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Post-translational modifications of proteins play an important role in their stability, solubility and in vivo function. Also, for several reasons, such as the Golgi fragmentation during cancerogenesis, glycosylation as the most common modification is especially promising in offering high cancer specificity which, in combination with tissue-specific biomarkers available in the case of prostate diseases (PSA, PSMA, PAP), may lead to the development of novel oncodiagnostic approaches. In this review, we present the importance of subterminal glycan structures based on the N-acetylated monosaccharides GlcNAc and GalNAc in N- and also O-glycans, structures of which they are a component (LacNAc, LacdiNAc, branched structures).

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Background: Cardiac remodelling, a crucial aspect of heart failure, is commonly investigated in preclinical models by quantifying cardiomyocyte cross-sectional area (CSA) and microvascular density (MVD) via histological methods, such as immunohistochemistry. To achieve this, optimized protocols are needed, and the species specificity is dependent on the antibody used. Lectin histochemistry offers several advantages compared to antibody-based immunohistochemistry, including as cost-effectiveness and cross-species applicability.

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Evaluation of Jacalin lectin sorbents for the extraction of the human chorionic gonadotropin glycoforms prior to analysis by nano liquid chromatography-high resolution mass spectrometry.

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Laboratory of Analytical, Bioanalytical Sciences and Miniaturization, Chemistry, Biology and Innovation (CBI) UMR 8231, ESPCI Paris PSL, CNRS, PSL Research University, Paris, France. Electronic address:

Human chorionic gonadotropin (hCG) is a dimeric, highly glycosylated hormone with a total of 4 N- and 4 O-glycosylation sites in its two subunits, hCGα and hCGβ. Recently, we developed a novel nano liquid chromatography coupled to high resolution mass spectrometry (nanoLC-HRMS) method for the analysis and thus the detection of the intact glycoforms of hCG. Here, a sorbent functionalized with the Jacalin lectin was evaluated in solid-phase extraction (SPE) for its potential to fractionate the hCG glycoforms prior to their nanoLC-HRMS analysis at the intact level, which may facilitate the detection of low-abundance glycoforms and may lead to a more detailed characterization of the hormone glycosylation.

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The crystal structure of Nictaba reveals its carbohydrate-binding properties and a new lectin dimerization mode.

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Department of Biotechnology, Faculty of Bioscience Engineering, Ghent University, Proeftuinstraat 86, 9000 Ghent, Belgium.

Nictaba is a (GlcNAc)n-binding, stress-inducible lectin from Nicotiana tabacum that serves as a representative for the Nictaba-related lectins, a group of proteins that play pivotal roles in plant defense mechanisms and stress response pathways. Despite extensive research into biological activities and physiological role(s) of the lectin, the three-dimensional structure of Nictaba remained largely unknown. Here, we report crystal structures for Nictaba in the apo form and bound to chitotriose.

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Biosensors have emerged as a pivotal technology in the biomedical field, significantly enhancing the rapidity and precision of biomolecule detection. These advancements are instrumental in refining diagnostic processes, optimizing treatments, and monitoring diseases more effectively. Central to the development of highly sensitive, selective, and stable biosensors are the bioreceptor and transducer components.

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