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Current Advances in Protein Glycosylation
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Current Advances in Protein Glycosylation

A special issue of Molecules (ISSN 1420-3049). This special issue belongs to the section "Bioorganic Chemistry".

Deadline for manuscript submissions: closed (1 March 2020) | Viewed by 20007

Special Issue Editor

Dr. François Foulquier

E-Mail Website
Guest Editor
Structural and Functional Glycobiology Unit, Université de Lille, Lille, France
Interests: protein glycosylation synthesis and metabolism; congenital disorders of glycosylation; endoplasmic reticulum associated degradation; Golgi homeostasis; manganese; ER–Golgi vesicular trafficking; free oligosaccharides

Special Issue Information

Dear Colleagues,

The field of protein glycosylation is scientifically and technologically increasing remarkably. Structurally complex and heterogeneous glycans on proteins govern many fundamental processes, such as protein conformation, stability, clearance, subcellular localization, receptor activation, cell signaling, and adhesion. The glycan code (glycocode), although far from being fully deciphered, is capital as abnormal protein glycosylation is found to be associated with diseases such as congenital disorders of glycosylation, cancer, inflammation, and immunity and neurodegenerative diseases. This Special Issue aims to cover all aspects of protein glycosylation as related to their metabolism, regulation, structural analysis, and cellular and molecular functions in physiological and pathological conditions.This Special Issue will welcome contributions (research articles and reviews) in all areas of protein glycosylation, including fundamental studies on the molecular basis of glycan biosynthesis in human health and diseases, the function of glycans at cellular and animal levels as well as the up-to-date technologies such as glycoproteomics, metabolic oligosaccharide engineering (MOE) to analyze the complexity of the glycocode.

Dr. François Foulquier
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. Molecules 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

  • Glycoproteins
  • Glycocode
  • N-glycosylation
  • O-glycosylation
  • Mannosylation
  • O-GlcNAc modification
  • Proteoglycan/glycosaminoglycans
  • ER protein glycosylation
  • Golgi protein glycosylation
  • Glycosyltransferases
  • Glycosidases
  • Lectins
  • Co-translational modification
  • Post-translational modification
  • Glycan binding proteins
  • Mucins
  • Glycomics
  • Glycoproteomics
  • Metabolic oligosaccharide engineering (MOE)
  • Metabolic diseases linked to protein glycosylation
  • Acquired diseases linked to protein glycosylation

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Published Papers (3 papers)

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Research

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14 pages, 2201 KiB  
Article
Sialic Acid Metabolic Engineering of Breast Cancer Cells Interferes with Adhesion and Migration
by Manimozhi Nagasundaram, Rüdiger Horstkorte and Vinayaga Srinivasan Gnanapragassam
Molecules 2020, 25(11), 2632; https://doi.org/10.3390/molecules25112632 - 5 Jun 2020
Cited by 16 | Viewed by 4010
Abstract
Breast cancer is the most frequent cancer diagnosed in women and the second most common cancer-causing death worldwide. The major problem around the management of breast cancer is its high heterogeneity and the development of therapeutic resistance. Therefore, understanding the fundamental breast cancer [...] Read more.
Breast cancer is the most frequent cancer diagnosed in women and the second most common cancer-causing death worldwide. The major problem around the management of breast cancer is its high heterogeneity and the development of therapeutic resistance. Therefore, understanding the fundamental breast cancer biology is crucial for better diagnosis and therapy. Protein sialylation is a key posttranslational modification of glycoproteins, which is also involved in tumor progression and metastasis. Increased expression of sialic acids (Sia) can interfere in receptor–ligand interactions and might protect tumor cells from the immune system. Furthermore, Sia content on the cell membrane plays a role in cancer resistance towards chemo- and radiation therapy. In this study, we glycoengineered MCF-7 breast cancer cells using a series of non-natural Sia precursors, which are prolonged in their acyl side chain. We observed a significant reduction in the natural Sia (N-Acetylneuraminic acid) expression after cultivation of MCF-7 cells with these Sia precursors. In addition, the expression of polySia, a unique glycosylation of the neural cell adhesion molecule NCAM, which interferes with cell adhesion, was decreased. We conclude that sialic acid engineering i) opens up novel opportunities to study the biological role of Sia in breast cancer and ii) provides a toolbox to examine the sialic acid-dependent complex cellular alterations in breast cancer cell biology. Full article
(This article belongs to the Special Issue Current Advances in Protein Glycosylation)
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25 pages, 1899 KiB  
Article
Potential Plasticity of the Mannoprotein Repertoire Associated to Mycobacterium tuberculosis Virulence Unveiled by Mass Spectrometry-Based Glycoproteomics
by Laure Tonini, Bashir Sadet, Alexandre Stella, David Bouyssié, Jérôme Nigou, Odile Burlet-Schiltz and Michel Rivière
Molecules 2020, 25(10), 2348; https://doi.org/10.3390/molecules25102348 - 18 May 2020
Cited by 6 | Viewed by 4283
Abstract
To date, Mycobacterium tuberculosis (Mtb) remains the world’s greatest infectious killer. The rise of multidrug-resistant strains stresses the need to identify new therapeutic targets to fight the epidemic. We previously demonstrated that bacterial protein-O-mannosylation is crucial for Mtb infectiousness, renewing the [...] Read more.
To date, Mycobacterium tuberculosis (Mtb) remains the world’s greatest infectious killer. The rise of multidrug-resistant strains stresses the need to identify new therapeutic targets to fight the epidemic. We previously demonstrated that bacterial protein-O-mannosylation is crucial for Mtb infectiousness, renewing the interest of the bacterial-secreted mannoproteins as potential drug-targetable virulence factors. The difficulty of inventorying the mannoprotein repertoire expressed by Mtb led us to design a stringent multi-step workflow for the reliable identification of glycosylated peptides by large-scale mass spectrometry-based proteomics. Applied to the differential analyses of glycoproteins secreted by the wild-type Mtb strain—and by its derived mutant invalidated for the protein-O-mannosylating enzyme PMTub—this approach led to the identification of not only most already known mannoproteins, but also of yet-unknown mannosylated proteins. In addition, analysis of the glycoproteome expressed by the isogenic recombinant Mtb strain overexpressing the PMTub gene revealed an unexpected mannosylation of proteins, with predicted or demonstrated functions in Mtb growth and interaction with the host cell. Since in parallel, a transient increased expression of the PMTub gene has been observed in the wild-type bacilli when infecting macrophages, our results strongly suggest that the Mtb mannoproteome may undergo adaptive regulation during infection of the host cells. Overall, our results provide deeper insights into the complexity of the repertoire of mannosylated proteins expressed by Mtb, and open the way to novel opportunities to search for still-unexploited potential therapeutic targets. Full article
(This article belongs to the Special Issue Current Advances in Protein Glycosylation)
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Review

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31 pages, 1801 KiB  
Review
Heparan Sulfate Proteoglycans Biosynthesis and Post Synthesis Mechanisms Combine Few Enzymes and Few Core Proteins to Generate Extensive Structural and Functional Diversity
by Thibault Annaval, Rebekka Wild, Yoann Crétinon, Rabia Sadir, Romain R. Vivès and Hugues Lortat-Jacob
Molecules 2020, 25(18), 4215; https://doi.org/10.3390/molecules25184215 - 14 Sep 2020
Cited by 59 | Viewed by 11334
Abstract
Glycosylation is a common and widespread post-translational modification that affects a large majority of proteins. Of these, a small minority, about 20, are specifically modified by the addition of heparan sulfate, a linear polysaccharide from the glycosaminoglycan family. The resulting molecules, heparan sulfate [...] Read more.
Glycosylation is a common and widespread post-translational modification that affects a large majority of proteins. Of these, a small minority, about 20, are specifically modified by the addition of heparan sulfate, a linear polysaccharide from the glycosaminoglycan family. The resulting molecules, heparan sulfate proteoglycans, nevertheless play a fundamental role in most biological functions by interacting with a myriad of proteins. This large functional repertoire stems from the ubiquitous presence of these molecules within the tissue and a tremendous structural variety of the heparan sulfate chains, generated through both biosynthesis and post synthesis mechanisms. The present review focusses on how proteoglycans are “gagosylated” and acquire structural complexity through the concerted action of Golgi-localized biosynthesis enzymes and extracellular modifying enzymes. It examines, in particular, the possibility that these enzymes form complexes of different modes of organization, leading to the synthesis of various oligosaccharide sequences. Full article
(This article belongs to the Special Issue Current Advances in Protein Glycosylation)
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