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Cells
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Functional Glycomics
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Functional Glycomics

A special issue of Cells (ISSN 2073-4409).

Deadline for manuscript submissions: closed (30 September 2019) | Viewed by 25820

Special Issue Editor

Dr. Hyun Joo An

E-Mail Website
Guest Editor
1. Asia Glycomics Reference Site, Chungnam National University, Daejeon 34134, Korea
2. Graduate School of Analytical Science and Technology, #455 College of Engineering II, Chungnam National University, Daejeon, Korea
Interests: bioanalytical mass spectrometry; glycoconjugates; glycomics; brain glycosylation; cancer biomarker; therapeutic glycoprotein

Special Issue Information

Dear Colleagues,

Glycosylation is a biological process involving a rich, complex, and highly regulated repertoire of cellular glycans that are attached to biological molecules such as proteins (glycoproteins) and lipids (glycolipids). Approximately little more than 70% of all proteins typically expressed in a cell undergo this modification. Glycosylation is thought to be the most complex post-translational modification, since it involves many enzymatic steps. Glycans participate in many biological processes, such as cell adhesion, cell signaling, cell–cell recognition, and cell–matrix interactions. They are also key functional components in protein biopharmaceuticals and are employed as disease biomarkers, viral vaccines, prebiotics, and in a host of other biomedical applications. As a result, glycomics, the study of the biological role of glycans produced by cells or tissues under specific time, location, and environmental conditions, has been rapidly expanding. However, because glycosylation, unlike other biological processes such as DNA and protein biosynthesis, is not a template-driven process, glycans displayed on a biomolecule are not readily predictable. Therefore, identifying and studying the glycan structures present in glycosylated molecules is an essential step to understand this important class of biomolecules and interpret complex biological processes.

In this Special Issue of Cells, we invite contributions, in the form of either original research articles or reviews, on aspects related to functional glycomics. Papers concerning technical issues or applications are also welcome.

Prof. Hyun Joo An
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. Cells is an international peer-reviewed open access semimonthly 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 2700 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

  • Glycomics
  • Glycotechnology
  • Glycosylation in Cellular Mechanism
  • Glycosylation Biosynthesis

Published Papers (4 papers)

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Research

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14 pages, 2158 KiB  
Article
Comprehensive Profiling of Surface Gangliosides Extracted from Various Cell Lines by LC-MS/MS
by Jua Lee, Heeyoun Hwang, Sumin Kim, Jaeyun Hwang, Jaekyung Yoon, Dongtan Yin, Sun Il Choi, Yun-Hee Kim, Yong-Sam Kim and Hyun Joo An
Cells 2019, 8(11), 1323; https://doi.org/10.3390/cells8111323 - 26 Oct 2019
Cited by 12 | Viewed by 5436
Abstract
Gangliosides act as a surface marker at the outer cellular membrane and play key roles in cancer cell invasion and metastasis. Despite the biological importance of gangliosides, they have been still poorly characterized due to the lack of effective analytical tools. Herein, we [...] Read more.
Gangliosides act as a surface marker at the outer cellular membrane and play key roles in cancer cell invasion and metastasis. Despite the biological importance of gangliosides, they have been still poorly characterized due to the lack of effective analytical tools. Herein, we performed molecular profiling and structural elucidation of intact gangliosides in various cell lines including CFPAC1, A549, NCI-H358, MCF7, and Caski. We identified and quantified a total of 76 gangliosides on cell membrane using C18 LC-MS/MS. Gangliosides found in each cell line exhibited high complexity and diversity both qualitatively and quantitatively. The most abundant species was GM3(d34:1) in CFPAC1, NCI-H358, and MCF7, while GM2(d34:1) and GM1(d34:1) were major components in A549 and Caski, respectively. Notably, glycan moieties showed more diversity between cancer cell lines than ceramide moieties. In addition, noncancerous pancreatic cell line (hTERT/HPNE) could be distinguished by gangliosides containing different levels of sialic acid compared with cancerous pancreatic cell line (CFPAC1). These results clearly demonstrated the feasibility of our analytical platform to comprehensive profile of cell surface gangliosides for identifying cell types and subgrouping cancer cell types. Full article
(This article belongs to the Special Issue Functional Glycomics)
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21 pages, 3458 KiB  
Article
N-Glycomic and Transcriptomic Changes Associated with CDX1 mRNA Expression in Colorectal Cancer Cell Lines
by Stephanie Holst, Jennifer L. Wilding, Kamila Koprowska, Yoann Rombouts and Manfred Wuhrer
Cells 2019, 8(3), 273; https://doi.org/10.3390/cells8030273 - 22 Mar 2019
Cited by 18 | Viewed by 6138
Abstract
The caudal-related homeobox protein 1 (CDX1) is a transcription factor, which is important in the development, differentiation, and homeostasis of the gut. Although the involvement of CDX genes in the regulation of the expression levels of a few glycosyltransferases has been shown, associations [...] Read more.
The caudal-related homeobox protein 1 (CDX1) is a transcription factor, which is important in the development, differentiation, and homeostasis of the gut. Although the involvement of CDX genes in the regulation of the expression levels of a few glycosyltransferases has been shown, associations between glycosylation phenotypes and CDX1 mRNA expression have hitherto not been well studied. Triggered by our previous study, we here characterized the N-glycomic phenotype of 16 colon cancer cell lines, selected for their differential CDX1 mRNA expression levels. We found that high CDX1 mRNA expression associated with a higher degree of multi-fucosylation on N-glycans, which is in line with our previous results and was supported by up-regulated gene expression of fucosyltransferases involved in antenna fucosylation. Interestingly, hepatocyte nuclear factors (HNF)4A and HNF1A were, among others, positively associated with high CDX1 mRNA expression and have been previously proven to regulate antenna fucosylation. Besides fucosylation, we found that high CDX1 mRNA expression in cancer cell lines also associated with low levels of sialylation and galactosylation and high levels of bisection on N-glycans. Altogether, our data highlight a possible role of CDX1 in altering the N-glycosylation of colorectal cancer cells, which is a hallmark of tumor development. Full article
(This article belongs to the Special Issue Functional Glycomics)
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Review

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24 pages, 917 KiB  
Review
Role of Protein Glycosylation in Host-Pathogen Interaction
by Borong Lin, Xue Qing, Jinling Liao and Kan Zhuo
Cells 2020, 9(4), 1022; https://doi.org/10.3390/cells9041022 - 20 Apr 2020
Cited by 85 | Viewed by 8862
Abstract
Host-pathogen interactions are fundamental to our understanding of infectious diseases. Protein glycosylation is one kind of common post-translational modification, forming glycoproteins and modulating numerous important biological processes. It also occurs in host-pathogen interaction, affecting host resistance or pathogen virulence often because glycans regulate [...] Read more.
Host-pathogen interactions are fundamental to our understanding of infectious diseases. Protein glycosylation is one kind of common post-translational modification, forming glycoproteins and modulating numerous important biological processes. It also occurs in host-pathogen interaction, affecting host resistance or pathogen virulence often because glycans regulate protein conformation, activity, and stability, etc. This review summarizes various roles of different glycoproteins during the interaction, which include: host glycoproteins prevent pathogens as barriers; pathogen glycoproteins promote pathogens to attack host proteins as weapons; pathogens glycosylate proteins of the host to enhance virulence; and hosts sense pathogen glycoproteins to induce resistance. In addition, this review also intends to summarize the roles of lectin (a class of protein entangled with glycoprotein) in host-pathogen interactions, including bacterial adhesins, viral lectins or host lectins. Although these studies show the importance of protein glycosylation in host-pathogen interaction, much remains to be discovered about the interaction mechanism. Full article
(This article belongs to the Special Issue Functional Glycomics)
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20 pages, 3209 KiB  
Review
Glycobiology of Human Fungal Pathogens: New Avenues for Drug Development
by Danielle J. Lee, Holly O’Donnell, Françoise H. Routier, Joe Tiralongo and Thomas Haselhorst
Cells 2019, 8(11), 1348; https://doi.org/10.3390/cells8111348 - 30 Oct 2019
Cited by 12 | Viewed by 4828
Abstract
Invasive fungal infections (IFI) are an increasing threat to the developing world, with fungal spores being ubiquitous and inhaled every day. Some fungal species are commensal organisms that are part of the normal human microbiota, and, as such, do not pose a threat [...] Read more.
Invasive fungal infections (IFI) are an increasing threat to the developing world, with fungal spores being ubiquitous and inhaled every day. Some fungal species are commensal organisms that are part of the normal human microbiota, and, as such, do not pose a threat to the immune system. However, when the natural balance of this association is disturbed or the host’s immune system is compromised, these fungal pathogens overtake the organism, and cause IFI. To understand the invasiveness of these pathogens and to address the growing problem of IFI, it is essential to identify the cellular processes of the invading organism and their virulence. In this review, we will discuss the prevalence and current options available to treat IFI, including recent reports of drug resistance. Nevertheless, the main focus of this review is to describe the glycobiology of human fungal pathogens and how various components of the fungal cell wall, particularly cell wall polysaccharides and glycoconjugates, are involved in fungal pathogenicity, their biosynthesis and how they can be potentially exploited to develop novel antifungal treatment options. We will specifically describe the nucleotide sugar transporters (NSTs) that are important in fungal survival and suggest that the inhibition of fungal NSTs may potentially be useful to prevent the establishment of fungal infections. Full article
(This article belongs to the Special Issue Functional Glycomics)
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