Herein we describe an assay that was developed to quantitate the binding of normal red blood cells (RBC), labeled with carboxy fluorescein diacetate (C-FDA), to rosetting Plasmodium falciparum-infected RBC. The binding of RBC obtained from various animal species or humans to different strains or clones of rosetting P. falciparum-infected RBC was studied. A strain-specific preference of rosetting was observed for either blood group A/AB or B/AB RBC for all parasites tested. The higher affinity of rosette binding of blood group A, B, or AB vs. O RBC was reflected in larger rosettes when a given parasite was grown in RBC of the preferred blood group. The small size of the rosettes formed when P. falciparum was grown in blood group O RBC may be the in vitro correlate of the relative protection against cerebral malaria afforded by belonging to blood group O rather than to blood group A or B. Rosettes of a blood group A-preferring parasite could be completely disrupted by heparin only when grown in blood group O or B RBC, but not when grown in blood group A RBC. Similarly, the rosettes of a blood group B-preferring parasite could be more easily disrupted by heparin when grown in blood group O or A RBC than when grown in blood group B RBC. Several different saccharides inhibited rosetting of group O RBC, including two monosaccharides that are basic components of heparin. The rosetting of the same parasites grown in blood group A or B RBC was less sensitive to heparin and was specifically inhibited only by the terminal mono- and trisaccharides of the A and the B blood group antigens, the H disaccharide, and fucose. Our results suggest that rosetting is mediated by multiple lectin-like interactions, the usage of which rely on the parasite phenotype and whether the receptors are present on the host cell or not.

/pdf/plasmodium-falciparum-erythrocyte-rosetting-is-mediated-by-1udobc4h03.pdf

Plasmodium falciparum erythrocyte rosetting is mediated by promiscuous lectin-like interactions.

The important roles played by human milk oligosaccharides (HMOS), the third major component of human milk, in the health of breast-fed infants have been increasingly recognized, as the structures of more than 100 different HMOS have now been elucidated. Despite the recognition of the various functions of HMOS as prebiotics, antiadhesive antimicrobials, and immunomodulators, the roles and the applications of individual HMOS species are less clear. This is mainly due to the limited accessibility to large amounts of individual HMOS in their pure forms. Current advances in the development of enzymatic, chemoenzymatic, whole-cell, and living-cell systems allow for the production of a growing number of HMOS in increasing amounts. This effort will greatly facilitate the elucidation of the important roles of HMOS and allow exploration into the applications of HMOS both as individual compounds and as mixtures of defined structures with desired functions. The structures, functions, and enzyme-catalyzed synthesis of HMOS are briefly surveyed to provide a general picture about the current progress on these aspects. Future efforts should be devoted to elucidating the structures of more complex HMOS, synthesizing more complex HMOS including those with branched structures, and developing HMOS-based or HMOS-inspired prebiotics, additives, and therapeutics.

Human Milk Oligosaccharides (HMOS): Structure, Function, and Enzyme-Catalyzed Synthesis.

AMONG the inherited neurologic diseases, the neuroaxonal dystrophies constitute a group of neurodegenerative disorders characterized by a common axonal lesion.1 These disorders include the infantil...

Neuroaxonal dystrophy due to lysosomal alpha-N-acetylgalactosaminidase deficiency.

Glycoprotéines et glycoprotéinoses

Human milk oligosaccharides seem to play an important role in the infant's defense against bacterial and viral infections of the gastrointestinal and the urogenital tract. In this study, we investigated the influence of dietary carbohydrates on the biosynthesis of lactose and oligosaccharides in the human mammary gland and their renal excretion by the human milk-fed infant. For this purpose, a lactating woman was given 27 g galactose (Gal) containing 2 g [13C] Gal (1-13C/99%) immediately after breakfast. In the following 36 h, milk (5-10 ml) was collected before each nursing. Infant's urine was collected over a period of 24 h. 13C-enrichment was measured in total milk, milk fat and protein, in the carbohydrate fraction as well as in urine by isotope ratio mass spectrometry (IRMS). Milk carbohydrates and deproteinized urine samples were fractionated by Sephadex G25 gel filtration and further analyzed by IRMS, high performance thin layer chromatography and and high pH anion exchange chromatography with pulsed amperometric detection (HPAEC-PAD). IRMS revealed that in milk a maximal delta 13CPDB was reached within 8 h after Gal intake which then rapidly declined in the following 8 h. The cumulative 13C-elimination over this first peak was 6.9% of the oral 13C-dose. The highest 13C-enrichment was detectable in the carbohydrate fraction, mainly in lactose and neutral oligosaccharides. Compared to the enrichment of human milk, the delta 13CPDB of infant's urine was delayed. In urine, the highest amount of 13C was found in the Sephadex G25 fractions which mainly contained lactose, fucosyl-lactose, lacto-N-tetraose (LNT), fucosyl-LNT and difucosyl-LNT. For further characterization, individual components were separated by HPAEC-PAD and subsequently analyzed by fast atom bombardment mass spectrometry and IRMS. The data show, that orally applied Gal is incorporated in milk, especially in lactose and neutral oligosaccharides. Obviously, some of these components were absorbed by the infant and then excreted with urine. There, oligosaccharides may serve as analogous receptors for bacterial or viral adhesion molecules, and, hence, may prevent urogenital infections in breastfed infants.

Secretion of 13C-labelled oligosaccharides into human milk and infant's urine after an oral [13C]galactose load.

Structures and serological activities of three oligosaccharides isolated from urines of nonstarved secretors and from secretors on lactose diet.

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Structures and serological activities of three oligosaccharides isolated from urines of nonstarved secretors and from secretors on lactose diet.