ijms-logo

Journal Browser

Journal Browser

Glycomics and Glycosylation Disorders

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

Deadline for manuscript submissions: closed (15 April 2024) | Viewed by 3907

Special Issue Editor

Special Issue Information

Dear Colleagues,

Glycomics "is the systematic study of all glycan structures of a given cell type or organism". Compared with genomics, proteomics, and metabolomics, it is a relatively new field.

The glycome represents the whole content of glycans and glycoconjugates of an organism/cell type. Each kind of organism/cell type has its own glycome whose composition changes greatly from one to another. Vertebrates, for instance, have free glycans, lipid associated glycans, glycoproteins, glycosaminoglycans, and GPI anchors.

Glycans, either free or as a part of a more complex biomolecule, participate in almost every biological process. The synthesis, the transfer, and the modification of glycan moieties on biomolecules are a finely tuned process that requires many steps and involves hundreds of different enzymes/proteins.

The glycome is the result of genetic and environmental factors such as cellular nutrients and pH, but also age, gender, and other variables (for example, smoking). In short, the glycome is a highly diverse and dynamic system, and as a consequence, the information it contains could provide precious insight into the cellular functions underlying physiological, non-physiological, or pathological conditions.

It is well known that structural and conformational aspects of glycans are very complex, and even a small change in a glycan structure can strongly influence the chemophysical properties of the glycomolecule, but more importantly, it affects the biological function(s), and in these cases, glycosylation disorders might occur.

This Special Issue aims to collect any kind of papers (reviews, original papers, perspective papers) regarding structural and/or functional studies on glycans and glycoconjugates, as well as on those aspects that can shed light on their physiological roles, their biosynthesis, and on the physiopathology of disorders of glycosylation. Lastly, since the study of the glycomolecules is incredibly challenging, methodological approaches and innovative tools are topics of utmost importance to focus on as well.

Prof. Dr. Maria Vittoria Cubellis
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

  • glycome
  • glycomics
  • glycomic analysis
  • glycans
  • glycoproteins
  • glycosylation pathway
  • N-glycosylation
  • O-glycosylation
  • GPI anchor
  • disorder of glycosylation

Published Papers (2 papers)

Order results
Result details
Select all
Export citation of selected articles as:

Research

Jump to: Other

7 pages, 924 KiB  
Communication
The Alterations of Serum N-glycome in Response to SARS-CoV-2 Vaccination
by Dalma Dojcsák, Zsófia Kardos, Miklós Szabó, Csaba Oláh, Zsolt Körömi, Béla Viskolcz and Csaba Váradi
Int. J. Mol. Sci. 2023, 24(7), 6203; https://doi.org/10.3390/ijms24076203 - 25 Mar 2023
Viewed by 1093
Abstract
The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) pandemic has caused a global concern since its outbreak in 2019, with one of the main solutions being vaccination. Altered glycosylation has been described in patients after SARS-CoV-2 infection, while the effect of vaccination on [...] Read more.
The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) pandemic has caused a global concern since its outbreak in 2019, with one of the main solutions being vaccination. Altered glycosylation has been described in patients after SARS-CoV-2 infection, while the effect of vaccination on serum glycoproteins remained unexplored. In this study, total serum glycosylation was analyzed in patients after SARS-CoV-2 infection and/or mRNA vaccination in order to identify potential glycosylation-based alterations. Enzyme-linked immunosorbent assay was applied to identify post-COVID-19 and post-Vaccinated patients and rule out potential outliers. Serum samples were deglycosylated by PNGase F digestion, and the released glycans were fluorescently derivatized using procainamide labeling. Solid-phase extraction was used to purify the labeled glycans followed by the analysis of hydrophilic-interaction liquid chromatography with fluorescence and mass-spectrometric detection. Alterations of serum N-glycome in response to SARS-CoV-2 infection and mRNA vaccination were revealed by linear discriminant analysis. Full article
(This article belongs to the Special Issue Glycomics and Glycosylation Disorders)
Show Figures

Figure 1

Other

Jump to: Research

18 pages, 1134 KiB  
Opinion
Mechanisms of Formation of Antibodies against Blood Group Antigens That Do Not Exist in the Body
by Alexander A. Mironov, Maksim A. Savin, Anna V. Zaitseva, Ivan D. Dimov and Irina S. Sesorova
Int. J. Mol. Sci. 2023, 24(20), 15044; https://doi.org/10.3390/ijms242015044 - 10 Oct 2023
Viewed by 2364
Abstract
The system of the four different human blood groups is based on the oligosaccharide antigens A or B, which are located on the surface of blood cells and other cells including endothelial cells, attached to the membrane proteins or lipids. After transfusion, the [...] Read more.
The system of the four different human blood groups is based on the oligosaccharide antigens A or B, which are located on the surface of blood cells and other cells including endothelial cells, attached to the membrane proteins or lipids. After transfusion, the presence of these antigens on the apical surface of endothelial cells could induce an immunological reaction against the host. The final oligosaccharide sequence of AgA consists of Gal-GlcNAc-Gal (GalNAc)-Fuc. AgB contains Gal-GlcNAc-Gal (Gal)-Fuc. These antigens are synthesised in the Golgi complex (GC) using unique Golgi glycosylation enzymes (GGEs). People with AgA also synthesise antibodies against AgB (group A [II]). People with AgB synthesise antibodies against AgA (group B [III]). People expressing AgA together with AgB (group AB [IV]) do not have these antibodies, while people who do not express these antigens (group O [0; I]) synthesise antibodies against both antigens. Consequently, the antibodies are synthesised against antigens that apparently do not exist in the body. Here, we compared the prediction power of the main hypotheses explaining the formation of these antibodies, namely, the concept of natural antibodies, the gut bacteria-derived antibody hypothesis, and the antibodies formed as a result of glycosylation mistakes or de-sialylation of polysaccharide chains. We assume that when the GC is overloaded with lipids, other less specialised GGEs could make mistakes and synthesise the antigens of these blood groups. Alternatively, under these conditions, the chylomicrons formed in the enterocytes may, under this overload, linger in the post-Golgi compartment, which is temporarily connected to the endosomes. These compartments contain neuraminidases that can cleave off sialic acid, unmasking these blood antigens located below the acid and inducing the production of antibodies. Full article
(This article belongs to the Special Issue Glycomics and Glycosylation Disorders)
Show Figures

Figure 1

Back to TopTop