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Nathan J Hare, Ling Y Lee, Ian Loke, Warwick J Britton, Bernadette M Saunders, Morten Thaysen-Andersen
Tuberculosis (TB) remains a prevalent and lethal infectious disease. The glycobiology associated with Mycobacterium tuberculosis infection of front-line alveolar macrophages is still unresolved. Herein, we investigated the regulation of protein N-glycosylation in human macrophages and their secreted microparticles (MPs) used for intercellular communication upon M. tb infection. LC-MS/MS-based proteomics and glycomics were performed to monitor the regulation of glycosylation enzymes and receptors and the N-glycome in in vitro-differentiated macrophages and in isolated MPs upon M...
October 19, 2016: Journal of Proteome Research
Frederique Lisacek, Julien Mariethoz, Davide Alocci, Pauline M Rudd, Jodie L Abrahams, Matthew P Campbell, Nicolle H Packer, Jonas Ståhle, Göran Widmalm, Elaine Mullen, Barbara Adamczyk, Miguel A Rojas-Macias, Chunsheng Jin, Niclas G Karlsson
The access to biodatabases for glycomics and glycoproteomics has proven to be essential for current glycobiological research. This chapter presents available databases that are devoted to different aspects of glycobioinformatics. This includes oligosaccharide sequence databases, experimental databases, 3D structure databases (of both glycans and glycorelated proteins) and association of glycans with tissue, disease, and proteins. Specific search protocols are also provided using tools associated with experimental databases for converting primary glycoanalytical data to glycan structural information...
2017: Methods in Molecular Biology
Jorin Hoogenboom, Nathalja Berghuis, Dario Cramer, Rene Geurts, Han Zuilhof, Tom Wennekes
BACKGROUND: Carbohydrates, also called glycans, play a crucial but not fully understood role in plant health and development. The non-template driven formation of glycans makes it impossible to image them in vivo with genetically encoded fluorescent tags and related molecular biology approaches. A solution to this problem is the use of tailor-made glycan analogs that are metabolically incorporated by the plant into its glycans. These metabolically incorporated probes can be visualized, but techniques documented so far use toxic copper-catalyzed labeling...
October 10, 2016: BMC Plant Biology
Monika S Doblin, Debra Mohnen, Antony Bacic
No abstract text is available yet for this article.
September 2016: Glycobiology
Wan-Ling Ho, Wen-Ming Hsu, Min-Chuan Huang, Kenji Kadomatsu, Akira Nakagawara
Glycosylation is the most complex post-translational modification of proteins. Altered glycans on the tumor- and host-cell surface and in the tumor microenvironment have been identified to mediate critical events in cancer pathogenesis and progression. Tumor-associated glycan changes comprise increased branching of N-glycans, higher density of O-glycans, generation of truncated versions of normal counterparts, and generation of unusual forms of terminal structures arising from sialylation and fucosylation. The functional role of tumor-associated glycans (Tn, sTn, T, and sLe(a/x)) is dependent on the interaction with lectins...
September 29, 2016: Journal of Hematology & Oncology
Moacyr J B M Rêgo, Antônio F Silva Filho, Ana P V Sobral, Eduardo I C Beltrão
The formation of new and functional structural components of several organs, such as parotid glands, can be influenced by the glycocode. This study analyzed the glycobiology of parotid salivary gland tissue during fetal development using specific biochemical probes (lectins and antibodies). Eleven parotid gland samples from human fetuses were obtained from spontaneous abortions at 14-28 weeks of gestation, and tissue sections were analyzed for lectin histochemistry and immunohistochemistry. From the 18th to 26th week, Canavalia ensiformis agglutinin, wheat germ agglutinin, Ulex europaeus agglutinin-I, peanut agglutinin, Sambucus nigra agglutinin, and Vicia villosa agglutinin lectin staining were predominantly observed in the apical and/or basement membranes of the ducts and tubulo-acinar units...
2016: Journal of Oral Science
Bruce A Baggenstoss, Edward N Harris, Jennifer L Washburn, Andria P Medina, Long Nguyen, Paul H Weigel
Hyaluronan synthases (HAS) normally make large (>MDa) hyaluronan (HA) products. Smaller HA fragments (e.g. 100-400 kDa) produced in vivo are associated with inflammation and cell signaling by HA receptors that bind small, but not large, HA. Although HA fragments can arise from breakdown by hyaluronidases, HAS might also be regulated directly to synthesize small HA. Here we examined the Streptococcus equisimilis HAS (SeHAS) C-terminus, which contains a tandem B-X7-B motif (K(398)-X7-R(406)-X7-K(414)), by testing the effects of 27 site-specific scanning mutations and 7 C-terminal truncations on HA synthesis activity and weight-average mass...
August 24, 2016: Glycobiology
Pierre-André Gilormini, Cédric Lion, Maxence Noel, Marie-Ange Krzewinski-Recchi, Anne Harduin-Lepers, Yann Guérardel, Christophe Biot
Natural and synthetically modified CMP-activated sialic acids are essential research tools in the field of glycobiology: among other applications, they can be used to probe glycans, detect sialylation defects at the cell surface, or carry out detailed studies of sialyltransferase activities. However, these chemical tools are notoriously unstable because of hydrolytic decomposition, and are very time-consuming and costly to obtain. They are nigh impossible to store with satisfactory purity, and their preparation requires multiple laborious purification steps that usually lead to heavy product loss...
August 19, 2016: Glycobiology
Mohamed I Hassan, Benjamin R Lundgren, Michael Chaumun, Dennis M Whitfield, Brady Clark, Ian C Schoenhofen, Christopher N Boddy
Legionaminic acid, Leg5,7Ac2 , a nonulosonic acid like 5-acetamido neuraminic acid (Neu5Ac, sialic acid), is found in cell surface glycoconjugates of bacteria including the pathogens Campylobacter jejuni, Acinetobacter baumanii and Legionella pneumophila. The presence of Leg5,7Ac2 has been correlated with virulence in humans by mechanisms that likely involve subversion of the host's immune system or interactions with host cell surfaces due to its similarity to Neu5Ac. Investigation into its role in bacterial physiology and pathogenicity is limited as there are no effective sources of it...
September 19, 2016: Angewandte Chemie
Guangyan Qing, Xiuling Li, Peng Xiong, Cheng Chen, Mimi Zhan, Xinmiao Liang, Taolei Sun
Glycoproteomics identifies and catalogs protein glycosylation and explores its impact on protein conformations and biofunctions. However, these studies are restricted by the bottleneck to enrich low-abundance glycopeptides from complex biosamples and the difficulties in analyzing glycan structures by mass spectrometry. Here, we report dipeptide as a simple but promising carbohydrate binding platform to tackle these problems. We build a hydropathy-index-based strategy for sequence optimization and screen out three optimal dipeptide sequences from 54 types of dipeptides...
August 31, 2016: ACS Applied Materials & Interfaces
L Raich, A Nin-Hill, A Ardèvol, C Rovira
Carbohydrates play crucial roles in many biological processes, from cell-cell adhesion to chemical signaling. Their complexity and diversity, related to α/β anomeric configuration, ring substituents, and conformational variations, require a diverse set of enzymes for their processing. Among them, glycoside hydrolases (GHs) are responsible for the hydrolysis of one of the strongest bonds in nature: the glycosidic bond. These highly specialized biological catalysts select particular conformations their carbohydrate substrates to enhance catalysis...
2016: Methods in Enzymology
Geert-Jan Boons, Peng Wu
No abstract text is available yet for this article.
August 2016: Glycobiology
Ana M Dias, Catarina R Almeida, Celso A Reis, Salomé S Pinho
Imaging flow cytometry is an emerging imaging technology that combines features of both conventional flow cytometry and fluorescence microscopy allowing quantification of the imaging parameters. The analysis of protein posttranslational modifications by glycosylation using imaging flow cytometry constitutes an important bioimaging tool in the glycobiology field. This technique allows quantification of the glycan fluorescence intensity, co-localization with proteins, and evaluation of the membrane/cytoplasmic expression...
2016: Methods in Molecular Biology
Wenpin Hou, Yushan Qiu, Nobuyuki Hashimoto, Wai-Ki Ching, Kiyoko F Aoki-Kinoshita
BACKGROUND: Abnormalities in glycan biosynthesis have been conclusively related to various diseases, whereas the complexity of the glycosylation process has impeded the quantitative analysis of biochemical experimental data for the identification of glycoforms contributing to disease. To overcome this limitation, the automatic construction of glycosylation reaction networks in silico is a critical step. RESULTS: In this paper, a framework K2014 is developed to automatically construct N-glycosylation networks in MATLAB with the involvement of the 27 most-known enzyme reaction rules of 22 enzymes, as an extension of previous model KB2005...
2016: BMC Bioinformatics
Lajos Jakab
Carbohydrate molecules connected mostly with covalent junctions to protein chains are called glycoproteins. These carbohydrate molecules are attached to the protein core in different qualities and order. When the protein core is connected with acidic components such as uronic acid or SO4 radicals, they are called proteoglycans. The currently used name "glycosaminoglycan" in this case is not entirely correct. In the living world polymannane structures occur, too. Glycoproteins do not only exceptionally hold acidic groups but they have neuraminic acid derivatives...
July 2016: Orvosi Hetilap
Yasuhiko Kizuka, Sho Funayama, Hidehiko Shogomori, Miyako Nakano, Kazuki Nakajima, Ritsuko Oka, Shinobu Kitazume, Yoshiki Yamaguchi, Masahiro Sano, Hiroaki Korekane, Tsui-Ling Hsu, Hsiu-Yu Lee, Chi-Huey Wong, Naoyuki Taniguchi
Fucose, a terminal sugar in glycoconjugates, critically regulates various physiological and pathological phenomena, including cancer development and inflammation. However, there are currently no probes for efficient labeling and detection of this sugar. We chemically synthesized a novel series of alkynyl-fucose analogs as probe candidates and found that 7-alkynyl-fucose gave the highest labeling efficiency and low cytotoxicity. Among the fucose analogs, 7-alkynyl-fucose was the best substrate against all five fucosyltransferases examined...
July 21, 2016: Cell Chemical Biology
Anup Mammen Oommen, Neeti Somaiya, Jisha Vijayan, Satheesh Kumar, Suri Venkatachalam, Lokesh Joshi
The perplexing nature of dynamic glycosylation modification plays imperative role in determining the regulatory role of key glycoconjugates involved in immune system. Systematic analysis of change in expression pattern of glycogenes and lectins can bring in a comprehensive understanding of genetic basis of the glycobiological changes occurring in pathological condition. Advancement in the field of glycobiology has capacitated the process of linking gene expression changes of glycogenes with its biological function...
October 7, 2016: Journal of Theoretical Biology
Hiromi Nakao, Shogo Matsumoto, Yuko Nagai, Aya Kojima, Hidenao Toyoda, Noritaka Hashii, Daisuke Takakura, Nana Kawasaki, Tomoko Yamaguchi, Kenji Kawabata, Nobuko Kawasaki, Toshisuke Kawasaki
Recently, we established two mouse monoclonal antibodies (R-10G and R-17F). The R-17F antibody (IgG1 subtype) exhibited a strong cytotoxic effect on hiPS/ES cells. The R-17F antigen isolated from a total lipid extract of hiPS (Tic) cells was identified as LNFP I (Fucα1-2Galβ1-3GlcNAcβ1-3Galβ1-4Glc). In the present study, R-17F binding proteins were isolated from hiPS (Tic) cell lysates with an affinity column of R-17F. They gave one major R-17F positive band around 250 kDa, and several minor bands between 150 kDa and 25 kDa...
July 19, 2016: Glycoconjugate Journal
Sandra V Bennun, Deniz Baycin Hizal, Kelley Heffner, Ozge Can, Hui Zhang, Michael J Betenbaugh
The number of proteins encoded in the human genome has been estimated at between 20,000 and 25,000, despite estimates that the entire proteome contains more than a million proteins. One reason for this difference is due to many post-translational modifications of protein that contribute to proteome complexity. Among these, glycosylation is of particular relevance because it serves to modify a large number of cellular proteins. Glycogenomics, glycoproteomics, glycomics, and glycoinformatics are helping to accelerate our understanding of the cellular events involved in generating the glycoproteome, the variety of glycan structures possible, and the importance of roles that glycans play in therapeutics and disease...
August 14, 2016: Journal of Molecular Biology
Yangyang Sun, Li Cheng, Yihua Gu, Aijie Xin, Bin Wu, Shumin Zhou, Shujuan Guo, Yin Liu, Hua Diao, Huijuan Shi, Guangyu Wang, Sheng-Ce Tao
Glycosylation is one of the most abundant and functionally important protein post-translational modifications. As such, technology for efficient glycosylation analysis is in high demand. Lectin microarrays are a powerful tool for such investigations and have been successfully applied for a variety of glycobiological studies. However, most of the current lectin microarrays are primarily constructed from plant lectins, which are not well suited for studies of human glycosylation because of the extreme complexity of human glycans...
September 2016: Molecular & Cellular Proteomics: MCP
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