Special Issue "Glycosylation—The Most Diverse Post-Translational Modification"
Deadline for manuscript submissions: 15 December 2021.
Interests: glycobiology; glycosylation; glycosyltransferases
Interests: lectins; carbohydrate-binding proteins; protein–carbohydrate interactions; carbohydrate recognition; glycosylation; biological activity; physiological importance; defense and immunity; stress proteins; glycobiology
Special Issues, Collections and Topics in MDPI journals
Special Issue in Molecules: Ribosome-Inactivating Proteins--Commemorative Issue in Honor of Professor Fiorenzo Stirpe
Special Issue in International Journal of Molecular Sciences: Plant Lectins: From Model Species to Crop Plants
Special Issue in International Journal of Molecular Sciences: Protein–Carbohydrate Interactions: Structure–Function Relationships
Glycosylation plays an important role in several types of biological and biochemical recognition processes ranging from fertilization and development to pathological events, such as infection, allergy, inflammation or cancer. Furthermore, the analyses of carbohydrate-based relations (host finding, recognition and invasion) between parasite and their hosts or intermediate hosts are a growing field of interest due to the implications in diagnostics, vaccine development, novel therapies and immune responses. Nowadays, the influence of the glycosylation on the mobility of pathogens between species is of particular interest.
This Special Issue aims to highlight aspects of protein glycosylation in all phyla. Contributions (research articles, reviews, communications) that cover the structural elucidation, the function, the biosynthesis or degradation of glycans and the characterization of enzymes involved in these processes are very welcome, as well as papers dealing with methodical improvements for the analysis of glycans or enzymes recognizing carbohydrate structures.
Prof. Dr. Erika Staudacher
Prof. Dr. Els Van Damme
Prof. Dr. Guy Smagghe
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 papers will be 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. Biomolecules is an international peer-reviewed open access monthly 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 2000 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.
The below list represents only planned manuscripts. Some of these manuscripts have not been received by the Editorial Office yet. Papers submitted to MDPI journals are subject to peer-review.
Title: Structural differences between non-sialylated and de-sialylated N-glycans of the human brain revealed by standardized graphitic carbon chromatography
Authors: Johannes Helm; Friedrich Altmann
Affiliation: Altmann lab at BOKU Vienna
Abstract: The brain N-glycome is known to be crucial for many biological functions, including the involvement in neuronal diseases. Although large structural studies of brain N-glycans were recently carried out, a deep isomer-specific analysis with definitive structures given is still required, as indicated by the recent discovery of novel structures with galactosylated bisecting GlcNAc. Here, we present a detailed, isomer-specific analysis of the human brain N-glycome based on standardized porous graphitic carbon (PGC)-LC-MS/MS. To achieve this goal, we biosynthesized glycans with substitutions typically occurring in the brain N-glycome and acquired their normalized retention times. Comparison of these values with the standardized retention times of neutral and desialylated N-glycan fractions of human brain led to an unambiguous assignment of most peaks, including linkage-isomers. Fundamental differences in the glycan-structures between the “naturally neutral” and desialylated glycans were found at the composition- and isomer-level. Arguably, the neutral and sialylated N-glycans derive from diverging biosynthetic pathways and are biosynthetically finished end products rather than just intermediates on their way to sialylation. Furthermore, the presented method proved to be a powerful tool for structural glycomics as substantiated also by the unveiling of four HNK-1 containing N-glycans.
Title: O-methylated N-glycans distinguish mosses from higher land plants
Authors: David Stenitzer; Reka Moscai; Eva Decker; Friedrich Altmann
Affiliation: Altmann lab at BOKU Vienna
Abstract: A stunning variety of N-glycan structures has emerged in the animal kingdom. In plants, however, N-glycosylation appears as conservative and strictly uniform. From archaic land plants to all kinds of gymno- and angiosperms, land plants express structures with the common pentasaccharide core substituted with xylose, core α1,3-fucose, terminal GlcNAc residues and Lewis A determinants. In contrast, green algae – though being “lower” plants - biosynthesize a plethora of species-specific unusual N-glycan structures, often with O-methylation. Mosses, a group of phylogenetically ancient land plants, were hitherto seen as harboring a N-glycosylation machinery identical to that of higher land plants. We have, however, analyzed the N-glycomes of several moss species using MALDI-TOF/TOF, PGC-MS/MS and GC-MS. While all species contained the plant-typical heptasaccharide with no, one or two terminal GlcNAc residues, many species exhibited MS signals with 14.02 Da increments as characteristic for O-methylation. Throughout all analyzed moss N-glycans the level of methylation differed strongly even in the same family. This first finding of methylation of N-glycans in land plants reminds of the presumable phylogenetic relation of mosses to green algae, where O-methylation of mannose and many other monosaccharides is a common trait.