory (somatic, visual, and auditory) and motor areas of the neocortex, hippocampus, and striatum of St3gal2-null mice as well as St3gal3-null and St3gal2/3-double null. Immunohistochemistry with highly specific primary antibodies for GABA, parvalbumin, calretinin, and calbindin were used for interneuron detection. St3gal2-null mice had decreased expression of all three analyzed types of calcium-binding interneurons in all analyzed regions of the neocortex. These results implicate gangliosides GD1a and GT1b in the process of interneuron migration and maturation. Full article

(This article belongs to the Special Issue Glycobiology: The New Discoveries, Approaches, and Technical Developments)

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