Relevant bibliographies by topics / Glycans

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  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers
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Academic literature on the topic 'Glycans'

Author: Grafiati
Published: 4 June 2021
Last updated: 7 September 2023

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Journal articles on the topic "Glycans"

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Barre, Annick, Els J. M. Van Damme, Bernard Klonjkowski, Mathias Simplicien, Jan Sudor, Hervé Benoist, and Pierre Rougé. "Legume Lectins with Different Specificities as Potential Glycan Probes for Pathogenic Enveloped Viruses." Cells 11, no. 3 (January 20, 2022): 339. http://dx.doi.org/10.3390/cells11030339.

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Pathogenic enveloped viruses are covered with a glycan shield that provides a dual function: the glycan structures contribute to virus protection as well as host cell recognition. The three classical types of N-glycans, in particular complex glycans, high-mannose glycans, and hybrid glycans, together with some O-glycans, participate in the glycan shield of the Ebola virus, influenza virus, human cytomegalovirus, herpes virus, human immunodeficiency virus, Lassa virus, and MERS-CoV, SARS-CoV, and SARS-CoV-2, which are responsible for respiratory syndromes. The glycans are linked to glycoproteins that occur as metastable prefusion glycoproteins on the surface of infectious virions such as gp120 of HIV, hemagglutinin of influenza, or spike proteins of beta-coronaviruses. Plant lectins with different carbohydrate-binding specificities and, especially, mannose-specific lectins from the Vicieae tribe, such as pea lectin and lentil lectin, can be used as glycan probes for targeting the glycan shield because of their specific interaction with the α1,6-fucosylated core Man3GlcNAc2, which predominantly occurs in complex and hybrid glycans. Other plant lectins with Neu5Ac specificity or GalNAc/T/Tn specificity can also serve as potential glycan probes for the often sialylated complex glycans and truncated O-glycans, respectively, which are abundantly distributed in the glycan shield of enveloped viruses. The biomedical and therapeutical potential of plant lectins as antiviral drugs is discussed.
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Sun, Xiuping, Hieng Chiong Tie, Bing Chen, and Lei Lu. "Glycans function as a Golgi export signal to promote the constitutive exocytic trafficking." Journal of Biological Chemistry 295, no. 43 (August 21, 2020): 14750–62. http://dx.doi.org/10.1074/jbc.ra120.014476.

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Most proteins in the secretory pathway are glycosylated. However, the role of glycans in membrane trafficking is still unclear. Here, we discovered that transmembrane secretory cargos, such as interleukin 2 receptor α subunit or Tac, transferrin receptor, and cluster of differentiation 8a, unexpectedly displayed substantial Golgi localization when their O-glycosylation was compromised. By quantitatively measuring their Golgi residence times, we found that the observed Golgi localization of O-glycan–deficient cargos is due to their slow Golgi export. Using a superresolution microscopy method that we previously developed, we revealed that O-glycan–deficient Tac chimeras localize at the interior of the trans-Golgi cisternae. O-Glycans were observed to be both necessary and sufficient for the efficient Golgi export of Tac chimeras. By sequentially introducing O-glycosylation sites to ST6GAL1, we demonstrated that O-glycan's effect on Golgi export is probably additive. Finally, the finding that N-glycosylated GFP substantially reduces the Golgi residence time of a Tac chimera suggests that N-glycans might have a similar effect. Therefore, both O- and N-glycans might function as a generic Golgi export signal at the trans-Golgi to promote the constitutive exocytic trafficking.
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Shirakawa, Asuka, Yoshiyuki Manabe, and Koichi Fukase. "Recent Advances in the Chemical Biology of N-Glycans." Molecules 26, no. 4 (February 16, 2021): 1040. http://dx.doi.org/10.3390/molecules26041040.

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Asparagine-linked N-glycans on proteins have diverse structures, and their functions vary according to their structures. In recent years, it has become possible to obtain high quantities of N-glycans via isolation and chemical/enzymatic/chemoenzymatic synthesis. This has allowed for progress in the elucidation of N-glycan functions at the molecular level. Interaction analyses with lectins by glycan arrays or nuclear magnetic resonance (NMR) using various N-glycans have revealed the molecular basis for the recognition of complex structures of N-glycans. Preparation of proteins modified with homogeneous N-glycans revealed the influence of N-glycan modifications on protein functions. Furthermore, N-glycans have potential applications in drug development. This review discusses recent advances in the chemical biology of N-glycans.
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Cheng, Bo, Qi Tang, Che Zhang, and Xing Chen. "Glycan Labeling and Analysis in Cells and In Vivo." Annual Review of Analytical Chemistry 14, no. 1 (June 5, 2021): 363–87. http://dx.doi.org/10.1146/annurev-anchem-091620-091314.

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As one of the major types of biomacromolecules in the cell, glycans play essential functional roles in various biological processes. Compared with proteins and nucleic acids, the analysis of glycans in situ has been more challenging. Herein we review recent advances in the development of methods and strategies for labeling, imaging, and profiling of glycans in cells and in vivo. Cellular glycans can be labeled by affinity-based probes, including lectin and antibody conjugates, direct chemical modification, metabolic glycan labeling, and chemoenzymatic labeling. These methods have been applied to label glycans with fluorophores, which enables the visualization and tracking of glycans in cells, tissues, and living organisms. Alternatively, labeling glycans with affinity tags has enabled the enrichment of glycoproteins for glycoproteomic profiling. Built on the glycan labeling methods, strategies enabling cell-selective and tissue-specific glycan labeling and protein-specific glycan imaging have been developed. With these methods and strategies, researchers are now better poised than ever to dissect the biological function of glycans in physiological or pathological contexts.
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Bushkin, G. Guy, Daniel M. Ratner, Jike Cui, Sulagna Banerjee, Manoj T. Duraisingh, Cameron V. Jennings, Jeffrey D. Dvorin, et al. "Suggestive Evidence for Darwinian Selection against Asparagine-Linked Glycans of Plasmodium falciparum and Toxoplasma gondii." Eukaryotic Cell 9, no. 2 (September 25, 2009): 228–41. http://dx.doi.org/10.1128/ec.00197-09.

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ABSTRACT We are interested in asparagine-linked glycans (N-glycans) of Plasmodium falciparum and Toxoplasma gondii, because their N-glycan structures have been controversial and because we hypothesize that there might be selection against N-glycans in nucleus-encoded proteins that must pass through the endoplasmic reticulum (ER) prior to threading into the apicoplast. In support of our hypothesis, we observed the following. First, in protists with apicoplasts, there is extensive secondary loss of Alg enzymes that make lipid-linked precursors to N-glycans. Theileria makes no N-glycans, and Plasmodium makes a severely truncated N-glycan precursor composed of one or two GlcNAc residues. Second, secreted proteins of Toxoplasma, which uses its own 10-sugar precursor (Glc3Man5GlcNAc2) and the host 14-sugar precursor (Glc3Man9GlcNAc2) to make N-glycans, have very few sites for N glycosylation, and there is additional selection against N-glycan sites in its apicoplast-targeted proteins. Third, while the GlcNAc-binding Griffonia simplicifolia lectin II labels ER, rhoptries, and surface of plasmodia, there is no apicoplast labeling. Similarly, the antiretroviral lectin cyanovirin-N, which binds to N-glycans of Toxoplasma, labels ER and rhoptries, but there is no apicoplast labeling. We conclude that possible selection against N-glycans in protists with apicoplasts occurs by eliminating N-glycans (Theileria), reducing their length (Plasmodium), or reducing the number of N-glycan sites (Toxoplasma). In addition, occupation of N-glycan sites is markedly reduced in apicoplast proteins versus some secretory proteins in both Plasmodium and Toxoplasma.
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Geissner, Andreas, Anika Reinhardt, Christoph Rademacher, Timo Johannssen, João Monteiro, Bernd Lepenies, Michel Thépaut, et al. "Microbe-focused glycan array screening platform." Proceedings of the National Academy of Sciences 116, no. 6 (January 22, 2019): 1958–67. http://dx.doi.org/10.1073/pnas.1800853116.

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Interactions between glycans and glycan binding proteins are essential for numerous processes in all kingdoms of life. Glycan microarrays are an excellent tool to examine protein–glycan interactions. Here, we present a microbe-focused glycan microarray platform based on oligosaccharides obtained by chemical synthesis. Glycans were generated by combining different carbohydrate synthesis approaches including automated glycan assembly, solution-phase synthesis, and chemoenzymatic methods. The current library of more than 300 glycans is as diverse as the mammalian glycan array from the Consortium for Functional Glycomics and, due to its microbial focus, highly complementary. This glycan platform is essential for the characterization of various classes of glycan binding proteins. Applications of this glycan array platform are highlighted by the characterization of innate immune receptors and bacterial virulence factors as well as the analysis of human humoral immunity to pathogenic glycans.
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Tsang, Kwong Y., Massimo Fantini, Anjum Zaki, Sharon A. Mavroukakis, Maria Pia Morelli, Christina M. Annunziata, and Philip M. Arlen. "Identification of the O-Glycan Epitope Targeted by the Anti-Human Carcinoma Monoclonal Antibody (mAb) NEO-201." Cancers 14, no. 20 (October 12, 2022): 4999. http://dx.doi.org/10.3390/cancers14204999.

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Truncated O-glycans expressed in cancer cells support tumor progression, and they may serve as potential targets to improve the monitoring and treatment of cancers. Previously, we reported that NEO-201 binds to several tumors expressing tumor-associated CEACAM5 and CEACAM6 variants but does not bind to those expressed in healthy tissues. This specific binding may be associated with the presence of truncated O-glycans attached on the protein sequence of these variants. To evaluate the glycosylation pattern targeted by NEO-201 we performed an O-glycan array consisting of 94 O-glycans. O-glycan profiles were elucidated from the human pancreatic cancer cell line CFPAC-1, human hematological neoplastic cells (HL-60, U937, K562) and human neutrophils. The O-glycan array analysis showed that NEO-201 interacts with core 1-4 O-glycans and that the binding to a specific core 1 O-glycan was the strongest. The O-glycan profiling of the NEO-201-reactive cells CFPAC-1, HL-60, U937 and human neutrophils showed that cells recognized by NEO-201 express mostly core 1 and/or extended core 1 O-glycans. In addition, NEO-201 mediates antibody-dependent cell-mediated cytotoxicity (ADCC) against tumor cells expressing core 1 or extended core 1 O-glycan profiles. These results demonstrated that NEO-201 binds to core 1 and extended core 1 O-glycans expressed in its target cells. Since GalNAc residue can be added onto threonine and serine to form O-glycans, it is very likely that NEO-201 recognizes these O-glycans attached to any protein with amino acid regions containing serine and threonine.
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Wu, Zhengliang L., Anthony D. Person, Yonglong Zou, Andrew J. Burton, Ravinder Singh, Barbara Burroughs, Dan Fryxell, et al. "Differential distribution of N- and O-Glycans and variable expression of sialyl-T antigen on HeLa cells—Revealed by direct fluorescent glycan imaging." Glycobiology 30, no. 7 (January 2, 2020): 454–62. http://dx.doi.org/10.1093/glycob/cwz110.

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Abstract Cells are covered with glycans. The expression and distribution of specific glycans on the surface of a cell are important for various cellular functions. Imaging these glycans is essential to aid elucidation of their biological roles. Here, utilizing methods of direct fluorescent glycan imaging, in which fluorescent sialic acids are directly incorporated into substrate glycans via recombinant sialyltranferases, we report the differential distribution of N- and O-glycans and variable expression of sialyl-T antigen on HeLa cells. While the expression of N-glycans tends to be more peripheral at positions where cell–cell interaction occurs, O-glycan expression is more granular but relatively evenly distributed on positive cells. While N-glycans are expressed on all cells, sialyl-T antigen expression exhibits a wide spectrum of variation with some cells being strongly positive and some cells being almost completely negative. The differential distribution of N- and O-glycans on cell surface reflects their distinctive roles in cell biology.
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Tharmalingam-Jaikaran, T., S. W. Walsh, P. A. McGettigan, O. Potter, W. B. Struwe, A. C. O. Evans, P. M. Rudd, and S. D. Carrington. "N-glycan profiling of bovine follicular fluid at key dominant follicle developmental stages." REPRODUCTION 148, no. 6 (December 2014): 569–80. http://dx.doi.org/10.1530/rep-14-0035.

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Follicular fluid (FF), an important microenvironment for the development of oocytes, contains many proteins that are glycosylated withN-linked glycans. This study aimed i) to present an initial analysis of theN-linked glycan profile of bovine FF using hydrophilic interaction liquid chromatography, anion exchange chromatography, high performance liquid chromatography (HPLC)-based separations and subsequent liquid chromatography–mass spectrometry/mass spectrometry analysis; ii) to determine differences in theN-glycan profile between FF from dominant and subordinate follicles from dairy heifers and lactating dairy cows and iii) to identify alterations in theN-glycan profile of FF during preovulatory follicle development using newly selected, differentiated (preovulatory) and luteinised dominant follicles from dairy heifers and lactating cows. We found that the majority of glycans on bovine FF are based on biantennary hypersialylated structures, where the glycans are sialylated on both the galactose andN-acetylglucosamine terminal sugars. A comparison of FFN-glycans from cows and heifers indicated higher levels of nonsialylated glycans with a lower proportion of sialylated glycans in cows than in heifers. Overall, as the follicle develops from Selection, Differentiation and Luteinisation in both cows and heifers, there is an overall decrease in sialylated structures on FFN-glycans.
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Zhang, Ying, Yuyang Zhu, Yi Lasanajak, David F. Smith, and Xuezheng Song. "O-Benzylhydroxylamine (BHA) as a Cleavable Tag for Isolation and Purification of Reducing Glycans." SLAS TECHNOLOGY: Translating Life Sciences Innovation 25, no. 4 (January 21, 2020): 388–96. http://dx.doi.org/10.1177/2472630319898150.

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Glycoscience has been recognized as an important area in biomedical research. Currently, a major obstacle for glycoscience study is the lack of diverse, biomedically relevant, and complex glycans in quantities sufficient for exploring their structural and functional aspects. Complementary to chemoenzymatic synthesis, natural glycans could serve as a great source of biomedically relevant glycans if they are available in sufficient quantities. We have recently developed oxidative release of natural glycans (ORNG) for large-scale release of N-glycans as free reducing glycans. While free reducing glycans can be readily derivatized with ultraviolet or fluorescent tags for high-performance liquid chromatography (HPLC) and mass spectrometry (MS) analysis, it is difficult to remove tags for the regeneration of free reducing glycans without affecting the structural integrity of glycans. To address this inconvenience, we explored the use of a cleavable tag, O-benzylhydroxylamine (BHA). Free reducing glycans are easily and efficiently labeled with BHA under mild conditions, enabling UV detection during HPLC purification. Individual glycan–BHA conjugates can then be separated using multidimensional HPLC and characterized by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF-MS) and MS/MS. The BHA tag can then be easily removed by palladium-on-carbon (Pd/C)-catalyzed hydrogenation to efficiently regenerate free reducing glycans with little effect on glycan structures. This procedure provides a simple and straightforward way to tag free reducing glycans for purification at a preparative scale using multidimensional HPLC and subsequently recover purified free reducing glycans.
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Dissertations / Theses on the topic "Glycans"

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Bharate, Priya [Verfasser]. "Automated Glycan Assembly of Oligomannose Glycans for Sensing Applications / Priya Bharate." Berlin : Freie Universität Berlin, 2017. http://d-nb.info/1147758336/34.

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Llop, Escorihuela Esther. "Structural analysis of eythropoietin glycans." Doctoral thesis, Universitat Pompeu Fabra, 2008. http://hdl.handle.net/10803/7129.

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La eritropoyetina o EPO es una hormona glicoproteica. En los seres humanos adultos, se produce principalmente en el riñón, en respuesta a la reducción de oxígeno en los tejidos (hipoxia tisular). La EPO estimula la eritropoyesis, es decir, estimula a las células madre de la médula ósea para que aumenten la producción de eritrocitos. La molécula de EPO está formada por una cadena peptídica de 165 aminoácidos que contiene dos puentes disulfuro, un O-glicano (Ser-126), y tres N-glicanos (Asn-24, 38, 83). En conjunto, la glicosilación de esta proteína representa aproximadamente el 40% del peso total (29.4 kDa). La EPO sintetizada con tecnología recombinante (rEPO) se administra como fármaco, desde el año 1989, para el tratamiento de anemias, insuficiencia renal, cancer etc. También se ha observado la utilización de rEPO en deportistas con el fin de aumentar el suministro de oxígeno a los tejidos y así incrementar el rendimiento en deportes de resistencia. En el año 2001, se comercializó una "nueva proteína estimuladora de la eritropoyesis" llamada NESP. Esta proteína es un análogo hiperglicosilado de la EPO que posee dos N-glicanos adicionales (Asn-30, 88). El número y composición de los N-glicanos es muy importante para el metabolismo de estas glicoproteínas, ya que el contenido de carbohidratos (número de ácidos siálicos) determina su vida media. Los métodos que se utilizan actualmente para diferenciar la eritropoyetina endógena urinaria (uEPO) de sus análogos recombinantes (rEPO, NESP) están basados en las diferencias que existen entre sus perfiles isoelectroforéticos (IEF). Se cree que estas diferencias provienen de las células y/o especies en las que se expresan estas glicoproteínas. En este estudio, se llevo a cabo la caracterización estructural de diferentes preparaciones de EPO recombinante. Para ello, se utilizaron las técnicas más comunes en el campo de la glicoproteómica además de otras nuevas, desarrolladas para poder analizar los glicanos de muestras procedentes de geles 2-DE. Los perfiles de glicosilación total de cada una de estas glicoproteínas mostraron características estructurales que pueden facilitar la detección de rEPO y NESP en atletas que abusan de estas sustancias. Un ejemplo es la presencia de Neu5Gc únicamente en fármacos que han sido expresados en células CHO. La metodología desarrollada en este trabajo, podría emplearse también, para el control de calidad de estos fármacos y para el diagnóstico de ciertas patologías.
Erythropoietin (EPO) is a glycoprotein hormone secreted primarily by adult kidneys in response to tissue hypoxia. It is involved in the maturation and ultimately regulation of the level of red blood cells. The EPO molecule comprises a single polypeptide chain of 165 aminoacids with two disulfide bonds, 1 O-linked (Ser-126), and 3 N-linked (Asn-24, 38, 83) glycans representing about 40% of the total mass (29.4 kDa). The recombinant analogue (rEPO), available since 1989 has found widespread use in the treatment of anaemia, renal failure, cancer etc. Besides, rEPO is illicitly used by athletes to boost the delivery of oxygen to the tissue and enhance performance in endurance sports. In 2001, a novel erythropoiesis-stimulating protein (NESP) was also marketed. NESP possesses two additional N-glycans (Asn-30, 88). The number and composition of the N-glycans is very important in the metabolism of this glycoprotein because the carbohydrate content (sialylation degree) determines its half-life time. Current tests to differentiate between urinary endogenous (uEPO) and its recombinant analogues (rEPO, NESP) are based on differences in their iso-electric focussing (IEF) profiles. Those differences are believed to stem from the cells/species in which they are expressed. In this study, the structural characterisation of different rEPO preparations was conducted using standard techniques in the field and developing new ones to address glycans from 2-DE sample preparations. Overall glycosylation profiling of each glycoprotein revealed structural features that may pave the way to the unambiguous detection of rEPOs and NESP abuse, such as the presence of Neu5Gc in CHO cell derived drugs only, and the developed methodology may be also employed for maintaining pharmaceutical quality control and for diagnosing pathologic conditions.
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Jaworek, Christine H. "Synthesis of inositol phosphate glycans /." Thesis, Connect to Dissertations & Theses @ Tufts University, 2000.

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Thesis (Ph.D.)--Tufts University, 2000.
Adviser: Marc d'Alarcao. Submitted to the Dept. of Chemistry. Includes bibliographical references (leaves 262-271). Access restricted to members of the Tufts University community. Also available via the World Wide Web;
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Wilson, Katherine. "The role of glycans in osteogenesis." Thesis, University of York, 2015. http://etheses.whiterose.ac.uk/10403/.

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Glycosylation is an abundant post translational modification of proteins, which occurs in the endoplasmic reticulum and Golgi. Nearly every secreted and plasma membrane localised protein is glycosylated. Mesenchymal stromal/stem cells (MSCs) are adult stem cells that can self-renew and differentiate into multiple cell types including: osteoblasts, adipocytes and chondrocytes. Due to their tri-lineage capacity and their immunoregulatory functions, MSCs are attractive tools for the treatment of multiple diseases and conditions. Key to their use in regenerative medicine is knowledge about what influences a MSC to differentiate into a particular cell type. Despite previous studies describing distinct glycan profiles of cells at different stages of development, whether glycans play a functional role in directing MSC differentiation is currently unknown. Here, utilizing an immortalized primary human MSC line (hTERT-MSCs), the N-glycans from MSCs and osteoblasts were harvested using the Filter aided N-glycan Separation (FANGS) method. Following permethylation, N-glycans were analysed by mass spectrometry (MALDI-TOF/TOF). This method allowed the reliable, quantitative, relative abundance of different glycan structures to be compared between the two cell types for the first time. Complex N-glycans were significantly more abundant in osteoblasts compared to MSCs. The N-glycan profiles of different hTERT-MSC lines were not significantly different, despite variations in differentiation potential. The glycosylation pathway was genetically disrupted by targeting a subunit of the Conserved Oligomeric Complex (COG) with a shRNA. As predicted, since COG is responsible for the tethering of vesicles carrying Golgi resident enzymes, Cog4 knock-down hTERT-MSCs had disrupted N- and O-glycan synthesis. Interestingly, Cog4 knock-down hTERT-MSCs showed reduced osteogenic capacity with reduced levels of mineralised extracellular matrix (ECM). Surprisingly, the chemical inhibition of complex N-glycan synthesis increased ECM mineralisation, whilst inhibition of O-glycan synthesis or proteoglycan sulfation mimicked the Cog4 knock-down cells with reduced mineralisation. These results showed a novel role of both N-and O-glycans in osteogenesis.
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Berry, Eric Zachary 1980. "Bioinformatics and database tools for glycans." Thesis, Massachusetts Institute of Technology, 2004. http://hdl.handle.net/1721.1/27085.

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Thesis (M. Eng. and S.B.)--Massachusetts Institute of Technology, Dept. of Electrical Engineering and Computer Science, 2004.
Includes bibliographical references (leaves 75-76).
Recent advances in biology have afforded scientists with the knowledge that polysaccharides play an active role in modulating cellular activities. Glycosaminoglycans (GAGs) are one such family of polysaccharides that play a very important role in regulating the functions of numerous important signaling molecules and enzymes in the cell. Developing bioinformatics tools has been integral to advancing genomics and proteomics. While these tools have been well-developed to store and process sequence and structure information for proteins and DNA, they are very poorly developed for polysaccharides. Glycan structures pose special problems because of their tremendous information density per fundamental unit, their often-branched structures, and the complicated nature of their building blocks. The GlycoBank, an online database of known GAG structures and functions, has been developed to overcome many of these difficulties by developing a common notation for researchers to describe GAG sequences, a common repository to view known structure-function relationships, and the complex tools and searches needed to facilitate their work. This thesis focuses on the development of GlycoBank. In addition, a large, NIGMS-funded consortium, the Consortium for Functional Glycomics, is a larger database that also aims to store polysaccharide structure-function information of a broader collection of polysaccharides. The ideas and concepts implemented in developing GlycoBank were instrumental in developing databases and bioinformatics tools for the Consortium for Functional Glycomics.
by Eric Zachary Berry.
M.Eng.and S.B.
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Stebbins, Nathan Wilson. "Decoding structure-function relationships of glycans." Thesis, Massachusetts Institute of Technology, 2017. http://hdl.handle.net/1721.1/110887.

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Thesis: Ph. D., Massachusetts Institute of Technology, Department of Biological Engineering, 2017.
Cataloged from PDF version of thesis.
Includes bibliographical references (pages 236-275).
Glycans are an important class of biological molecules that regulate a variety of physiological processes such as signal transduction, tissue development and microbial pathogenesis. However, due to the structural complexity of glycans and the unique intricacies of glycan-protein interactions, elucidating glycan structure-function relationships is challenging. Thus, uncovering the biological function of glycans requires an integrated approach, incorporating structural analysis of glycans, and glycan-proteins interactions with functional analysis. In this thesis, I develop new tools and implement integrated approaches to study glycans and glycan-binding proteins (GBPs). I apply these approaches to study glycans and GBPs in two areas: i) the role of hemagglutinin-glycan receptor specificity in human adaptation and pathogenesis of influenza and ii) the function of glycan regulation of cell-microenvironment interaction in cancer progression. Section 1: Influenza poses a significant public health threat and there is a constant looming threat of a pandemic. Pandemic viruses emerge when avian viruses acquire mutations that enable human adaptation, leading to infection of an antigenically naive host. Influenza Hemagglutinin (HA), and HA-glycan receptor interactions, play a central role in host tropism, transmissibility, and immune recognition. In section one, I develop and apply an integrated approach comprised of structural modeling, inter-amino acid network analysis, biochemical assays, and bioinformatics tools to study the hemagglutinin-glycan interaction and, in some cases, HA's antigenic properties. Using this approach, we i) identify the structural determinants required, and potential mutational paths, for H5N1 to quantitatively switch it's binding specificity to human glycans receptors, ii) identify the mutations that enable the 2013 outbreak H7N9 HA to improve binding to human glycan receptors in the upper respiratory tract, iii) uncover H3N2 strains that are currently circulating in birds and swine that possess features of a virus that could potentially re-emerge and cause a pandemic, and iv) characterize the glycan binding specificity of a novel 2011 Seal H3N8 HA. The approaches implemented here and the findings of these studies provide a framework for improved surveillance of influenza viruses circulating in non-human hosts that pose a pandemic threat. Section 2: Glycans are abundant on the cell surface, and at the cell-ECM interface where they mediate interactions between cells and their microenvironment. Despite this, the function of glycans in cancer progression remains largely understudied. Here, I develop an integrated approach to characterize the cell surface glycome, including N-linked, 0-linked glycans, and HSGAGs. This approach integrates glycogene expression data, analytical tools, and glycan binding protein reagents. I demonstrate that this platform enables rapid and efficient characterization of the N- and 0-linked glycome in a model cell system, representing metastatic versus non-metastatic cancer cells. Next, I apply this integrated approach to uncover new roles of glycans. I study the role that HSGAGs play in regulating cancer stem cell (CSC) activity in breast cancer. Here, we report that SULF1, an HSGAG modifying enzyme, is required for efficient tumor initiation, growth and metastasis of CSCs. Furthermore, we identify a putative mechanism by which SULF1 regulates interactions between CSCs and their microenvironment. The approaches implemented here and the finding of these studies Overall, this thesis provides important tools, approaches and insights to enable and improve the study of glycans and glycan binding proteins. Together the work here provides a framework for decoding structure-function relationship of glycans.
by Nathan Wilson Stebbins.
Ph. D.
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Bohm, Raphael. "Structural Insights into Glycan Interactions of Human Pathogens." Thesis, Griffith University, 2014. http://hdl.handle.net/10072/366018.

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Glycans are major components of every cell surface. In addition to their importance in many physiological processes, glycans play a key role during infection of many pathogens. The identification and characterisation of glycan-pathogen interactions at a molecular and atomic level is therefore a crucial step towards the design of novel antimicrobial drugs and vaccines. Protein functions related to glycan interactions include glycan biosynthesis (glycosyltransferases), glycan recognition (lectins) and glycan degradation (glycosylhydrolases). This thesis investigates structure-function relationships of four glycan binding proteins that are important for the infectivity of three major human pathogens: the polysialyltransferase (polyST) of Neisseria meningitidis serogroup B (NmB), the viral protein 8* (VP8*) of rotavirus, and the hemagglutinin (HA) and the neuraminidase (NA) of influenza A virus (IAV).
Thesis (PhD Doctorate)
Doctor of Philosophy (PhD)
Institute for Glycomics
Science, Environment, Engineering and Technology
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Yosief, Hailemichael. "Synthetic glycans for toxin and pathogen detection." University of Cincinnati / OhioLINK, 2013. http://rave.ohiolink.edu/etdc/view?acc_num=ucin1367936841.

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Prokopishyn, Nicole Lesley. "Integrin Ã3ß1, cancer-associated glycans and colon cancer." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1997. http://www.collectionscanada.ca/obj/s4/f2/dsk3/ftp04/nq23967.pdf.

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Sun, Yan Jenny. "Glycans of cationic peanut, Arachis hypogaea L., peroxidase." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1998. http://www.collectionscanada.ca/obj/s4/f2/dsk2/ftp01/MQ30702.pdf.

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Books on the topic "Glycans"

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Pavão, Mauro S. G., ed. Glycans in Diseases and Therapeutics. Berlin, Heidelberg: Springer Berlin Heidelberg, 2011. http://dx.doi.org/10.1007/978-3-642-16833-8.

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Glycans: Biochemistry, characterization and applications. Hauppauge] New York: Nova Biomedical, Nova Science Publishers, Inc., 2012.

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Pantophlet, Ralph, ed. HIV glycans in infection and immunity. New York, NY: Springer New York, 2014. http://dx.doi.org/10.1007/978-1-4614-8872-9.

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Pantophlet, Ralph. HIV glycans in infection and immunity. New York: Springer, 2014.

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Michèle, Aubery, ed. Glycans in cell interaction and recognition: Therapeutic aspects. Australia: Harwood Academic, 2001.

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Symposium on Biomedical Functions and Biotechnology of Natural and Artificial Polymers (1995 Honolulu, Hawaii). Biomedical functions and biotechnology of natural and artificial polymers: Self-assemblies, hybrid complexes, and biological conjugates of glycans, liposomes, polyethylene glycols, polyisopropylacrylamides, and polypeptides. Mount Prospect, IL: ATL Press, 1996.

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Kilcoyne, Michelle, and Jared Q. Gerlach, eds. Glycan Microarrays. New York, NY: Springer US, 2022. http://dx.doi.org/10.1007/978-1-0716-2148-6.

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Jong, Gerardus de. The physiological significance of transferrin microheterogeneity: An interpretation of the role of N-linked glycans in transferrin and iron metabolism ...Proeefschrift ter verkrijging van de graad van doctor... 1993 ... Rotterdam: [Department of Chemical Pathology, Erasmus University Rotherham?], 1993.

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Rezvani. La glycine. [Arles, France]: Actes sud, 1991.

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P, Ottersen O., and Storm-Mathisen Jon, eds. Glycine neurotransmission. Chichester: Wiley, 1990.

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Book chapters on the topic "Glycans"

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Nakakita, Shin-ichi, and Jun Hirabayashi. "Preparation of Glycan Arrays Using Pyridylaminated Glycans." In Methods in Molecular Biology, 225–35. New York, NY: Springer New York, 2016. http://dx.doi.org/10.1007/978-1-4939-3136-1_16.

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Borsig, Lubor. "Glycans in Cancer." In Glycans in Diseases and Therapeutics, 63–81. Berlin, Heidelberg: Springer Berlin Heidelberg, 2011. http://dx.doi.org/10.1007/978-3-642-16833-8_3.

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Janin-Bussat, Marie-Claire, Elsa Wagner-Rousset, Christine Klinguer-Hamour, Nathalie Corvaia, Alain van Dorsselaer, and Alain Beck. "Antibody Glycans Characterization." In Antibody Engineering, 635–56. Berlin, Heidelberg: Springer Berlin Heidelberg, 2010. http://dx.doi.org/10.1007/978-3-642-01144-3_40.

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Kim, Cheorl-Ho. "Glycans in Glycoimmunology." In Glycobiology of Innate Immunology, 115–98. Singapore: Springer Singapore, 2022. http://dx.doi.org/10.1007/978-981-16-9081-5_4.

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Wong, Chi-Huey. "Chemoenzymatic Synthesis Chemo-enzymatic synthesis of Glycans Glycans : Overview." In Glycoscience: Biology and Medicine, 293–94. Tokyo: Springer Japan, 2014. http://dx.doi.org/10.1007/978-4-431-54841-6_102.

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Pickford, Claire, Rebecca Holley, Kate Meade, and Catherine Merry. "Glycans in Embryonic Stem Cells." In Glycans in Diseases and Therapeutics, 113–37. Berlin, Heidelberg: Springer Berlin Heidelberg, 2011. http://dx.doi.org/10.1007/978-3-642-16833-8_5.

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Zulueta, Medel Manuel L., and Shang-Cheng Hung. "Synthesis of Sulfated Glycans." In Glycoscience: Biology and Medicine, 1–7. Tokyo: Springer Japan, 2014. http://dx.doi.org/10.1007/978-4-431-54836-2_107-1.

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Suenaga, Tadahiro, and Hisashi Arase. "Viral Interactions with Glycans." In Glycoscience: Biology and Medicine, 1–9. Tokyo: Springer Japan, 2014. http://dx.doi.org/10.1007/978-4-431-54836-2_152-1.

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Zulueta, Medel Manuel L., and Shang-Cheng Hung. "Synthesis of Sulfated Glycans." In Glycoscience: Biology and Medicine, 365–71. Tokyo: Springer Japan, 2014. http://dx.doi.org/10.1007/978-4-431-54841-6_107.

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Suenaga, Tadahiro, and Hisashi Arase. "Viral Interactions with Glycans." In Glycoscience: Biology and Medicine, 785–94. Tokyo: Springer Japan, 2014. http://dx.doi.org/10.1007/978-4-431-54841-6_152.

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Conference papers on the topic "Glycans"

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Yoshida, Yukiko, Koji Matsuoka, Tomoki Chiba, Toshiaki Suzuki, Keiji Tanaka, and Tadashi Tai. "N-GLYCANS ARE RECOGNIZED BY E3 UBIQUITIN-LIGASE." In XXIst International Carbohydrate Symposium 2002. TheScientificWorld Ltd, 2002. http://dx.doi.org/10.1100/tsw.2002.430.

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Molhoek, Anoushka K., Joyce Lübbers, Juan J. Garcia-Vellejo, Sandra J. van Vliet, René E. M. Toes, and Yvette van Kooyk. "08.05 How do glycans affect immune cells in ra?" In 37th European Workshop for Rheumatology Research 2–4 March 2017 Athens, Greece. BMJ Publishing Group Ltd and European League Against Rheumatism, 2017. http://dx.doi.org/10.1136/annrheumdis-2016-211055.5.

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Radhakrishnan, Prakash, James A. Grunkemeyer, Henrik Clausen, and Michael A. Hollingsworth. "Abstract A69: TruncatedO-glycans enhance tumorigenicity of pancreatic tumors." In Abstracts: AACR Special Conference on Pancreatic Cancer: Progress and Challenges; June 18-21, 2012; Lake Tahoe, NV. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.panca2012-a69.

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Molhoek, A., L. Hafkenscheid, R. Toes, S. van Vliet, and Y. van Kooyk. "P002 How do glycans affect immune cells in rheumatoid arthritis?" In 38th European Workshop for Rheumatology Research, 22–24 February 2018, Geneva, Switzerland. BMJ Publishing Group Ltd and European League Against Rheumatism, 2018. http://dx.doi.org/10.1136/annrheumdis-2018-ewrr2018.29.

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Saitou, Atsushi, Motoko Takahashi, Saori Yokoyama, Naoki Fujitani, Sigeru Ariki, Atsushi Saito, Kouji Kuronuma, Hirohumi Chiba, and Hiroki Takahashi. "Analysis of the structures and functions of N-glycans of MET." In ERS International Congress 2020 abstracts. European Respiratory Society, 2020. http://dx.doi.org/10.1183/13993003.congress-2020.1646.

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Panzarini, Elisa, Stefania Mariano, and Luciana Dini. "Glycans coated silver nanoparticles induces autophagy and necrosis in HeLa cells." In NANOFORUM 2014. AIP Publishing LLC, 2015. http://dx.doi.org/10.1063/1.4922573.

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Besancon, Camille, Alexandre Guillot, Sebastien Blaise, Manuel Dauchez, Nicolas Belloy, Jessica Prevoteau-Jonquet, and Stephanie Baud. "New visualization of dynamical flexibility of N-Glycans: Umbrella Visualization in UnityMol." In 2018 IEEE International Conference on Bioinformatics and Biomedicine (BIBM). IEEE, 2018. http://dx.doi.org/10.1109/bibm.2018.8621256.

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Cuello, H., V. Segatori, M. Alberto, C. Gulino, R. Aschero, L. Galluzzo Mutti, K. Madauss, D. Alonso, F. Lubieniecki, and M. Gabri. "PO-232 Lewis glycans and their epigenetic regulation are associated with neuroblastoma aggressiveness." In Abstracts of the 25th Biennial Congress of the European Association for Cancer Research, Amsterdam, The Netherlands, 30 June – 3 July 2018. BMJ Publishing Group Ltd, 2018. http://dx.doi.org/10.1136/esmoopen-2018-eacr25.266.

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Karbassi, Behjatolah Monzavi, Thomas Kieber-Emmons, and Steven R. Post. "Abstract 1450: Tumor-associated glycans interact with macrophages through class-A scavenger receptor." In Proceedings: AACR 107th Annual Meeting 2016; April 16-20, 2016; New Orleans, LA. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1538-7445.am2016-1450.

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Saunders, Mary R., Hyun Joo An, David J. Olivos, Yoshiko Maeda, Ryan G. Lim, Carlito B. Lebrilla, and Kit S. Lam. "Abstract 2316: Therapeutic targeting of novel human stem cell and cancer associated glycans." In Proceedings: AACR 102nd Annual Meeting 2011‐‐ Apr 2‐6, 2011; Orlando, FL. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1538-7445.am2011-2316.

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Reports on the topic "Glycans"

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Sharon, Amir, and Maor Bar-Peled. Identification of new glycan metabolic pathways in the fungal pathogen Botrytis cinerea and their role in fungus-plant interactions. United States Department of Agriculture, 2012. http://dx.doi.org/10.32747/2012.7597916.bard.

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The involvement of glycans in microbial adherence, recognition and signaling is often a critical determinant of pathogenesis. Although the major glycan components of fungal cell walls have been identified there is limited information available on its ‘minor sugar components’ and how these change during different stages of fungal development. Our aim was to define the role of Rhacontaining-glycans in the gray mold disease caused by the necrotrophic fungus B. cinerea. The research was built on the discovery of two genes, Bcdhand bcer, that are involved in formation of UDP-KDG and UDP-Rha, two UDP- sugars that may serve as donors for the synthesis of cell surface glycans. Objectives of the proposed research included: 1) To determine the function of B. cinereaBcDh and BcEr in glycan biosynthesis and in pathogenesis, 2) To determine the expression pattern of BcDH and BcERand cellular localization of their encoded proteins, 3) Characterize the structure and distribution of Rha- containing glycans, 4) Characterization of the UDP-sugar enzymes and potential of GTs involved in glycanrhamnosylation. To address these objectives we generated a series of B. cinereamutants with modifications in the bchdhand bcergenes and the phenotype and sugar metabolism in the resulting strains were characterized. Analysis of sugar metabolites showed that changes in the genes caused changes in primary and secondary sugars, including abolishment of rhamnose, however abolishment of rhamnose synthesis did not cause changes in the fungal phenotype. In contrast, we found that deletion of the second gene, bcer, leads to accumulation of the intermediate sugar – UDP- KDG, and that such mutants suffer from a range of defects including reduced virulence. Further analyses confirmed that UDP-KDG is toxic to the fungus. Studies on mode of action suggested that UDP-KDG might affect integrity of the fungal cell wall, possibly by inhibiting UDP-sugars metabolic enzymes. Our results confirm that bcdhand bcerrepresent a single pathway of rhamnose synthesis in B. cinerea, that rhamnose does not affect in vitro development or virulence of the fungus. We also concluded that UDP-KDG is toxic to B. cinereaand hence UDP-KDG or compounds that inhibit Er enzymes and lead to accumulation of UDP-KDG might have antifungal activity. This toxicity is likely the case with other fungi, this became apparent in a collaborative work with Prof. Bart Thomma of Wageningen University, NETHERLANDS . We have shown the deletion of ER mutant in Verticillium dahlia gave plants resistance to the fungal infection.
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Lowenthal, Mark. Certification of Standard Reference Material® 3655 Glycans in Solution (Frozen). Gaithersburg, MD: National Institute of Standards and Technology, 2022. http://dx.doi.org/10.6028/nist.sp.260-224.

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Fluhr, Robert, and Maor Bar-Peled. Novel Lectin Controls Wound-responses in Arabidopsis. United States Department of Agriculture, January 2012. http://dx.doi.org/10.32747/2012.7697123.bard.

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Innate immune responses in animals and plants involve receptors that recognize microbe-associated molecules. In plants, one set of this defense system is characterized by large families of TIR–nucleotide binding site–leucine-rich repeat (TIR-NBS-LRR) resistance genes. The direct interaction between plant proteins harboring the TIR domain with proteins that transmit and facilitate a signaling pathway has yet to be shown. The Arabidopsis genome encodes TIR-domain containing genes that lack NBS and LRR whose functions are unknown. Here we investigated the functional role of such protein, TLW1 (TIR LECTIN WOUNDRESPONSIVE1). The TLW1 gene encodes a protein with two domains: a TIR domain linked to a lectin-containing domain. Our specific aim in this proposal was to examine the ramifications of the TL1-glycan interaction by; A) The functional characterization of TL1 activity in the context of plant wound response and B) Examine the hypothesis that wounding induced specific polysaccharides and examine them as candidates for TL-1 interactive glycan compounds. The Weizmann group showed TLW1 transcripts are rapidly induced by wounding in a JA-independent pathway and T-DNA-tagged tlw1 mutants that lack TLW1 transcripts, fail to initiate the full systemic wound response. Transcriptome methodology analysis was set up and transcriptome analyses indicates a two-fold reduced level of JA-responsive but not JA-independent transcripts. The TIR domain of TLW1 was found to interact directly with the KAT2/PED1 gene product responsible for the final b-oxidation steps in peroxisomal-basedJA biosynthesis. To identify potential binding target(s) of TL1 in plant wound response, the CCRC group first expressed recombinant TL1 in bacterial cells and optimized conditions for the protein expression. TL1 was most highly expressed in ArcticExpress cell line. Different types of extraction buffers and extraction methods were used to prepare plant extracts for TL1 binding assay. Optimized condition for glycan labeling was determined, and 2-aminobenzamide was used to label plant extracts. Sensitivity of MALDI and LC-MS using standard glycans. THAP (2,4,6- Trihydroxyacetophenone) showed minimal background peaks at positive mode of MALDI, however, it was insensitive with a minimum detection level of 100 ng. Using LC-MS, sensitivity was highly increased enough to detect 30 pmol concentration. However, patterns of total glycans displayed no significant difference between different extraction conditions when samples were separated with Dionex ICS-2000 ion chromatography system. Transgenic plants over-expressing lectin domains were generated to obtain active lectin domain in plant cells. Insertion of the overexpression construct into the plant genome was confirmed by antibiotic selection and genomic DNA PCR. However, RT-PCR analysis was not able to detect increased level of the transcripts. Binding ability of azelaic acid to recombinant TL1. Azelaic acid was detected in GST-TL1 elution fraction, however, DHB matrix has the same mass in background signals, which needs to be further tested on other matrices. The major findings showed the importance of TLW1 in regulating wound response. The findings demonstrate completely novel and unexpected TIR domain interactions and reveal a control nexus and mechanism that contributes to the propagation of wound responses in Arabidopsis. The implications are to our understanding of the function of TIR domains and to the notion that early molecular events occur systemically within minutes of a plant sustaining a wound. A WEB site (http://genome.weizmann.ac.il/hormonometer/) was set up that enables scientists to interact with a collated plant hormone database.
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Radhakrishnan, Prakash. Mucin Glycan: Expression and Potential Role in Prostate Cancer Metastasis. Fort Belvoir, VA: Defense Technical Information Center, January 2009. http://dx.doi.org/10.21236/ada508269.

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Johnson, Kevin D. Scouting Recommendations for Soybean Aphid Aphis glycines Management. Ames: Iowa State University, Digital Repository, 2006. http://dx.doi.org/10.31274/farmprogressreports-180814-1859.

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Johnson, Kevin D., and Matthew E. O'Neal. Soybean Aphid Aphis glycines Populations in Central Iowa, 2004. Ames: Iowa State University, Digital Repository, 2005. http://dx.doi.org/10.31274/farmprogressreports-180814-1882.

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Johnson, Kevin D. Soybean Aphid Aphis glycines Populations in Northeast Iowa, 2004. Ames: Iowa State University, Digital Repository, 2005. http://dx.doi.org/10.31274/farmprogressreports-180814-2535.

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Strong-Gunderson, J. M., S. Wheelis, S. L. Carroll, M. D. Waltz, and A. V. Palumbo. Degradation of high concentrations of glycols, antifreeze, and deicing fluids. Office of Scientific and Technical Information (OSTI), December 1995. http://dx.doi.org/10.2172/146759.

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Randel, L. A., and C. J. King. Separation of glycols from dilute aqueous solutions via complexation with boronic acids. Office of Scientific and Technical Information (OSTI), July 1991. http://dx.doi.org/10.2172/5152445.

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Kavanaugh, Brian. The Potential Use of Glycine to Enhance Radiation Therapy for Prostate Cancer. Fort Belvoir, VA: Defense Technical Information Center, May 2012. http://dx.doi.org/10.21236/ada564159.

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