Submit to IJMS Review for IJMS Propose a Special Issue

Journal Menu

Journal Browser

Correlating Structural and Functional Attributes of Glycans and Glycoconjugates

Special Issue Editors
Special Issue Information
Keywords
Published Papers

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

Deadline for manuscript submissions: closed (13 April 2023) | Viewed by 4932

Share This Special Issue

Special Issue Editor

Dr. Kshitij Khatri

E-Mail Website
Guest Editor

Center for Biomedical Mass Spectrometry, Department of Biochemistry, Boston University Medical Campus, 670 Albany Street, Boston, MA 02118, USA
Interests: glycosylation

Special Issue Information

Dear Colleagues,

Glycosylation is central to all living organisms—these biopolymers exist almost ubiquitously across biological systems and serve many important biological functions, ranging from their roles as energy and nutrition sources, to being structural determinants, and mediating cellular signaling and intercellular interactions. More importantly. glycans appear as modifications that decorate proteins and lipids, and the newly discovered glycosylation of RNA molecules from the Bertozzi group opens up an entirely new field of study in glycobiology. The recent COVID-19 pandemic has also re-emphasized the involvement of glycans on viral envelopes and their importance in virus fitness, immune-evasion, and host interactions. These interactions are mediated by glycans and glycoconjugates in the host extracellular matrix, further strengthening the importance of glycosylation in human health and disease.

The last decade has seen exponential advancement in methodologies for deep and rapid analysis of glycans and glycoconjugates. These improvements in technology have enabled direct correlations of structural attributes of these molecules with functional outcomes. This Special Issue focuses on original research or review articles elucidating structural features of glycans and glycoconjugates, and their impact on biological functions and pathways.

Dr. Kshitij Khatri
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
glycoanalytics
glycan-mediated interactions
glycoproteins
glycolipids
glycoRNA
extracellular matrix

Published Papers (3 papers)

Download All Papers

Research

Jump to: Review

15 pages, 33494 KiB

Open AccessArticle

Alterations in the Glycan Composition of Serum Glycoproteins in Attention-Deficit Hyperactivity Disorder

by Kristína Kianičková, Lucia Pažitná, Paras H. Kundalia, Zuzana Pakanová, Marek Nemčovič, Peter Baráth, Eva Katrlíková, Ján Šuba, Jana Trebatická and Jaroslav Katrlík

Int. J. Mol. Sci. 2023, 24(10), 8745; https://doi.org/10.3390/ijms24108745 - 14 May 2023

Cited by 3 | Viewed by 1530

Abstract

Changes in protein glycosylation are associated with most biological processes, and the importance of glycomic analysis in the research of disorders is constantly increasing, including in the neurodevelopmental field. We glycoprofiled sera in 10 children with attention-deficit hyperactivity disorder (ADHD) and 10 matching healthy controls for 3 types of samples: whole serum, sera after depletion of abundant proteins (albumin and IgG), and isolated IgG. The analytical methods used were a lectin-based glycoprotein microarray enabling high-throughput glycan analysis and matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) mass spectrometry (MS) as a standard method for the identification of glycan structures. For microarray analysis, the samples printed on microarray slides were incubated with biotinylated lectins and detected using the fluorescent conjugate of streptavidin by a microarray scanner. In the ADHD patient samples, we found increased antennary fucosylation, decreased di-/triantennary N-glycans with bisecting N-acetylglucosamine (GlcNAc), and decreased α2-3 sialylation. The results obtained by both independent methods were consistent. The study’s sample size and design do not allow far-reaching conclusions to be drawn. In any case, there is a strong demand for a better and more comprehensive diagnosis of ADHD, and the obtained results emphasize that the presented approach brings new horizons to studying functional associations of glycan alterations in ADHD. Full article

(This article belongs to the Special Issue Correlating Structural and Functional Attributes of Glycans and Glycoconjugates)

► Show Figures

Figure 1

11 pages, 1820 KiB

Open AccessArticle

1,5-Anhydro-D-Fructose Exhibits Satiety Effects via the Activation of Oxytocin Neurons in the Paraventricular Nucleus

by Masanori Nakata, Yuto Yamaguchi, Hikaru Monnkawa, Midori Takahashi, Boyang Zhang, Putra Santoso, Toshihiko Yada and Ikuro Maruyama

Int. J. Mol. Sci. 2023, 24(9), 8248; https://doi.org/10.3390/ijms24098248 - 4 May 2023

Cited by 1 | Viewed by 1489

Abstract

1,5-Anhydro-D-fructose (1,5-AF) is a bioactive monosaccharide that is produced by the glycogenolysis in mammalians and is metabolized to 1,5-anhydro-D-glucitol (1,5-AG). 1,5-AG is used as a marker of glycemic control in diabetes patients. 1,5-AF has a variety of physiological activities, but its effects on energy metabolism, including feeding behavior, are unclarified. The present study examined whether 1,5-AF possesses the effect of satiety. Peroral administration of 1,5-AF, and not of 1,5-AG, suppressed daily food intake. Intracerebroventricular (ICV) administration of 1,5-AF also suppressed feeding. To investigate the neurons targeted by 1,5-AF, we investigated c-Fos expression in the hypothalamus and brain stem. ICV injection of 1,5-AF significantly increased c-Fos positive oxytocin neurons and mRNA expression of oxytocin in the paraventricular nucleus (PVN). Moreover, 1,5-AF increased cytosolic Ca²⁺ concentration of oxytocin neurons in the PVN. Furthermore, the satiety effect of 1,5-AF was abolished in oxytocin knockout mice. These findings reveal that 1,5-AF activates PVN oxytocin neurons to suppress feeding, indicating its potential as the energy storage monitoring messenger to the hypothalamus for integrative regulation of energy metabolism. Full article

(This article belongs to the Special Issue Correlating Structural and Functional Attributes of Glycans and Glycoconjugates)

► Show Figures

Figure 1

Review

Jump to: Research

16 pages, 1685 KiB

Open AccessReview

Gut Microbial Sialidases and Their Role in the Metabolism of Human Milk Sialylated Glycans

by Diego Muñoz-Provencio and María J. Yebra

Int. J. Mol. Sci. 2023, 24(12), 9994; https://doi.org/10.3390/ijms24129994 - 10 Jun 2023

Cited by 2 | Viewed by 1550

Abstract

Sialic acids (SAs) are α-keto-acid sugars with a nine-carbon backbone present at the non-reducing end of human milk oligosaccharides and the glycan moiety of glycoconjugates. SAs displayed on cell surfaces participate in the regulation of many physiologically important cellular and molecular processes, including signaling and adhesion. Additionally, sialyl-oligosaccharides from human milk act as prebiotics in the colon by promoting the settling and proliferation of specific bacteria with SA metabolism capabilities. Sialidases are glycosyl hydrolases that release α-2,3-, α-2,6- and α-2,8-glycosidic linkages of terminal SA residues from oligosaccharides, glycoproteins and glycolipids. The research on sialidases has been traditionally focused on pathogenic microorganisms, where these enzymes are considered virulence factors. There is now a growing interest in sialidases from commensal and probiotic bacteria and their potential transglycosylation activity for the production of functional mimics of human milk oligosaccharides to complement infant formulas. This review provides an overview of exo-alpha-sialidases of bacteria present in the human gastrointestinal tract and some insights into their biological role and biotechnological applications. Full article

(This article belongs to the Special Issue Correlating Structural and Functional Attributes of Glycans and Glycoconjugates)

► Show Figures