Glycan microarrays are widely used to elucidate carbohydrate binding specificity and affinity of various analytes including proteins, microorganisms, cells, and tissues. Glycan microarrays comprise a wide variety of platforms, differing in surface chemistry, presentation of carbohydrates, carbohydrate valency, and detection strategies, all of which impact on analyte performance. This chapter describes detailed methods for printing neoglycoprotein and glycoprotein microarrays on hydrogel-coated slides and incubation of these glycan microarrays with fluorescently labeled lectins.
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Glycosylation profiling of monkeypox virus structural proteins with poly Ser-Arg materials.
Analyst
January 2025
Key Laboratory of Phytochemistry and Natural Medicines, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian 116023, P. R. China.
Although the glycosylation of viral proteins plays a critical role in the process of viral invasion into host cells, studies on the glycosylation of monkeypox virus (MPXV) structural proteins have not yet been reported. To investigate the importance of MPXV protein glycosylation, poly Ser-Arg (poly SR) materials capable of simultaneously enriching both -glycopeptides and -glycopeptides were synthesized by surface-initiated reversible addition-fragmentation chain transfer (SI-RAFT) polymerization. The poly SR materials were evaluated using the digest mixture of standard proteins containing bovine fetuin and bovine serum albumin, and the digest of complex biological samples including bovine sperm tail lysate, mouse sperm tail lysate, mouse brain lysate, and human serum.
View Article and Find Full Text PDFIdentification of a circulating carbohydrate antigen as a highly specific and sensitive target for schistosomiasis serology.
J Clin Microbiol
January 2025
Leiden University Center for Infectious Diseases, Leiden University Medical Center, Leiden, the Netherlands.
Unlabelled: The World Health Organization (WHO) 2030 roadmap for schistosomiasis calls for development of highly sensitive and specific diagnostic tools to continue and sustain progress towards elimination. Serological assays are excellent for sensitive detection of primary schistosome infections and for schistosomiasis surveillance in near- and post-elimination settings. To develop accurate assay formats, it is necessary to identify defined antibody targets with low cross-reactivity and potential for standardized production.
View Article and Find Full Text PDFLectin Microarray Analysis of Salivary Gland Glycoproteins from the Arboviral Vector Aedes aegypti and the Malaria Vector Anopheles stephensi.
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Department of Zoology, Faculty of Science, University of Jaffna, Jaffna, Sri Lanka.
Background And Objectives: Salivary glands proteins but not glycoconjugates have been previously studied in mosquito vectors of human diseases. Glycoconjugates from salivary gland-derived proteins from human-feeding tick vectors can elicit hypersensitivity reactions which may also occur with mosquito bites. Protein glycoconjugate in salivary glands of the principal arboviral vector Aedes aegypti and the rapidly spreading malaria vector Anopheles stephensi were therefore investigated.
View Article and Find Full Text PDFExpanding the recognition of monosaccharides and glycans: A comprehensive analytical approach using chemical-nose/tongue technology and a comparison to lectin microarrays.
BBA Adv
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Cellular and Molecular Biotechnology Research Institute, National Institute of Advanced Industrial Science and Technology (AIST), Tsukuba, Ibaraki 305-8565, Japan.
Chemical-nose/tongue technologies are emerging as promising analytical tools for glycan analysis. After briefly introducing the importance of glycans and their analytical methods, including the lectin microarray (LMA) as one of the gold standards, the fundamental principles underlying chemical noses/tongues are explained and various applications for monosaccharides and glycans are introduced. Then, the similarities and differences of these two approaches are discussed.
View Article and Find Full Text PDFOrthogonal-Group-Controlled Site-Selective I-Branching of Poly-N-acetyllactosamine Chains Reveals Unique Binding Specificities of Proteins towards I-Antigens.
Angew Chem Int Ed Engl
January 2025
Department of Chemistry and Center for Diagnostics & Therapeutics, Georgia State University, 50 Decatur Street SE, Atlanta, GA 30303, USA.
Poly-N-acetyllactosamine (poly-LacNAc) is ubiquitously expressed on cell surface glycoconjugates, serving as the backbone of complex glycans and an extended scaffold that presents diverse glycan epitopes. The branching of poly-LacNAc, where internal galactose (Gal) residues have β1-6 linked N-acetylglucosamine (GlcNAc) attached, forms the blood group I-antigen, which is closely associated with various physiological and pathological processes including cancer progression. However, the underlying mechanisms remain unclear as many of the I-antigen sequences are undefined and inaccessible.
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