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Nocardia Corynebacteroides
General and special structures, microbial producers, production conditions and chemo-enzymatic modifications as The conformational epitope of type III group B Streptococcus capsular In order to further characterize the conformational epitope of GBSPIII, we synthesized various oligosaccharides with the GBSPIII-related structures by a tailor-assembly synthetic scheme and a more traditional block-wise chemo-enzymatic approach. The oligosaccharides were used to probe the conformational epitope of GBSPIII using number of complementary techniques. The protective epitope of GPSPIII was further defined as length-dependent and conformational. The results of the studies confirmed that two repeating units place between chain length 2RU to 7RU. Epitope optimization and multivalency were observed between 7RU and RU. The data support our hypothesis that the conformational epitope is an extended helical segment of the GBSPIII.

2'-fucosyllactose exists mainly in the random coil form, which structurally mimics short oligosaccharide self-antigens, but it can infrequently and spontaneously form extended helices. Although not prevalent in GBSPIII the immune system preferentially selects these helical epitopes because they are unique to the Structural determination of the N-glycans of a lepidopteran arylphorin reveals the presence of a monoglucosylated oligosaccharide in the storage protein.Kim S(1), Hwang SK, Dwek RA, Rudd PM, Ahn YH, Kim EH, Cheong C, Kim SI, Park NS, The structures of the oligosaccharides attached to arylphorin from Chinese oak silkworm, Antheraea pernyi, have been determined. Arylphorin, a storage protein present in fifth larval hemolymph, contained 4% (ww) of carbohydrate that was composed of FucGlcNAcGlcMan4113 moles per mole protein. Four moles of GlcNAc in oligomannose-type oligosaccharides strongly suggest that the protein contains two N-glycosylation sites. Normal-phase HPLC and mass spectrometry oligosaccharide profiles confirmed that arylphorin contained mainly oligomannose-type glycans as well as truncated mannose-type structures with or without fucosylation. Interestingly, the most abundant oligosaccharide was monoglucosylated Man9-GlcNAc2, which was characterized by normal-phase HPLC, mass spectrometry, Aspergillus saitoi alpha-mannosidase digestion, and 1H 0 MHz NMR spectrometry.

This glycan structure is not normally present in secreted mammalian glycoproteins; however, it has been identified in avian species. The Glc1Man9GlcNAc2 structure was present only in arylphorin, whereas other hemolymph proteins contained only oligomannose and truncated oligosaccharides. The oligosaccharide was also detected in the arylphorin of another silkworm, Bombyx mori, suggesting a specific function for the Glc1Man9GlcNAc2 glycan. There were no processed glucosylated oligosaccharides such as Glc1Man5-8GlcNAc2. Furthermore, Glc1Man9GlcNAc2 was not released from arylophorin by PNGase F under nondenaturing conditions, suggesting that the N-glycosidic linkage to Asn is protected by the protein. Glc1Man9GlcNAc2 may play a role in the folding of arylphorin or in the assembly of hexamers.Use of diethyl squarate for the coupling of oligosaccharide amines to carrier proteins and characterization of the resulting neoglycoproteins by MALDI-TOF The 8-methoxycarbonyloctyl glycosides of GlcNAc beta, Gal beta 1-4Glc beta, Fuc alpha 1-2Fuc alpha 1-3GalNAc beta and Fuc alpha 1-2Gal beta 1-3[Fuc alpha 1-4]GlcNac beta were converted to primary amines by reaction with neat ethylenediamine and then coupled to bovine serum albumin (BSA) using diethyl squarate as the connector.

The average degree of incorporation of the sugar onto the protein, as well as the molecular weight distribution, could be conveniently determined using matrix assisted laser desorption ionizationtime of flight colour-tests or analysis of cleaved ligand. The present coupling method has the advantages of proceeding under very mild conditions, yielding controlled incorporation values and can reliably be used for the coupling of very small Automated carbohydrate synthesis to drive chemical glycomics.This feature article describes the development of the first automated solid-phase oligosaccharide synthesizer. A series of chemical challenges had to be addressed to accomplish this breakthrough and provide rapid access to oligosaccharides of biological significance. Accelerated synthesis of glycoconjugates promises to greatly impact the emerging field of glycobiology. Chemical glycomics uses synthetic carbohydrates and analogs to study their role in recognition, signal transduction pathways and other events of fundamental biomedical significance and shapes up to become the next major wave in biomedical research.
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