Study-Period-Deaths-Group-Effects-Administration-Gos-r

Therefore, it was concluded that GOS had no effects on the development of animals 4 days after birth. Since, there were no abnormalities due to administration of GOS in the macroscopic examination, organ weight or histopathology of the reproductive organs or differentiation (incisor eruption and eyelid opening) of males or females, it was concluded that repeated oral administration of GOS at mgkgday for 6 weeks from day 4 after birth had no effects on postnatal development. The no observed effect level of GOS by repeated oral administration for 6 weeks from day 4 after birth was mgkgday for both males and females The capsular dynamics of Cryptococcus neoformans.Cryptococcus neoformans is a soil-dwelling fungus that causes life-threatening illness in immunocompromised individuals and latently infects many healthy individuals. Fucosylated oligosaccharides , unlike other human pathogenic fungi, is surrounded by a polysaccharide capsule that is essential for survival and enables C.

neoformans to thwart the mammalian immune system. The capsule is a dynamic structure that undergoes changes in size and rearranges during budding. Here, the latest information and unresolved questions regarding capsule synthesis, structure, assembly, growth and rearrangements are discussed along with the concept that self-assembly is important in capsular dynamics.The domain-swapped dimer of cyanovirin-N contains two sets of oligosaccharide The binding of high-mannose oligosaccharides to the domain-swapped dimeric form of the potent HIV-inactivating protein cyanovirin-N (CV-N) was investigated in solution by NMR, complementing recent structural studies by X-ray crystallography on similar complexes [J. Biol. Chem. 277 (02) 34336].

The crystal structures of CV-N dimer complexed with Man-9 and hexamannoside revealed two carbohydrate binding sites on opposite ends of the molecule. No binding was observed at site 1, previously identified on the solution monomer of CV-N [Structure 9 (01) 931; Shenoy et al., Chem. Biol. 9 (02) 19]. Here, we report the presence of four sugar binding sites on the CV-N dimer in solution, identified by chemical shift mapping with hexamannoside and nonamannoside, synthetic substructures of Man-9. Human Milk Glycans demonstrate that in solution the domain-swapped CV-N dimer, like the CV-N monomer, contains two types of sites that are available for carbohydrate binding, suggesting that the occlusion of the primary sites in the crystal is due to specific features of the solid state.

Chemoenzymatic synthesis of heparin oligosaccharides with both anti-factor Xa Heparan sulfate (HS) and heparin are highly sulfated polysaccharides. Heparin is a commonly used anticoagulant drug that inhibits the activities of factors Xa and IIa (also known as thrombin) to prevent blood clot formation. Here, we report the synthesis of a series of size-defined oligosaccharides to probe the minimum size requirement for an oligosaccharide with anti-IIa activity. The synthesis was completed by a chemoenzymatic approach involving glycosyltransferases, HS sulfotransferases, and C(5)-epimerase. We demonstrate the ability to synthesize highly purified N-sulfo-oligosaccharides having up to 21 saccharide residues. The results from anti-Xa and anti-IIa activity measurements revealed that an oligosaccharide longer than 19 saccharide residues is necessary to display anti-IIa activity. The oligosaccharides also exhibit low binding toward platelet factor 4, raising the possibility of preparing a synthetic heparin with a reduced effect of heparin-induced thrombocytopenia.

The results from this study demonstrate the ability to synthesize large HS oligosaccharides and provide a unique tool to probe the structure and function relationships of HS that require the use of large HS fragments.Significance of the oligosaccharides of the porcine reproductive and respiratory syndrome virus glycoproteins GP2a and GP5 for infectious virus production.Wissink EHJ(1), Kroese MV(1), Maneschijn-Bonsing JG(1), Meulenberg JJM(1), van Diseases, Edelhertweg 15, PO Box 65, 80 AB Lelystad, The Netherlands.The arterivirus porcine reproductive and respiratory syndrome virus (PRRSV) contains four glycoproteins, GP(2a), GP(3), GP(4) and GP(5), the functions of which are still largely unresolved. In this study, the significance of the N-glycosylation of the GP(2a) and GP(5) proteins of PRRSV strain LV was investigated. Both glycoproteins contain two predicted N-glycosylation sites that are highly conserved between North American-type and European-type PRRSV. Using human milk oligosaccharides -directed mutagenesis, single and double mutant full-length PRRSV cDNA clones were generated.