Tyvelose
(Synonyms: D-Tyvelose) 目录号 : GC41225A 3,6-dideoxyhexose terminal sugar and the immunodominant component of T. spiralis antigens
Cas No.:5658-12-8
Sample solution is provided at 25 µL, 10mM.
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Tyvelose is an unusual 3,6-dideoxyhexose terminal sugar and the immunodominant component of glycoprotein antigens in the parasitic helminth T. spiralis, which is responsible for trichinosis in humans. It is produced in high amounts by the infective larva and is immunodominant during the muscle stage of infection. Mice immunized with tyvelose-BSA produce IgG1 antibodies to tyvelose but are not resistant to infection by T. spiralis. Tyvelose-specific antibodies (2.5 mg/20 g) administered to rat pups leads to expulsion of first stage larvae from the intestine within one hour.
Cas No. | 5658-12-8 | SDF | |
别名 | D-Tyvelose | ||
Canonical SMILES | O=C[C@H](C[C@@H]([C@@H](C)O)O)O | ||
分子式 | C6H12O4 | 分子量 | 148.2 |
溶解度 | DMF: 20 mg/ml,DMSO: 20 mg/ml,Ethanol: 10 mg/ml,PBS (pH 7.2): 10 mg/ml | 储存条件 | Store at -20°C |
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1 mg | 5 mg | 10 mg | |
1 mM | 6.7476 mL | 33.7382 mL | 67.4764 mL |
5 mM | 1.3495 mL | 6.7476 mL | 13.4953 mL |
10 mM | 0.6748 mL | 3.3738 mL | 6.7476 mL |
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Tyvelose and protective responses to the intestinal stages of Trichinella spiralis
Parasitol Int 2002 Mar;51(1):91-8.PMID:11880231DOI:10.1016/s1383-5769(02)00002-8.
The unusual sugar Tyvelose is the immunodominant portion of the major larval glycoprotein antigens of Trichinella spiralis, which play an important role in generating immunity against the intestinal stages of infection. The possibility that the Tyvelose component itself may have a host- or parasite-protective role in the intestine was tested by following the outcome of challenge infections in mice primed and boosted with tyvelose-BSA, or in mice primed with tyvelose-BSA before boosting with larval antigen. Although antibody responses were raised against Tyvelose there was no evidence of protective immunity against the intestinal stages, as assessed by total adult worm recovery or by size and fecundity of female worms in immunized mice. Equally, priming with tyvelose-BSA before boosting with larval antigen had no effect on the expression of immunity against a challenge infection. The predominant antibody isotype recorded in all immunized mice was IgG1, suggesting the induction of type 2 T cell responses, and this was confirmed by cytokine analysis, mesenteric node lymphocytes of all mice showing production of IL-5 but not IFN-gamma. Clearly immunization with Tyvelose had no significant effect on T cell polarization. The data show that, with the experimental design employed, there was no evidence for a functional role of Tyvelose in either host- or parasite-protection during the intestinal phase of infection.
High resolution x-ray structure of Tyvelose epimerase from Salmonella typhi
J Biol Chem 2003 Jun 6;278(23):20874-81.PMID:12642575DOI:10.1074/jbc.M301948200.
Tyvelose epimerase catalyzes the last step in the biosynthesis of Tyvelose by converting CDP-d-paratose to CDP-d-tyvelose. This unusual 3,6-dideoxyhexose occurs in the O-antigens of some types of Gram-negative bacteria. Here we describe the cloning, protein purification, and high-resolution x-ray crystallographic analysis of Tyvelose epimerase from Salmonella typhi complexed with CDP. The enzyme from S. typhi is a homotetramer with each subunit containing 339 amino acid residues and a tightly bound NAD+ cofactor. The quaternary structure of the enzyme displays 222 symmetry and can be aptly described as a dimer of dimers. Each subunit folds into two distinct lobes: the N-terminal motif responsible for NAD+ binding and the C-terminal region that harbors the binding site for CDP. The analysis described here demonstrates that Tyvelose epimerase belongs to the short-chain dehydrogenase/reductase superfamily of enzymes. Indeed, its active site is reminiscent to that observed for UDP-galactose 4-epimerase, an enzyme that plays a key role in galactose metabolism. Unlike UDP-galactose 4-epimerase where the conversion of configuration occurs about C-4 of the UDP-glucose or UDP-galactose substrates, in the reaction catalyzed by Tyvelose epimerase, the inversion of stereochemistry occurs at C-2. On the basis of the observed binding mode for CDP, it is possible to predict the manner in which the substrate, CDP-paratose, and the product, CDP-tyvelose, might be accommodated within the active site of Tyvelose epimerase.
Antibodies to Tyvelose exhibit multiple modes of interference with the epithelial niche of Trichinella spiralis
Infect Immun 2000 Apr;68(4):1912-8.PMID:10722582DOI:10.1128/IAI.68.4.1912-1918.2000.
Infection with the parasitic nematode Trichinella spiralis is initiated when the L1 larva invades host intestinal epithelial cells. Monoclonal antibodies specific for glycans on the larval surface and secreted glycoproteins protect the intestine against infection. Protective antibodies recognize Tyvelose which caps the target glycan. In this study, we used an in vitro model of invasion to further examine the mechanism(s) by which tyvelose-specific antibodies protect epithelial cells against T. spiralis. Using cell lines that vary in susceptibility to invasion, we confirmed and clarified the results of our in vivo studies by documenting three modes of interference: exclusion of larvae from cells, encumbrance of larvae as they migrated within epithelial monolayers, and inhibition of parasite development. Excluded larvae bear cephalic caps (C. S. McVay et al., Infect. Immun. 66:1941-1945, 1998) of immune complexes that may physically block invasion or may interfere with sensory reception. Monovalent Fab fragments prepared from a tyvelose-specific antibody also excluded larvae from cells, demonstrating that antibody binding can inhibit the parasite in the absence of antigen aggregation and cap formation. In contrast, encumbered larvae caused extensive damage to the monolayer yet were not successful in establishing a niche, as reflected by their failure to molt. These results show that antibodies to Tyvelose exhibit multiple modes of inhibitory activity, further implicating tyvelose-bearing glycoproteins as mediators of invasion and niche establishment by T. spiralis.
Novel tyvelose-containing tri- and tetra-antennary N-glycans in the immunodominant antigens of the intracellular parasite Trichinella spiralis
Glycobiology 1994 Oct;4(5):593-603.PMID:7881173DOI:10.1093/glycob/4.5.593.
The larval stage of the intestinal nematode, Trichinella spiralis, secretes and displays on its cuticle a number of antigenically cross-reactive glycoproteins. These so-called TSL-1 antigens induce a powerful antibody response in parasitized animals. In rats, anti-TSL-1 antibodies mediate a protective immunity that expels invading larvae from the intestine. The vast majority of anti-TSL-1 antibodies are specific for glycans. Although the biological functions of TSL-1 antigens are not known, the powerful effect of glycan-specific antibodies on the intestinal survival of T. spiralis suggests that they play an important role in parasite establishment. Little is known about the structures of the glycans present on the TSL-1 glycoproteins. Recent studies have suggested, however, that the antigens contain very unusual glycans (Wisnewski, N., McNeil, M., Grieve, R.B. and Wassom, D.L., Mol. Biochem. Parasitol., 61, 25-36, 1993). Sugar and linkage analysis of the combined secreted products unexpectedly showed that a major terminal sugar is Tyvelose (3,6-dideoxy-D-arabino-hexose; Tyv) which has previously been found only in certain gram-negative bacterial lipopolysaccharides. In this paper, we report the first rigorous structural study of oligosaccharides released from TSL-1 antigens by peptide N-glycosidase F digestion. Using strategies based on fast atom bombardment mass spectrometry (FAB-MS), we have discovered a novel family of tri- and tetra-antennary N-glycans whose antennae are comprised of the tyvelose-capped structure: Tyv1,3GalNAc beta 1,4(Fuc alpha 1,3)GlcNAc beta 1-. Thus a major population of TSL-1 glycans contains clusters of hydrophobic terminal structures which are likely to be highly immunogenic.
Structure and gene cluster of a tyvelose-containing O-polysaccharide of an entomopathogenic bacterium Yersinia entomophaga MH96T related to Yersinia pseudotuberculosis
Carbohydr Res 2017 Jun 5;445:93-97.PMID:28460348DOI:10.1016/j.carres.2017.04.013.
An O-polysaccharide was isolated from the lipopolysaccharide of an entomopathogenic bacterium Yersinia entomophaga MH96T by mild acid hydrolysis and studied by 2D NMR spectroscopy. The following structure of the branched tetrasaccharide repeating unit of the polysaccharide was established: where Tyv indicates 3,6-dideoxy-d-arabino-hexose (Tyvelose). The structure established is consistent with the gene content of the O-antigen gene cluster. The O-polysaccharide structure and gene cluster of Y. entomophaga are related to those of some Y. pseudotuberculosis serotypes.