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Journal articles on the topic 'Glycan microarray'

Author: Grafiati

Published: 9 September 2021

Last updated: 6 February 2022

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1

Smith, David F., Richard D. Cummings, and Xuezheng Song. "History and future of shotgun glycomics." Biochemical Society Transactions 47, no. 1 (2019): 1–11. http://dx.doi.org/10.1042/bst20170487.

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Abstract Glycans in polysaccharides and glycoconjugates of the hydrophilic exterior of all animal cells participate in signal transduction, cellular adhesion, intercellular signaling, and sites for binding of pathogens largely through protein–glycan interactions. Microarrays of defined glycans have been used to study the binding specificities of biologically relevant glycan-binding proteins (GBP), but such arrays are limited by their lack of diversity or relevance to the GBP being investigated. Shotgun glycan microarrays are made up of structurally undefined glycans that were released from nat

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2

Cao, Yiwei, Sang-Jun Park, Akul Y. Mehta, Richard D. Cummings, and Wonpil Im. "GlyMDB: Glycan Microarray Database and analysis toolset." Bioinformatics 36, no. 8 (2019): 2438–42. http://dx.doi.org/10.1093/bioinformatics/btz934.

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Abstract Motivation Glycan microarrays are capable of illuminating the interactions of glycan-binding proteins (GBPs) against hundreds of defined glycan structures, and have revolutionized the investigations of protein–carbohydrate interactions underlying numerous critical biological activities. However, it is difficult to interpret microarray data and identify structural determinants promoting glycan binding to glycan-binding proteins due to the ambiguity in microarray fluorescence intensity and complexity in branched glycan structures. To facilitate analysis of glycan microarray data alongsi

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Mehta, Akul Y., Jamie Heimburg-Molinaro, and Richard D. Cummings. "Tools for generating and analyzing glycan microarray data." Beilstein Journal of Organic Chemistry 16 (September 10, 2020): 2260–71. http://dx.doi.org/10.3762/bjoc.16.187.

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Glycans are one of the major biological polymers found in the mammalian body. They play a vital role in a number of physiologic and pathologic conditions. Glycan microarrays allow a plethora of information to be obtained on protein–glycan binding interactions. In this review, we describe the intricacies of the generation of glycan microarray data and the experimental methods for studying binding. We highlight the importance of this knowledge before moving on to the data analysis. We then highlight a number of tools for the analysis of glycan microarray data such as data repositories, data visu

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4

Geissner, Andreas, Anika Reinhardt, Christoph Rademacher, et al. "Microbe-focused glycan array screening platform." Proceedings of the National Academy of Sciences 116, no. 6 (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

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5

Tikhonov, Aleksei, Olga Smoldovskaya, Guzel Feyzkhanova, Nikolay Kushlinskii, and Alla Rubina. "Glycan-specific antibodies as potential cancer biomarkers: a focus on microarray applications." Clinical Chemistry and Laboratory Medicine (CCLM) 58, no. 10 (2020): 1611–22. http://dx.doi.org/10.1515/cclm-2019-1161.

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AbstractGlycosylation is one of the most common posttranslational modifications of proteins and lipids. In the case of tumors, cell transformation accompanied by aberrant glycosylation results in the expression of tumor-associated glycans that promote tumor invasion. As part of the innate immunity, anti-glycan antibodies recognize tumor-associated glycans, and these antibodies can be present in the bloodstream in the early stages of cancer. Recently, anti-glycan antibody profiles have been of interest in various cancer studies. Novel advantages in the field of analytical techniques have simpli

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6

Li, Chunxia, Angelina S. Palma, Pengtao Zhang, et al. "Noncovalent microarrays from synthetic amino-terminating glycans: Implications in expanding glycan microarray diversity and platform comparison." Glycobiology 31, no. 8 (2021): 931–46. http://dx.doi.org/10.1093/glycob/cwab037.

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Abstract Glycan microarrays have played important roles in detection and specificity assignment of glycan recognition by proteins. However, the size and diversity of glycan libraries in current microarray systems are small compared to estimated glycomes, and these may lead to missed detection or incomplete assignment. For microarray construction, covalent and noncovalent immobilization are the two types of methods used, but a direct comparison of results from the two platforms is required. Here we develop a chemical strategy to prepare lipid-linked probes from both naturally derived aldehyde-t

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7

Mende, Marco, Vittorio Bordoni, Alexandra Tsouka, Felix F. Loeffler, Martina Delbianco, and Peter H. Seeberger. "Multivalent glycan arrays." Faraday Discussions 219 (2019): 9–32. http://dx.doi.org/10.1039/c9fd00080a.

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8

Mickum, Megan L., Nina Salinger Prasanphanich, Xuezheng Song, et al. "Identification of Antigenic Glycans from Schistosoma mansoni by Using a Shotgun Egg Glycan Microarray." Infection and Immunity 84, no. 5 (2016): 1371–86. http://dx.doi.org/10.1128/iai.01349-15.

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Infection of mammals by the parasitic helminthSchistosoma mansoniinduces antibodies to glycan antigens in worms and eggs, but the differential nature of the immune response among infected mammals is poorly understood. To better define these responses, we used a shotgun glycomics approach in which N-glycans from schistosome egg glycoproteins were prepared, derivatized, separated, and used to generate an egg shotgun glycan microarray. This array was interrogated with sera from infected mice, rhesus monkeys, and humans and with glycan-binding proteins and antibodies to gather information about th

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9

Wu, Nian, Lisete M. Silva, Yan Liu, et al. "Glycan Markers of Human Stem Cells Assigned with Beam Search Arrays." Molecular & Cellular Proteomics 18, no. 10 (2019): 1981–2002. http://dx.doi.org/10.1074/mcp.ra119.001309.

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Glycan antigens recognized by monoclonal antibodies have served as stem cell markers. To understand regulation of their biosynthesis and their roles in stem cell behavior precise assignments are required. We have applied state-of-the-art glycan array technologies to compare the glycans bound by five antibodies that recognize carbohydrates on human stem cells. These are: FC10.2, TRA-1–60, TRA-1–81, anti-i and R-10G. Microarray analyses with a panel of sequence-defined glycans corroborate that FC10.2, TRA-1–60, TRA-1–81 recognize the type 1-(Galβ-3GlcNAc)-terminating backbone sequence, Galβ-3Glc

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10

Li, Lei, Wanyi Guan, Gaolan Zhang, et al. "Microarray analyses of closely related glycoforms reveal different accessibilities of glycan determinants on N-glycan branches." Glycobiology 30, no. 5 (2019): 334–45. http://dx.doi.org/10.1093/glycob/cwz100.

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Abstract Glycans mediate a wide variety of biological roles via recognition by glycan-binding proteins (GBPs). Comprehensive knowledge of such interaction is thus fundamental to glycobiology. While the primary binding feature of GBPs can be easily uncovered by using a simple glycan microarray harboring limited numbers of glycan motifs, their fine specificities are harder to interpret. In this study, we prepared 98 closely related N-glycoforms that contain 5 common glycan epitopes which allowed the determination of the fine binding specificities of several plant lectins and anti-glycan antibodi

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11

Gao, Chao, Kathrin Stavenhagen, Barbara Eckmair, et al. "Differential recognition of oligomannose isomers by glycan-binding proteins involved in innate and adaptive immunity." Science Advances 7, no. 24 (2021): eabf6834. http://dx.doi.org/10.1126/sciadv.abf6834.

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The recognition of oligomannose-type glycans in innate and adaptive immunity is elusive due to multiple closely related isomeric glycan structures. To explore the functions of oligomannoses, we developed a multifaceted approach combining mass spectrometry assignments of oligomannose substructures and the development of a comprehensive oligomannose microarray. This defined microarray encompasses both linear and branched glycans, varying in linkages, branching patterns, and phosphorylation status. With this resource, we identified unique recognition of oligomannose motifs by innate immune recept

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12

Mehta, Akul Y., and Richard D. Cummings. "GLAD: GLycan Array Dashboard, a visual analytics tool for glycan microarrays." Bioinformatics 35, no. 18 (2019): 3536–37. http://dx.doi.org/10.1093/bioinformatics/btz075.

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Abstract Motivation Traditional glycan microarray data is typically presented as excel files with limited visualization and interactivity. Thus, comparisons and analysis of glycan array data have been difficult, and there is need for a tool to facilitate data mining of glycan array data. Results GLAD (GLycan Array Dashboard) is a web-based tool to visualize, analyze, present and mine glycan microarray data. GLAD allows users to input multiple data files to create comparisons. GLAD extends the capability of the microarray data to produce more comparative visualizations in the form of grouped ba

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13

Prudden, Anthony R., Lin Liu, Chantelle J. Capicciotti, et al. "Synthesis of asymmetrical multiantennary human milk oligosaccharides." Proceedings of the National Academy of Sciences 114, no. 27 (2017): 6954–59. http://dx.doi.org/10.1073/pnas.1701785114.

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Despite mammalian glycans typically having highly complex asymmetrical multiantennary architectures, chemical and chemoenzymatic synthesis has almost exclusively focused on the preparation of simpler symmetrical structures. This deficiency hampers investigations into the biology of glycan-binding proteins, which in turn complicates the biomedical use of this class of biomolecules. Herein, we describe an enzymatic strategy, using a limited number of human glycosyltransferases, to access a collection of 60 asymmetric, multiantennary human milk oligosaccharides (HMOs), which were used to develop

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14

Temme, J. Sebastian, Christopher T. Campbell, and Jeffrey C. Gildersleeve. "Factors contributing to variability of glycan microarray binding profiles." Faraday Discussions 219 (2019): 90–111. http://dx.doi.org/10.1039/c9fd00021f.

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15

Wang, Linlin, Richard D. Cummings, David F. Smith, et al. "Cross-platform comparison of glycan microarray formats." Glycobiology 24, no. 6 (2014): 507–17. http://dx.doi.org/10.1093/glycob/cwu019.

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16

Song, Xuezheng, Yi Lasanajak, Linda J. Olson, et al. "Glycan Microarray Analysis of P-type Lectins Reveals Distinct Phosphomannose Glycan Recognition." Journal of Biological Chemistry 284, no. 50 (2009): 35201–14. http://dx.doi.org/10.1074/jbc.m109.056119.

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17

Liu, Yan. "Neoglycolipid (NGL)-based oligosaccharide microarrays and highlights of their recent applications in studies of the molecular basis of pathogen–host interactions." Biochemical Society Transactions 38, no. 5 (2010): 1361–67. http://dx.doi.org/10.1042/bst0381361.

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Carbohydrate microarray technologies are new developments at the frontier of glycomics that are showing great promise as tools for high-throughput analysis of carbohydrate-mediated interactions and the elucidation of carbohydrate ligands involved not only in endogenous receptor systems, but also pathogen–host interactions. The main advantage of microarray analysis is that a broad range of glycan sequences can be immobilized on solid matrices as minute spots and simultaneously interrogated. Different methodologies have emerged for constructing carbohydrate microarrays. The NGL (neoglycolipid)-b

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18

Srinivasan, Karunya, Sucharita Roy, Nathaniel Washburn, et al. "A Quantitative Microtiter Assay for Sialylated Glycoform Analyses Using Lectin Complexes." Journal of Biomolecular Screening 20, no. 6 (2015): 768–78. http://dx.doi.org/10.1177/1087057115577597.

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Fidelity of glycan structures is a key requirement for biotherapeutics, with carbohydrates playing an important role for therapeutic efficacy. Comprehensive glycan profiling techniques such as liquid chromatography (LC) and mass spectrometry (MS), while providing detailed description of glycan structures, require glycan cleavage, labeling, and paradigms to deconvolute the considerable data sets they generate. On the other hand, lectins as probes on microarrays have recently been used in orthogonal approaches for in situ glycoprofiling but require analyte labeling to take advantage of the capab

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19

Amoah, Abena S., Elias K. Asuming-Brempong, Benedicta B. Obeng, et al. "Identification of dominant anti-glycan IgE responses in school children by glycan microarray." Journal of Allergy and Clinical Immunology 141, no. 3 (2018): 1130–33. http://dx.doi.org/10.1016/j.jaci.2017.09.040.

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20

Hyun, Ji Young, Jaeyoung Pai, and Injae Shin. "The Glycan Microarray Story from Construction to Applications." Accounts of Chemical Research 50, no. 4 (2017): 1069–78. http://dx.doi.org/10.1021/acs.accounts.7b00043.

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21

Nishijima, Yoshihiro, Masashi Toyoda, Mayu Yamazaki-Inoue, et al. "Glycan profiling of endometrial cancers using lectin microarray." Genes to Cells 17, no. 10 (2012): 826–36. http://dx.doi.org/10.1111/gtc.12003.

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22

McCombs, Janet E., Jason P. Diaz, Kevin J. Luebke, and Jennifer J. Kohler. "Glycan specificity of neuraminidases determined in microarray format." Carbohydrate Research 428 (June 2016): 31–40. http://dx.doi.org/10.1016/j.carres.2016.04.003.

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23

Ruprecht, Colin, Max P. Bartetzko, Deborah Senf, et al. "A Synthetic Glycan Microarray Enables Epitope Mapping of Plant Cell Wall Glycan-Directed Antibodies." Plant Physiology 175, no. 3 (2017): 1094–104. http://dx.doi.org/10.1104/pp.17.00737.

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24

KOBAYASHI, YUSUKE, KENTA MASUDA, KOUJI BANNO, et al. "Glycan profiling of gestational choriocarcinoma using a lectin microarray." Oncology Reports 31, no. 3 (2014): 1121–26. http://dx.doi.org/10.3892/or.2014.2979.

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25

Narla, Satya Nandana, and Xue-Long Sun. "Glyco-macroligand microarray with controlled orientation and glycan density." Lab on a Chip 12, no. 9 (2012): 1656. http://dx.doi.org/10.1039/c2lc21224b.

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26

Zupancic, Margaret L., Matthew Frieman, David Smith, Richard A. Alvarez, Richard D. Cummings, and Brendan P. Cormack. "Glycan microarray analysis of Candida glabrata adhesin ligand specificity." Molecular Microbiology 68, no. 3 (2008): 547–59. http://dx.doi.org/10.1111/j.1365-2958.2008.06184.x.

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27

Song, Xuezheng, Baoyun Xia, Sean R. Stowell, Yi Lasanajak, David F. Smith, and Richard D. Cummings. "Novel Fluorescent Glycan Microarray Strategy Reveals Ligands for Galectins." Chemistry & Biology 16, no. 1 (2009): 36–47. http://dx.doi.org/10.1016/j.chembiol.2008.11.004.

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28

Padler-Karavani, Vered. "Glycan Microarray Reveal the Sweet Side of Cancer Vaccines." Cell Chemical Biology 23, no. 12 (2016): 1446–47. http://dx.doi.org/10.1016/j.chembiol.2016.12.002.

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29

Park, Tae-Joon, Moo-Yeal Lee, Jonathan S. Dordick, and Robert J. Linhardt. "Signal amplification of target protein on heparin glycan microarray." Analytical Biochemistry 383, no. 1 (2008): 116–21. http://dx.doi.org/10.1016/j.ab.2008.07.037.

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30

Yan, Maomao, Yuyang Zhu, Xueyun Liu, et al. "Next-Generation Glycan Microarray Enabled by DNA-Coded Glycan Library and Next-Generation Sequencing Technology." Analytical Chemistry 91, no. 14 (2019): 9221–28. http://dx.doi.org/10.1021/acs.analchem.9b01988.

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31

Yokose, Takahiro, Yasuaki Kabe, Atsushi Matsuda, et al. "O-Glycan-Altered Extracellular Vesicles: A Specific Serum Marker Elevated in Pancreatic Cancer." Cancers 12, no. 9 (2020): 2469. http://dx.doi.org/10.3390/cancers12092469.

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Pancreatic cancer (PC) is among the most lethal malignancies due to an often delayed and difficult initial diagnosis. Therefore, the development of a novel, early stage, diagnostic PC marker in liquid biopsies is of great significance. In this study, we analyzed the differential glycomic profiling of extracellular vesicles (EVs) derived from serum (two cohorts including 117 PC patients and 98 normal controls) using lectin microarray. The glyco-candidates of PC-specific EVs were quantified using a high-sensitive exosome-counting system, ExoCounter. An absolute quantification system for altered

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32

Li, Hong, Liming Wei, Pan Fang, and Pengyuan Yang. "Recent advances in the fabrication and detection of lectin microarrays and their application in glycobiology analysis." Anal. Methods 6, no. 7 (2014): 2003–14. http://dx.doi.org/10.1039/c3ay41974f.

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33

Anani, Waseem Q., Heather E. Ashwood, Anna Schmidt, Robert T. Burns, Gregory A. Denomme, and Karin M. Hoffmeister. "Predictive modeling of complex ABO glycan phenotypes by lectin microarrays." Blood Advances 4, no. 16 (2020): 3960–70. http://dx.doi.org/10.1182/bloodadvances.2020002051.

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Abstract Serological classification of individuals as A, B, O, or AB is a mainstay of blood banking. ABO blood groups or ABH antigens, in addition to other surface glycans, act as unique red blood cell (RBC) signatures and direct immune responses. ABO subgroups present as weakened, mixed field, or unexpected reactivity with serological reagents, but specific designations remain complex. Lectins detect glycan motifs with some recognizing ABH antigens. We evaluated a 45-probe lectin microarray to rapidly analyze ABO blood groups and associated unique glycan signatures within complex biological s

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34

Jain, Prashant, Chethan D. Shanthamurthy, Shani Leviatan Ben-Arye, Robert J. Woods, Raghavendra Kikkeri, and Vered Padler-Karavani. "Discovery of rare sulfated N-unsubstituted glucosamine based heparan sulfate analogs selectively activating chemokines." Chemical Science 12, no. 10 (2021): 3674–81. http://dx.doi.org/10.1039/d0sc05862a.

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We report the synthesis of novel HS tetrasaccharides. High throughput screening using glycan microarray and SPR identified the rare HS analog for selectively inhibiting CCL2 mediated cell migration and invasion.

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35

HIRABAYASHI, Jun. "Development of lectin microarray, an advanced system for glycan profiling." Synthesiology 7, no. 2 (2014): 105–17. http://dx.doi.org/10.5571/synth.7.105.

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36

HIRABAYASHI, Jun. "Development of lectin microarray, an advanced system for glycan profiling." Synthesiology English edition 7, no. 2 (2014): 105–17. http://dx.doi.org/10.5571/syntheng.7.105.

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37

Zhang, Hanyuan, Alanna M. Klose, and Benjamin L. Miller. "Label-Free, Multiplex Glycan Microarray Biosensor for Influenza Virus Detection." Bioconjugate Chemistry 32, no. 3 (2021): 533–40. http://dx.doi.org/10.1021/acs.bioconjchem.0c00718.

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38

Crawford, Conor J., Maggie P. Wear, Daniel F. Q. Smith, et al. "A glycan FRET assay for detection and characterization of catalytic antibodies to the Cryptococcus neoformans capsule." Proceedings of the National Academy of Sciences 118, no. 5 (2021): e2016198118. http://dx.doi.org/10.1073/pnas.2016198118.

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Classic antibody functions include opsonization, complement activation, and enhancement of cellular antimicrobial function. Antibodies can also have catalytic activity, although the contribution of catalysis to their biological functions has been more difficult to establish. With the ubiquity of catalytic antibodies against glycans virtually unknown, we sought to advance this knowledge. The use of a glycan microarray allowed epitope mapping of several monoclonal antibodies (mAbs) against the capsule of Cryptococcus neoformans. From this, we designed and synthesized two glycan-based FRET probes

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39

Wang, Denong, Jin Tang, Shaoyi Liu, and Jiaoti Huang. "Carbohydrate Microarrays Identify Blood Group Precursor Cryptic Epitopes as Potential Immunological Targets of Breast Cancer." Journal of Immunology Research 2015 (2015): 1–9. http://dx.doi.org/10.1155/2015/510810.

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Using carbohydrate microarrays, we explored potential natural ligands of antitumor monoclonal antibody HAE3. This antibody was raised against a murine mammary tumor antigen but was found to cross-react with a number of human epithelial tumors in tissues. Our carbohydrate microarray analysis reveals that HAE3 is specific for anO-glycan cryptic epitope that is normally hidden in the cores of blood group substances. Using HAE3 to screen tumor cell surface markers by flow cytometry, we found that the HAE3 glycoepitope,gpHAE3, was highly expressed by a number of human breast cancer cell lines, incl

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40

't Hart, Ingrid M. E., Tiehai Li, Margreet A. Wolfert, Shuo Wang, Kelley W. Moremen, and Geert-Jan Boons. "Chemoenzymatic synthesis of the oligosaccharide moiety of the tumor-associated antigen disialosyl globopentaosylceramide." Organic & Biomolecular Chemistry 17, no. 31 (2019): 7304–8. http://dx.doi.org/10.1039/c9ob01368g.

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The oligosaccharide of the tumor-associated antigen DSGb5 was synthesized in a chemoenzymatic manner by exploiting the mammalian glycosyl transferases ST3Gal1 and ST6GalNAc5, and its binding with Siglec-7 was investigated by glycan microarray technology.

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41

van Diepen, Angela, Cornelis H. Smit, Loes van Egmond, et al. "Differential Anti-Glycan Antibody Responses in Schistosoma mansoni-Infected Children and Adults Studied by Shotgun Glycan Microarray." PLoS Neglected Tropical Diseases 6, no. 11 (2012): e1922. http://dx.doi.org/10.1371/journal.pntd.0001922.

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Chen, Pei, YinKun Liu, XiaoNan Kang, Lu Sun, PengYuan Yang, and ZhaoYou Tang. "Identification of N-glycan of alpha-fetoprotein by lectin affinity microarray." Journal of Cancer Research and Clinical Oncology 134, no. 8 (2008): 851–60. http://dx.doi.org/10.1007/s00432-008-0357-7.

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43

Stevens, James, Ola Blixt, James C. Paulson, and Ian A. Wilson. "Glycan microarray technologies: tools to survey host specificity of influenza viruses." Nature Reviews Microbiology 4, no. 11 (2006): 857–64. http://dx.doi.org/10.1038/nrmicro1530.

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44

Gross, Stephanie, and Jörg Andrä. "Anticancer peptide NK-2 targets cell surface sulphated glycans rather than sialic acids." Biological Chemistry 393, no. 8 (2012): 817–27. http://dx.doi.org/10.1515/hsz-2012-0136.

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Abstract Some antimicrobial peptides have emerged as potential anticancer agents. In contrast to chemotherapeutics, they act primarily by physical disruption of the cancer cell membrane. Selective targeting of these cationic peptides still remains elusive. We focus on the interaction of α-helical peptides NK-2, cathelicidin LL32, and melittin with PC-3 prostate cancer cells, and we provide strong evidence that, amongst the anionic glycans covering the cell surface, sulphated carbohydrates rather than sialic acids are the preferred interaction sites of the peptides. To test the significance of

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45

Song, Xuezheng, Jamie Heimburg‐Molinaro, David F. Smith, and Richard D. Cummings. "Derivatization of Free Natural Glycans for Incorporation onto Glycan Arrays: Derivatizing Glycans on the Microscale for Microarray and Other Applications." Current Protocols in Chemical Biology 3, no. 2 (2011): 53–63. http://dx.doi.org/10.1002/9780470559277.ch100194.

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46

Kuno, Atsushi, Noboru Uchiyama, Shiori Koseki-Kuno, et al. "Evanescent-field fluorescence-assisted lectin microarray: a new strategy for glycan profiling." Nature Methods 2, no. 11 (2005): 851–56. http://dx.doi.org/10.1038/nmeth803.

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47

de Boer, Arjen R., Cornelis H. Hokke, André M. Deelder, and M. Wuhrer. "Serum antibody screening by surface plasmon resonance using a natural glycan microarray." Glycoconjugate Journal 25, no. 1 (2008): 75–84. http://dx.doi.org/10.1007/s10719-007-9100-x.

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48

Aranzamendi, Carmen, Boris Tefsen, Montse Jansen, et al. "Glycan microarray profiling of parasite infection sera identifies the LDNF glycan as a potential antigen for serodiagnosis of trichinellosis." Experimental Parasitology 129, no. 3 (2011): 221–26. http://dx.doi.org/10.1016/j.exppara.2011.08.015.

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49

Smit, Cornelis H., Christiaan L. Kies, Hamish E. G. McWilliam, Els N. T. Meeusen, Cornelis H. Hokke, and Angela van Diepen. "Local Antiglycan Antibody Responses to Skin Stage and Migratory Schistosomula of Schistosoma japonicum." Infection and Immunity 84, no. 1 (2015): 21–33. http://dx.doi.org/10.1128/iai.00954-15.

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Schistosomiasis is a tropical disease affecting over 230 million people worldwide. Although effective drug treatment is available, reinfections are common, and development of immunity is slow. Most antibodies raised during schistosome infection are directed against glycans, some of which are thought to be protective. Developing schistosomula are considered most vulnerable to immune attack, and better understanding of local antibody responses raised against glycans expressed by this life stage might reveal possible glycan vaccine candidates for future vaccine research. We used antibody-secretin

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50

Khasbiullina, Nailia R., Nadezhda V. Shilova, Maxim E. Navakouski, et al. "Repertoire of Abs primed by bacteria in gnotobiotic mice." Innate Immunity 24, no. 3 (2018): 180–87. http://dx.doi.org/10.1177/1753425918763524.

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Innate immunity natural Abs (NAbs) execute a number of functions, including protection and surveillance. Despite active research, the stimuli that induce the formation of NAbs are still described only hypothetically. Here, we compared repertoires of anti-glycan Abs in the peripheral blood of mice that received per os various bacteria. The repertoires of Abs of mice primed in this way were compared using a microarray that included about 350 glycans, as well as 150 bacterial polysaccharides. Sterile mice did not possess anti-glycan Abs. Oral inoculation of a single strain or combination of two t

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