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Advances in Glycobiology

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

Deadline for manuscript submissions: closed (15 March 2022) | Viewed by 5475

Special Issue Editors


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Guest Editor
Department of Biochemistry and Molecular Biology, Faculty of Science, University of Rajshahi, Rajshahi 6205, Bangladesh
Interests: protein biochemistry; lectin-glycan interaction; structural glycobiology; anticancer drug development; nanomedicines; antibiofilm and antifungal activities; multidrug resistance

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Guest Editor
School of Sciences, Yokohama City University, 22-2, Seto, Kanazawa-Ku, Yokohama 236-0027, Japan
Interests: glycobiology; lectins; marine invertebrates
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Glycans are molecular codes for molecular communication in living systems. Diversities of carbohydrate chains characterized by the specific enzymes orient the various phenomenon in normal and abnormal. Since glycans are present both in and on cells being affected with the external environments, this field has the advantage of providing a perspective to understand the cellular mechanisms from the peripheral.

For this reason, glycobiology provides new viewpoints day by day as an interdisciplinary and cutting-edge field for focusing on weak but specific interactions in cells. Being able to comprehensively understand the evolution of glycans and their recognition molecules possessed by all living organisms will lead to the discovery of new perspectives in future life and environmental sciences. In addition, highly sensitive diagnostics have advanced due to the code and decipherment of sugar chains, and new drugs focusing on sugar chains will develop.

This Special Issue "Advances in Glycobiology" welcomes articles and reviews relating to the wide topics of current glycoscience and glycoengineering. We also expect that this accumulation of knowledge will provide clues to elucidate the issue of COVID-19, in addition to many other diseases and biological mechanisms.

Dr. Imtiaj Hasan
Prof. Dr. Yasuhiro Ozeki
Guest Editors

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

  • antimicrobial activity
  • astrobiology
  • body defense
  • cell regulatory activity
  • glycoconjugates
  • glycosides
  • lectins
  • oligosaccharides
  • polysaccharides
  • purification

Published Papers (2 papers)

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Research

10 pages, 278 KiB  
Article
N-Glycosylation Patterns across the Age-Related Macular Degeneration Spectrum
by Ivona Bućan, Jelena Škunca Herman, Iris Jerončić Tomić, Olga Gornik, Zoran Vatavuk, Kajo Bućan, Gordan Lauc and Ozren Polašek
Molecules 2022, 27(6), 1774; https://doi.org/10.3390/molecules27061774 - 8 Mar 2022
Cited by 3 | Viewed by 1629
Abstract
The pathogenesis of age-related macular degeneration (AMD) remains elusive, despite numerous research studies. Therefore, we aimed to investigate the changes of plasma and IgG-specific N-glycosylation across the disease severity spectrum. We examined 2835 subjects from the 10.001 Dalmatians project, originating from the [...] Read more.
The pathogenesis of age-related macular degeneration (AMD) remains elusive, despite numerous research studies. Therefore, we aimed to investigate the changes of plasma and IgG-specific N-glycosylation across the disease severity spectrum. We examined 2835 subjects from the 10.001 Dalmatians project, originating from the isolated Croatian islands of Vis and Korčula. All subjects were classified into four groups, namely (i) bilateral AMD, (ii) unilateral AMD, (iii) early-onset drusen, and (iv) controls. We analysed plasma and IgG N-glycans measured by HPLC and their association with retinal fundus photographs. There were 106 (3.7%) detected cases of AMD; 66 of them were bilateral. In addition, 45 (0.9%) subjects were recorded as having early-onset retinal drusen. We detected several interesting differences across the analysed groups, suggesting that N-glycans can be used as a biomarker for AMD. Multivariate analysis suggested a significant decrease in the immunomodulatory bi-antennary glycan structures in unilateral AMD (adjusted odds ratio 0.43 (95% confidence interval 0.22–0.79)). We also detected a substantial increase in the pro-inflammatory tetra-antennary plasma glycans in bilateral AMD (7.90 (2.94–20.95)). Notably, some of these associations were not identified in the aggregated analysis, where all three disease stages were collapsed into a single category, suggesting the need for better-refined phenotypes and the use of disease severity stages in the analysis of more complex diseases. Age-related macular degeneration progression is characterised by the complex interplay of various mechanisms, some of which can be detected by measuring plasma and IgG N-glycans. As opposed to a simple case-control study, more advanced and refined study designs are needed to understand the pathogenesis of complex diseases. Full article
(This article belongs to the Special Issue Advances in Glycobiology)
9 pages, 1470 KiB  
Communication
Diverse Localization Patterns of an R-Type Lectin in Marine Annelids
by Sarkar M. Abe Kawsar, Imtiaj Hasan, Sultana Rajia, Yasuhiro Koide, Yuki Fujii, Ryuhei Hayashi, Masao Yamada and Yasuhiro Ozeki
Molecules 2021, 26(16), 4799; https://doi.org/10.3390/molecules26164799 - 7 Aug 2021
Cited by 1 | Viewed by 2380
Abstract
Lectins facilitate cell–cell contact and are critical in many cellular processes. Studying lectins may help us understand the mechanisms underlying tissue regeneration. We investigated the localization of an R-type lectin in a marine annelid (Perinereis sp.) with remarkable tissue regeneration abilities. Perinereis [...] Read more.
Lectins facilitate cell–cell contact and are critical in many cellular processes. Studying lectins may help us understand the mechanisms underlying tissue regeneration. We investigated the localization of an R-type lectin in a marine annelid (Perinereis sp.) with remarkable tissue regeneration abilities. Perinereis nuntia lectin (PnL), a galactose-binding lectin with repeating Gln-X-Trp motifs, is derived from the ricin B-chain. An antiserum was raised against PnL to specifically detect a 32-kDa lectin in the crude extracts from homogenized lugworms. The antiserum detected PnL in the epidermis, setae, oblique muscle, acicula, nerve cord, and nephridium of the annelid. Some of these tissues and organs also produced Galactose (Gal) or N-acetylgalactosamine (GalNAc), which was detected by fluorescent-labeled plant lectin. These results indicated that the PnL was produced in the tissues originating from the endoderm, mesoderm, and ectoderm. Besides, the localizing pattern of PnL partially merged with the binding pattern of a fluorescent-labeled mushroom lectin that binds to Gal and GalNAc. It suggested that PnL co-localized with galactose-containing glycans in Annelid tissue; this might be the reason PnL needed to be extracted with haptenic sugar, such as d-galactose, in the buffer. Furthermore, we found that a fluorescein isothiocyanate-labeled Gal/GalNAc-binding mushroom lectin binding pattern in the annelid tissue overlapped with the localizing pattern of PnL. These findings suggest that lectin functions by interacting with Gal-containing glycoconjugates in the tissues. Full article
(This article belongs to the Special Issue Advances in Glycobiology)
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