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Query: UNIPROT:P17931 (galectin-3)
 2,860 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The arrangement of carbohydrate molecules on surfaces of fungal cells may play an important role in nonself recognition of these microorganisms by potential invertebrate hosts. Changes in the ability of various galactose and mannose-specific lectins to bind to surface components on cell walls of the insect pathogen Paecilomyces farinosus were therefore examined during growth and differentiation of the fungus. Fluorescein isothiocyanate conjugates of concanavalin A (Con A, specific for alpha-D-mannose) and peanut agglutinin (PNA, beta-D-galactose) bound inconsistently to blastospores and weakly to mycelia except at apical regions where strong fluorescence was observed. Labeling patterns were similar on cells tested with a galactose-specific lectin purified from Spodoptera exigua (beet armyworm) hemolymph, but Bandeiraea simplicifolia lectin (BS-I alpha-D-galactose) bound only to mycelia. Electron microscopy using ferritin and gold probes showed that the galactomannans are located in a loosely bound coating on the cell wall surface. Variations in lectin binding patterns are apparently due to absence (e.g., by shedding) of the coat or to rearrangement of carbohydrate components in the coat. Staining of Western blots of dithiothreitol (DTT) cell wall extracts further indicated that the BS-I-binding entity is a unique component of the mycelial surface since, as in the fluorescence studies, blastospore preparations were not labeled. Staining of blastospore blots with other galactose-specific probes (e.g., PNA) was comparable to staining of mycelial blots.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Variations in the ability of galactose and mannose-specific lectins to bind to cell wall surfaces during growth of the insect pathogenic fungus Paecilomyces farinosus. 833 Jun 30

The modular synthesis of 7 libraries containing 51 self-assembling amphiphilic Janus dendrimers with the monosaccharides D-mannose and D-galactose and the disaccharide D-lactose in their hydrophilic part is reported. These unprecedented sugar-containing dendrimers are named amphiphilic Janus glycodendrimers. Their self-assembly by simple injection of THF or ethanol solution into water or buffer and by hydration was analyzed by a combination of methods including dynamic light scattering, confocal microscopy, cryogenic transmission electron microscopy, Fourier transform analysis, and micropipet-aspiration experiments to assess mechanical properties. These libraries revealed a diversity of hard and soft assemblies, including unilamellar spherical, polygonal, and tubular vesicles denoted glycodendrimersomes, aggregates of Janus glycodendrimers and rodlike micelles named glycodendrimer aggregates and glycodendrimermicelles, cubosomes denoted glycodendrimercubosomes, and solid lamellae. These assemblies are stable over time in water and in buffer, exhibit narrow molecular-weight distribution, and display dimensions that are programmable by the concentration of the solution from which they are injected. This study elaborated the molecular principles leading to single-type soft glycodendrimersomes assembled from amphiphilic Janus glycodendrimers. The multivalency of glycodendrimersomes with different sizes and their ligand bioactivity were demonstrated by selective agglutination with a diversity of sugar-binding protein receptors such as the plant lectins concanavalin A and the highly toxic mistletoe Viscum album L. agglutinin, the bacterial lectin PA-IL from Pseudomonas aeruginosa, and, of special biomedical relevance, human adhesion/growth-regulatory galectin-3 and galectin-4. These results demonstrated the candidacy of glycodendrimersomes as new mimics of biological membranes with programmable glycan ligand presentations, as supramolecular lectin blockers, vaccines, and targeted delivery devices.
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PMID:Modular synthesis of amphiphilic Janus glycodendrimers and their self-assembly into glycodendrimersomes and other complex architectures with bioactivity to biomedically relevant lectins. 2369 29