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Javier Ramos-Soriano, M Carmen de la Fuente, Noelia de la Cruz, Rute C Figueiredo, Javier Rojo, José J Reina
The high-mannose oligosaccharide (or its corresponding Man9 epitope) is the most abundant structure present in pathogen envelope glycoproteins. These glycans play a key role in the pathogenesis of several pathogens and also in the communication with the immune system. Understanding the mechanism of action of these glycans requires the access to pure and chemically well-defined structures in reasonable amounts. The synthesis of these complex branched oligosaccharides is not trivial and few syntheses are reported in the literature with several synthetic and purification steps and low overall yields...
October 20, 2017: Organic & Biomolecular Chemistry
Zehui Zhang, Fan Wang, Chuandao Chen, Zhou Zheng, Jude Juventus Aweya, Yueling Zhang
Hemocyanin is an important multifunctional non-specific immune molecule. In this study, we purified lectin binding and non-lectin binding hemocyanin from Litopenaeus vannamei using Concanavalin A (ConA) lectin affinity chromatography (designated HMC-C and HMC-NC, respectively). Analysis of the carbohydrate content showed that HMC-C had about 20 times as much carbohydrate as HMC-NC. 54 and 42 peaks were observed in HMC-C and HMC-NC by HPLC, which reduced to 49 and 6 peaks, respectively, when digested with trypsin and repurified with ConA lectin column...
October 16, 2017: Immunology Letters
Víctor M Castillo-Acosta, Jan Balzarini, Dolores González-Pacanowska
No abstract text is available yet for this article.
October 16, 2017: Trends in Parasitology
Cheng-Te Hsiao, Hung-Wei Cheng, Chi-Ming Huang, Hao-Ru Li, Meng-Hsin Ou, Jie-Rong Huang, Kay-Hooi Khoo, Helen Wenshin Yu, Yin-Quan Chen, Yang-Kao Wang, Arthur Chiou, Jean-Cheng Kuo
Directed cell migration is an important step in effective wound healing and requires the dynamic control of the formation of cell-extracellular matrix interactions. Plasma fibronectin is an extracellular matrix glycoprotein present in blood plasma that plays crucial roles in modulating cellular adhesion and migration and thereby helping to mediate all steps of wound healing. In order to seek safe sources of plasma fibronectin for its practical use in wound dressing, we isolated fibronectin from human (homo) and porcine plasma and demonstrated that both have a similar ability as a suitable substrate for the stimulation of cell adhesion and for directing cell migration...
September 19, 2017: Oncotarget
Muchena J Kailemia, Gege Xu, Maurice Y Wong, Qiongyu Li, Elisha Goonatilleke, Frank Leon, Carlito B Lebrilla
The review focuses on recent aspects (last three years) of glycosylation analyses that provide relevant information about cancer. It includes recent development in glycan and protein enrichment methods for discovery of cancer markers. It will however focus on the recent technological developments in mass spectrometry (MS), bioinformatics and separation methods as they apply toward identifying cancer markers. More specifically, it will cover advances in matrix-assisted laser desorption/ionization (MALDI), electrospray ionization (ESI), capillary electrophoresis (CE), and liquid chromatography (LC) coupled to mass spectrometry...
October 19, 2017: Analytical Chemistry
Esteban Cruz, Joel Cain, Ben Crossett, Veysel Kayser
The study of influenza virus evolution in humans has revealed a significant role of glycosylation profile alterations in the viral glycoproteins - hemagglutinin (HA) and neuraminidase (NA), in the emergence of both seasonal and pandemic strains. Viral antigenic drift can modify the number and location of glycosylation sites, altering a wide range of biological activities and the antigenic properties of the strain. In view of the key role of glycans in determining antigenicity, elucidating the glycosylation profiles of influenza strains is a requirement towards the development of improved vaccines...
October 19, 2017: Human Vaccines & Immunotherapeutics
Ruixiang Blake Zheng, Sabine A F Jégouzo, Maju Joe, Yu Bai, Huu-Anh Tran, Ke Shen, Jörn Saupe, Li Xia, Md Faiaz Ahmed, Yu-Hsuan Liu, Pratap Subhashrao Patil, Ashish Tripathi, Shang-Cheng Hung, Maureen E Taylor, Todd L Lowary, Kurt Drickamer
An array of homogenous glycans representing all the major carbohydrate structures present in the cell wall of the human pathogen Mycobacterium tuberculosis and other mycobacteria has been probed with a panel of glycan-binding receptors expressed on cells of the mammalian innate immune system. The results provide an overview of interactions between mycobacterial glycans and receptors that mediate uptake and survival in macrophages, dendritic cells and sinusoidal endothelial cells. A subset of the wide variety of glycan structures present on mycobacterial surfaces interact with cells of the innate immune system through the receptors tested...
October 19, 2017: ACS Chemical Biology
Gianluca Accogli, Giovanni Scillitani, Donatella Mentino, Salvatore Desantis
The Octopus vulgaris farming is impaired by the high mortality of the paralarvae during the first month of life. Several factors have been investigated in this regard, but no data exist on the body surface mucus, which represents the interface with the outside environment. This study included morphometric analysis and glycoconjugates characterization of skin mucus in reared Octopus vulgaris paralarvae during the first month of life. Four types of mucous cells were distinguished:  mucous 1 (m1) and mucous 2 (m2) cells were scattered in the mantle epidermis, mucous 3 (m3) and mucous 4 (m4) in the epithelium surrounding the sucker...
September 12, 2017: European Journal of Histochemistry: EJH
Gerard Artigas, Joao Monteiro, Hiroshi Hinou, Shin-Ichiro Nishimura, Bernd Lepenies, Fayna Garcia Martin
The macrophage galactose-type lectin (MGL) recognises glycan moieties exposed by pathogens and malignant cells. Particularly, mucin-1 (MUC1) glycoprotein presents an altered glycosylation in several cancers. To estimate the ability of distinct MGL orthologs to recognise aberrant glycan cores in mucins, we applied evanescent-field detection to a versatile MUC1-like glycopeptide microarray platform. Here, as binding was sequence-dependent, we demonstrated that not only sugars, but also peptide region, impacts the recognition of murine MGL1 (mMGL1)...
October 18, 2017: Journal of Medicinal Chemistry
Jennifer Schoberer, Yun-Ji Shin, Ulrike Vavra, Christiane Veit, Richard Strasser
Protein N-glycosylation is an essential posttranslational modification which is initiated in the endoplasmic reticulum. In plants, the N-glycans play a pivotal role for protein folding and quality control. Through the interaction of glycan processing and binding reactions mediated by ER-resident glycosidases and specific carbohydrate binding proteins, the N-glycans contribute to the adoption of a native protein conformation. Properly folded glycoproteins are released from these processes and allowed to continue their transit to the Golgi where further processing and maturation of N-glycans leads to the formation of more complex structures with different functions...
2018: Methods in Molecular Biology
Zhigang Wu, Yunpeng Liu, Lei Li, Xiu-Feng Wan, He Zhu, Yuxi Guo, Mohui Wei, Wanyi Guan, Peng George Wang
N-Glycans are normally involved in crucial physiological and disease processes by interactions with glycan-binding proteins. So far structurally defined N-glycans have been good candidates for glycan binding study. Herein, a class of homogeneous asymmetric N-glycans was synthesized by coupling glycan-oxazoline and N-glycans using EndoM N175Q catalyzed quick glycan extension. Branch-biased binding and spacial inhibition caused by the bulky group on the other branch of N-glycan were observed in glycan protein interactions involving lectins and these glycans by glycan microarray study...
October 18, 2017: Organic & Biomolecular Chemistry
Yining Huang, Ron Orlando
The biologic activity of IgG molecules is modulated by its crystallizable fragment N-glycosylation, and thus, the analysis of IgG glycosylation is critical. A standard approach to analyze glycosylation of IgGs involves the release of the N-glycans by the enzyme peptide N-glycosidase F, which cleaves the linkage between the asparagine residue and innermost N-acetylglucosamine (GlcNAc) of all N-glycans except those containing a 3-linked fucose attached to the reducing terminal GlcNAc residue. The importance of obtaining complete glycan release for accurate quantitation led us to investigate the kinetics of this de-glycosylation reaction for IgG glycopeptides and to determine the effect of glycan structure and amino acid sequence on the rate of glycan release from glycopeptides of IgGs...
October 9, 2017: Journal of Biomolecular Techniques: JBT
Kristina Poljak, Jörg Breitling, Robert Gauss, George Rugarabamu, Mauro Pellanda, Markus Aebi
N-linked protein glycosylation is an essential and highly conserved post-translational modification in eukaryotes. The transfer of a glycan from a lipid-linked oligosaccharide (LLO) donor to the asparagine residue of a nascent polypeptide chain is catalyzed by an oligosaccharyltransferase (OST) in the lumen of the endoplasmic reticulum (ER). Trypanosoma brucei encodes three paralogue single protein OSTs called TbSTT3A, TbSTT3B and TbSTT3C that can functionally complement the Saccharomyces cerevisiae OST, making it an ideal experimental system to study the fundamental properties of OST activity...
October 17, 2017: Journal of Biological Chemistry
Ling Chong Wang, Liu Qing Di, Jun Song Li, Li Hong Hu, Jian Ming Cheng, Hao Wu
Over the past decades, numerous Mollusca species have received more attention in development and utilization as valuable bio-resources. Many efforts have been focused on investigating mollusk polysaccharides because of their rich content, ease of extraction, diversified sorts, specific structure, various biofunctions and potent activities. To date, many mollusks, especially species of gastropods, bivalves, or cephalopods, have been reported containing polysaccharide compounds in tissues with abundant amount, and most of polysaccharides are obtainable through combining techniques of extraction, separation and purification...
October 17, 2017: Critical Reviews in Food Science and Nutrition
Lucia Paolini, Flavia Orizio, Sara Busatto, Annalisa Radeghieri, Roberto Bresciani, Paolo Bergese, Eugenio Monti
Sialidases are glycohydrolases that remove terminal sialic acid residues from oligosaccharides, glycolipids and glycoproteins. The plasma membrane-associated sialidase NEU3 is involved in the fine tuning of sialic acid containing glycans directly on the cell surface and plays relevant roles in important biological phenomena such as cell differentiation, molecular recognition and cancer transformation. Extracellular vesicles are membranous structures with a diameter of 0.03-1 m released by cells and detectable in blood, urine, as well as in culture media...
October 17, 2017: Biochemistry
James Sy-Keen Woon, Mukram M Mackeen, Rosli M Illias, Nor M Mahadi, William J Broughton, Abdul Munir Abdul Murad, Farah Diba Abu Bakar
BACKGROUND: Aspergillus niger, along with many other lignocellulolytic fungi, has been widely used as a commercial workhorse for cellulase production. A fungal cellulase system generally includes three major classes of enzymes i.e., β-glucosidases, endoglucanases and cellobiohydrolases. Cellobiohydrolases (CBH) are vital to the degradation of crystalline cellulose present in lignocellulosic biomass. However, A. niger naturally secretes low levels of CBH. Hence, recombinant production of A...
2017: PeerJ
Mark S Han, John T Simpson
The analysis of protein glycosylation by mass spectrometry (MS) has been a challenging technical problem. Quantification by HPLC of N-linked glycans can be executed by the use of peptide-N-glycosidase F to release them from the protein, followed by attachment of a fluorescent label and subsequent fluorescence detection. Similar quantification of O-linked glycans is not possible, as a result of the lack of a universal deglycosylation enzyme. Site-specific analyses by MS, such as the use of proteases to digest the glycoprotein, are difficult to use for quantification of glycans, as a result of the presence of miscleavages...
October 3, 2017: Journal of Biomolecular Techniques: JBT
Xuexia Li, Xiaoyan Xu, Xiongjian Rao, Yinping Tian, Wen Yi
Recruitment of human endogenous antibodies to target and eliminate tumor cells is a promising therapeutic strategy in the biomedical field. Current antibody-recruiting molecules are typically bi-functional agents that utilize cell-surface receptor binding property for targeting. This approach has intrinsic limitations due to the heterogeneity of tumor cells and the limited number of receptors on the cell surface. Here we report a targeting strategy based on remodeling of cell surface glycans through metabolic engineering and bioorthogonal chemical ligation...
October 10, 2017: Carbohydrate Research
Yasuhiko Kizuka, Miyako Nakano, Yoshiki Yamaguchi, Kazuki Nakajima, Ritsuko Oka, Keiko Sato, Chien-Tai Ren, Tsui-Ling Hsu, Chi-Huey Wong, Naoyuki Taniguchi
Fucosylation is a glycan modification critically involved in cancer and inflammation. Although potent fucosylation inhibitors are useful for basic and clinical research, only a few inhibitors have been developed. Here, we focus on a fucose analog with an alkyne group, 6-alkynyl-fucose (6-Alk-Fuc), which is used widely as a detection probe for fucosylated glycans, but is also suggested for use as a fucosylation inhibitor. Our glycan analysis using lectin and mass spectrometry demonstrated that 6-Alk-Fuc is a potent and general inhibitor of cellular fucosylation, with much higher potency than the existing inhibitor, 2-fluoro-fucose (2-F-Fuc)...
September 19, 2017: Cell Chemical Biology
Montserrat Mancera-Arteu, Estela Giménez, José Barbosa, Rosa Peracaula, Victòria Sanz-Nebot
In this work, a μZIC-HILIC-MS/MS methodology was established in negative ion mode for the characterization of glycan isomers. The possibility to separate the glycan isomers by the μZIC-HILIC strategy coupled to a high resolution tandem mass spectrometry detection permitted us to obtain valuable information about each glycan structure. The most important diagnostic ion fragments previously described to characterize structural features of glycans, were evaluated in this study using hAGP as model glycoprotein...
October 23, 2017: Analytica Chimica Acta
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