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New Insights into Protein Glycosylation II

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

Deadline for manuscript submissions: 30 September 2024 | Viewed by 2652

Special Issue Editor


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Guest Editor
School of Pharmaceutical Sciences, University of Shizuoka, Shizuoka 422-8526, Japan
Interests: glycoproteomics; protein quality control; protein folding; EGF repeats; O-glycosylation; O-glucosylation; mass spectrometry; glycosyltransferase; notch signaling; biohchemistry; glycobiology; cancer biology
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Special Issue Information

Dear Colleagues,

Our first Special Issue on protein glycosylation was a great success (https://www.mdpi.com/journal/molecules/special_issues/molecules_glycoproteomics), with its excellent original papers and review articles. I believe that this contributed in no small measure to our integrated understanding of life. At the same time, we were able to reaffirm that there are still some things we do not understand, such as the heterogeneity and functional diversity of glycans. Therefore, as a guest editor, I am launching a second Special Issue on protein glycosylation.

Protein glycosylation includes N-linked glycosylation and mucin-type O-linked glycosylation starting with GalNAc in addition to O-Fuc, O-Gal, O-Glc, extracellular and intracellular O-GlcNAc, O-Man and O-Xyl, and C-Man. As in the first Special Issue, adopting an interdisciplinary approach, this Special Issue will showcase the structures/functions and analytical methods of protein glycosylation. Their functions may be involved in, but are not limited to, diverse biological processes such as cellular signaling, immunity, neural function, pathological conditions such as cancer, and viral infections, including COVID-19. The Special Issue will accept regular original Articles and Reviews. (Please note that the former includes Communications of preliminary, but significant results).

Prof. Dr. Hideyuki Takeuchi
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

  • O-glycosylation
  • N-glycosylation
  • C-mannosylation
  • glycosaminoglycans
  • nucleocytoplasmic O-GlcNAc
  • glycosyltransferase
  • human disease
  • congenital disorders of glycosylation
  • cancer
  • glycan analysis

Related Special Issue

Published Papers (3 papers)

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Research

13 pages, 3133 KiB  
Article
Comparative Conformational Analysis of Acyclic Sugar Alcohols Ribitol, Xylitol and d-Arabitol by Solution NMR and Molecular Dynamics Simulations
by Shiho Ohno, Noriyoshi Manabe, Jun Uzawa and Yoshiki Yamaguchi
Molecules 2024, 29(5), 1072; https://doi.org/10.3390/molecules29051072 - 29 Feb 2024
Viewed by 727
Abstract
Ribitol (C5H12O5) is an acyclic sugar alcohol that was recently identified in O-mannose glycan on mammalian α-dystroglycan. The conformation and dynamics of acyclic sugar alcohols such as ribitol are dependent on the stereochemistry of the [...] Read more.
Ribitol (C5H12O5) is an acyclic sugar alcohol that was recently identified in O-mannose glycan on mammalian α-dystroglycan. The conformation and dynamics of acyclic sugar alcohols such as ribitol are dependent on the stereochemistry of the hydroxyl groups; however, the dynamics are not fully understood. To gain insights into the conformation and dynamics of sugar alcohols, we carried out comparative analyses of ribitol, d-arabitol and xylitol by a crystal structure database search, solution NMR analysis and molecular dynamics (MD) simulations. The crystal structures of the sugar alcohols showed a limited number of conformations, suggesting that only certain stable conformations are prevalent among all possible conformations. The three-bond scholar coupling constants and exchange rates of hydroxyl protons were measured to obtain information on the backbone torsion angle and possible hydrogen bonding of each hydroxyl group. The 100 ns MD simulations indicate that the ribitol backbone has frequent conformational transitions with torsion angles between 180 and ±60, while d-arabitol and xylitol showed fewer conformational transitions. Taking our experimental and computational data together, it can be concluded that ribitol is more flexible than d-arabitol or xylitol, and the flexibility is at least in part defined by the configuration of the OH groups, which may form intramolecular hydrogen bonds. Full article
(This article belongs to the Special Issue New Insights into Protein Glycosylation II)
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11 pages, 1918 KiB  
Article
Efficient Escorting Strategy for Aggregation-Prone Notch EGF Repeats with Sparcl1
by Yuji Kondo, Yuxin Li and Tetsuya Okajima
Molecules 2024, 29(5), 1031; https://doi.org/10.3390/molecules29051031 - 27 Feb 2024
Viewed by 705
Abstract
Epidermal growth factor (EGF) repeats are present in various proteins and form well-defined structures with three disulfide bonds. One representative protein is the Notch receptor. Each EGF repeat contains unique atypical O-linked glycans, such as O-linked N-acetylglucosamine (O-GlcNAc). To [...] Read more.
Epidermal growth factor (EGF) repeats are present in various proteins and form well-defined structures with three disulfide bonds. One representative protein is the Notch receptor. Each EGF repeat contains unique atypical O-linked glycans, such as O-linked N-acetylglucosamine (O-GlcNAc). To generate a monoclonal antibody against the O-GlcNAc moiety in mouse Notch1, we expressed the recombinant C-terminal His6-tagged Notch1 EGF14-15 protein in HEK293T cells to prepare the immunogen. Most of the proteins were not secreted and showed higher molecular weight ladders in the cell lysate, suggesting protein aggregation. To overcome this issue, we fused Sparcl1 as an extracellular escorting tag to the N-terminus of Notch1 EGF14-15. The fusion protein was efficiently secreted extracellularly without protein aggregates in the lysates. Following PreScission protease treatment, Notch1 EGF14-15 was efficiently released from the escorting tag. Notch1 EGF14-15 prepared using this method was indeed O-GlcNAcylated. The optimal length of the escorting tag was determined by generating deletion mutants to improve the extracellular secretion of EGF14-15. Hence, a large amount of EGF14-15 was successfully prepared from the culture supernatant of HEK293T cells, which were otherwise prone to aggregation. Full article
(This article belongs to the Special Issue New Insights into Protein Glycosylation II)
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16 pages, 5236 KiB  
Article
GlcNAc6ST2/CHST4 Is Essential for the Synthesis of R-10G-Reactive Keratan Sulfate/Sulfated N-Acetyllactosamine Oligosaccharides in Mouse Pleural Mesothelium
by Yoshiko Takeda-Uchimura, Midori Ikezaki, Tomoya O. Akama, Yoshito Ihara, Fabrice Allain, Kazuchika Nishitsuji and Kenji Uchimura
Molecules 2024, 29(4), 764; https://doi.org/10.3390/molecules29040764 - 7 Feb 2024
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Abstract
We recently showed that 6-sulfo sialyl N-acetyllactosamine (LacNAc) in O-linked glycans recognized by the CL40 antibody is abundant in the pleural mesothelium under physiological conditions and that these glycans undergo complementary synthesis by GlcNAc6ST2 (encoded by Chst4) and GlcNAc6ST3 (encoded [...] Read more.
We recently showed that 6-sulfo sialyl N-acetyllactosamine (LacNAc) in O-linked glycans recognized by the CL40 antibody is abundant in the pleural mesothelium under physiological conditions and that these glycans undergo complementary synthesis by GlcNAc6ST2 (encoded by Chst4) and GlcNAc6ST3 (encoded by Chst5) in mice. GlcNAc6ST3 is essential for the synthesis of R-10G-positive keratan sulfate (KS) in the brain. The predicted minimum epitope of the R-10G antibody is a dimeric asialo 6-sulfo LacNAc. Whether R-10G-reactive KS/sulfated LacNAc oligosaccharides are also present in the pleural mesothelium was unknown. The question of which GlcNAc6STs are responsible for R-10G-reactive glycans was an additional issue to be clarified. Here, we show that R-10G-reactive glycans are as abundant in the pulmonary pleura as CL40-reactive glycans and that GlcNAc6ST3 is only partially involved in the synthesis of these pleural R-10G glycans, unlike in the adult brain. Unexpectedly, GlcNAc6ST2 is essential for the synthesis of R-10G-positive KS/sulfated LacNAc oligosaccharides in the lung pleura. The type of GlcNAc6ST and the magnitude of its contribution to KS glycan synthesis varied among tissues in vivo. We show that GlcNAc6ST2 is required and sufficient for R-10G-reactive KS synthesis in the lung pleura. Interestingly, R-10G immunoreactivity in KSGal6ST (encoded by Chst1) and C6ST1 (encoded by Chst3) double-deficient mouse lungs was markedly increased. MUC16, a mucin molecule, was shown to be a candidate carrier protein for pleural R-10G-reactive glycans. These results suggest that R-10G-reactive KS/sulfated LacNAc oligosaccharides may play a role in mesothelial cell proliferation and differentiation. Further elucidation of the functions of sulfated glycans synthesized by GlcNAc6ST2 and GlcNAc6ST3, such as R-10G and CL40 glycans, in pathological conditions may lead to a better understanding of the underlying mechanisms of the physiopathology of the lung mesothelium. Full article
(This article belongs to the Special Issue New Insights into Protein Glycosylation II)
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