scholarly journals Surface Glycan Modification of Cellular Nanosponges to Promote SARS-CoV-2 Inhibition

2021 ◽  
Author(s):  
Xiangzhao Ai ◽  
Dan Wang ◽  
Anna Honko ◽  
Yaou Duan ◽  
Igor Gavrish ◽  
...  
Keyword(s):  
Glycan Modification

scholarly journals Structural analysis of broiler chicken small intestinal mucin O-glycan modification by Clostridium perfringens

2019 ◽  
Vol 98 (10) ◽  
pp. 5074-5088 ◽  
Author(s):  
Jaclyn L MacMillan ◽  
Sara D Vicaretti ◽  
Benjamin Noyovitz ◽  
Xiaohui Xing ◽  
Kristin E Low ◽  
...  
Keyword(s):  
Structural Analysis ◽  
Clostridium Perfringens ◽  
Broiler Chicken ◽  
Intestinal Mucin ◽  
Small Intestinal ◽  
Glycan Modification

scholarly journals Antibody blood-brain barrier efflux is modulated by glycan modification

2017 ◽  
Vol 1861 (9) ◽  
pp. 2228-2239 ◽  
Author(s):  
John M. Finke ◽  
Kari R. Ayres ◽  
Ryan P. Brisbin ◽  
Hali A. Hill ◽  
Emily E. Wing ◽  
...  
Keyword(s):  
Blood Brain Barrier ◽  
Brain Barrier ◽  
Blood Brain ◽  
Glycan Modification

scholarly journals Characterizing Protein Glycosylation through On-Chip Glycan Modification and Probing

2016 ◽  
Vol 88 (23) ◽  
pp. 11584-11592 ◽  
Author(s):  
Bryan S. Reatini ◽  
Elliot Ensink ◽  
Brian Liau ◽  
Jessica Y. Sinha ◽  
Thomas W. Powers ◽  
...  
Keyword(s):  
Protein Glycosylation ◽  
On Chip ◽  
Glycan Modification

The role of N-Glycan modification of TNFR1 in inflammatory microglia activation

2015 ◽  
Vol 32 (9) ◽  
pp. 685-693 ◽  
Author(s):  
Lijian Han ◽  
Dongmei Zhang ◽  
Tao Tao ◽  
Xiaolei Sun ◽  
Xiaojuan Liu ◽  
...  
Keyword(s):  
Microglia Activation ◽  
Glycan Modification

scholarly journals Identification, Characterization, and Biosynthesis of a NovelN-Glycan Modification in the Fruiting Body of the BasidiomyceteCoprinopsis cinerea

2010 ◽  
Vol 285 (14) ◽  
pp. 10715-10723 ◽  
Author(s):  
Reto Buser ◽  
Zbigniew Lazar ◽  
Sonja Käser ◽  
Markus Künzler ◽  
Markus Aebi
Keyword(s):  
Fruiting Body ◽  
Glycan Modification

scholarly journals Complex N-Glycans Are Important for Normal Fruit Ripening and Seed Development in Tomato

2021 ◽  
Vol 12 ◽  
Author(s):  
Heidi Kaulfürst-Soboll ◽  
Melanie Mertens-Beer ◽  
Randolf Brehler ◽  
Markus Albert ◽  
Antje von Schaewen
Keyword(s):  
Rna Interference ◽  
Fruit Ripening ◽  
Reproductive Stage ◽  
Pcr Analysis ◽  
Plant Responses ◽  
Rt Pcr ◽  
Signaling Crosstalk ◽  
Long Time ◽  
Glycan Modification

Complex N-glycan modification of secretory glycoproteins in plants is still not well understood. Essential in animals, where a lack of complex N-glycans is embryo-lethal, their presence in plants seemed less relevant for a long time mostly because Arabidopsis thaliana cgl1 mutants lacking N-acetyl-glucosaminyltransferase I (GNTI, the enzyme initiating complex N-glycan maturation in the Golgi apparatus) are viable and showed only minor impairments regarding stress tolerance or development. A different picture emerged when a rice (Oryza sativa) gntI T-DNA mutant was found to be unable to reach the reproductive stage. Here, we report on tomato (Solanum lycopersicum) lines that showed severe impairments upon two RNA interference (RNAi) approaches. Originally created to shed light on the role of core α1,3-fucose and β1,2-xylose residues in food allergy, plants with strongly reduced GNTI activity developed necrotic fruit-attached stalks and early fruit drop combined with patchy incomplete ripening. Correspondingly, semiquantitative RT-PCR of the abscission zone (az) revealed an increase of abscission markers. Also, GNTI-RNA interference (RNAi) plants were more susceptible to sporadic infection. To obtain vital tomatoes with comparable low allergenic potential, Golgi α-mannosidase II (MANII) was chosen as the second target. The resulting phenotypes were oppositional: MANII-reduced plants carried normal-looking fruits that remained attached for extended time without signs of necrosis. Fruits contained no or only few, but enlarged, seeds. Furthermore, leaves developed rolled-up rims simultaneously during the reproductive stage. Trials to cross MANII-reduced plants failed, while GNTI-reduced plants could be (back-)crossed, retaining their characteristic phenotype. This phenotype could not be overcome by ethephon or indole-3-acetic acid (IAA) application, but the latter was able to mimic patchy fruit ripening in wild-type. Phytohormones measured in leaves and 1-aminocyclopropane-1-carboxylic acid (ACC) contents in fruits showed no significant differences. Together, the findings hint at altered liberation/perception of protein-bound N-glycans, known to trigger auxin-like effects. Concomitantly, semiquantitative RT-PCR analysis revealed differences in auxin-responsive genes, indicating the importance of complex N-glycan modification for hormone signaling/crosstalk. Another possible role of altered glycoprotein life span seems subordinate, as concluded from transient expression of Arabidopsis KORRIGAN KOR1-GFP fusion proteins in RNAi plants of Nicotiana benthamiana. In summary, our analyses stress the importance of complex N-glycan maturation for normal plant responses, especially in fruit-bearing crops like tomato.

scholarly journals Combining functional metagenomics and glycoanalytics to identify enzymes that facilitate structural characterization of sulfated N-glycans

2021 ◽  
Vol 20 (1) ◽  
Author(s):  
Léa Chuzel ◽  
Samantha L. Fossa ◽  
Madison L. Boisvert ◽  
Samanta Cajic ◽  
René Hennig ◽  
...  
Keyword(s):  
Pituitary Hormones ◽  
Biological Functions ◽  
Functional Metagenomics ◽  
Specific Detection ◽  
Terminal Position ◽  
Capillary Gel Electrophoresis ◽  
Laser Induced Fluorescence Detection ◽  
Ability To Act ◽  
Glycan Modification

Abstract Background Sulfate modification of N-glycans is important for several biological functions such as clearance of pituitary hormones or immunoregulation. Yet, the prevalence of this N-glycan modification and its functions remain largely unexplored. Characterization of N-glycans bearing sulfate modifications is hampered in part by a lack of enzymes that enable site-specific detection of N-glycan sulfation. In this study, we used functional metagenomic screening to identify enzymes that act upon sulfated N-acetylglucosamine (GlcNAc). Using multiplexed capillary gel electrophoresis with laser-induced fluorescence detection (xCGE-LIF) -based glycoanalysis we proved their ability to act upon GlcNAc-6-SO4 on N-glycans. Results Our screen identified a sugar-specific sulfatase that specifically removes sulfate from GlcNAc-6-SO4 when it is in a terminal position on an N-glycan. Additionally, in the absence of calcium, this sulfatase binds to the sulfated glycan but does not remove the sulfate group, suggesting it could be used for selective isolation of sulfated N-glycans. Further, we describe isolation of a sulfate-dependent hexosaminidase that removes intact GlcNAc-6-SO4 (but not asulfated GlcNAc) from a terminal position on N-glycans. Finally, the use of these enzymes to detect the presence of sulfated N-glycans by xCGE-LIF is demonstrated. Conclusion The present study demonstrates the feasibility of using functional metagenomic screening combined with glycoanalytics to discover enzymes that act upon chemical modifications of glycans. The discovered enzymes represent new specificities that can help resolve the presence of GlcNAc-6-SO4 in N-glycan structural analyses.

scholarly journals A Systematic Review on the Implications of O-linked Glycan Branching and Truncating Enzymes on Cancer Progression and Metastasis

Cells ◽  
2020 ◽  
Vol 9 (2) ◽  
pp. 446 ◽  
Author(s):  
Rohitesh Gupta ◽  
Frank Leon ◽  
Sanchita Rauth ◽  
Surinder K. Batra ◽  
Moorthy P. Ponnusamy
Keyword(s):  
Systematic Review ◽  
Cancer Progression ◽  
Protein Interactions ◽  
Biological Function ◽  
Cancer Growth ◽  
Post Translational Modifications ◽  
Comprehensive Review ◽  
Downstream Signaling ◽  
Multiple Cancers ◽  
Glycan Modification

Glycosylation is the most commonly occurring post-translational modifications, and is believed to modify over 50% of all proteins. The process of glycan modification is directed by different glycosyltransferases, depending on the cell in which it is expressed. These small carbohydrate molecules consist of multiple glycan families that facilitate cell–cell interactions, protein interactions, and downstream signaling. An alteration of several types of O-glycan core structures have been implicated in multiple cancers, largely due to differential glycosyltransferase expression or activity. Consequently, aberrant O-linked glycosylation has been extensively demonstrated to affect biological function and protein integrity that directly result in cancer growth and progression of several diseases. Herein, we provide a comprehensive review of several initiating enzymes involved in the synthesis of O-linked glycosylation that significantly contribute to a number of different cancers.

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