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  • 1
    Electronic Resource
    Electronic Resource
    The α-d-mannan core of a complex cell-wall heteroglycan of Trichoderma reesei is responsible for β-glucosidase activation (1995)
    Springer
    Archives of microbiology 164 (1995), S. 414-419 
    Details
    ISSN: 1432-072X
    Keywords: Key words Heteroglycan ; Cell walls ; 1 ; 6-α-d-Mannan ; Trichoderma ; Aspergillus ; β-Glucosidase ; Glycosidases
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A heteroglycan responsible for the binding of the enzyme β-1,4-d-glucosidase (EC 3.2.1.21) to fungal cell walls was isolated from cell walls of the filamentous fungus Trichoderma reesei. The heteroglycan, composed of mannose, galactose, glucose, and glucuronic acid, also activated β-1,4-d-glucosidase, β-1,4-d-xylosidase and N-acetyl-β-1,4-d-glucosaminidase activity in vitro. The structural backbone of this heteroglycan was prepared by acid hydrolysis and gel filtration. The molecular structure of the core of the heteroglycan was determined by NMR studies as a linear α-1,6-d-mannan. The mannan core obtained by acid degradation stimulated the β-glucosidase activity by 90%. Several glycosidases from Aspergillus niger were also activated by the T. reesei heteroglycan. The β-glucosidase of Trichoderma was activated by mannan from Saccharomyces cerevisiae to a comparable extent.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002030050283
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  • 2
    Electronic Resource
    Electronic Resource
    Crystallization and preliminary X-ray diffraction analysis of two homologous antigen-binding fragments in complex with different carbohydrate antigens (2001)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 57 (2001), S. 1872-1876 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: The antigen-binding fragments (Fab) of two murine monoclonal antibodies (mAb) S25-2 and S45-18, specific for carbohydrate epitopes in the lipopolysacchaide of the bacterial family Chlamydiaceae, have been crystallized in the presence and absence of synthetic oligosaccharides corresponding to their respective haptens. Crystals of both Fabs show different morphology depending on the presence of antigens. The sequence of mAb S45-18 was determined and shows a remarkable homology to that reported for mAb S25-2. These crystals offer an unparalleled opportunity to compare the structure and modes of binding of two homologous antibodies to similar but distinct carbohydrate epitopes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444901014536
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  • 3
    Electronic Resource
    Electronic Resource
    Occurence of antibodies against chlamydial lipopolysaccharide in human sera as measured by ELISA using an artificial glycoconjugate antigen (1994)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS immunology and medical microbiology 8 (1994), S. 0 
    Details
    ISSN: 1574-695X
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Abstract An artificial glycoconjugate containing, as a ligand, the deacylated carbohydrate backbone of a recombinant Chlamydia-specific lipopolysaccharide was used as a solid-phase antigen in ELISA to measure antibodies against chlamydial LPS. The specificity and reproducibility of the assay was shown by using a panel of prototype monoclonal antibodies representing the spectrum of antibodies also occuring in patient sera. These mAbs recognized Chlamydia-specific epitopes [α2→8-linked disaccharide of 3-deoxy-d-manno-octulosonic acid (Kdo) or the trisaccharide αKdo-(2→8)-→Kdo] or those shared between chlamydial and Re-type LPS (αKdo, α→4-linked Kdo disacccharide). The assay was used to measure IgG, IgA and IgM antibodies against chlamydial LPS in patients with genital or respiratory tract infections. In comparison to the results obtained with sera from blood donors, it became evident that both types of infection result in significant changes in the profile of LPS antibodies.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-695X.1994.tb00422.x
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  • 4
    Electronic Resource
    Electronic Resource
    Characterization of monoclonal antibodies recognizing three distinct, phosphorylated carbohydrate epitopes in the lipopolysaccharide of the deep rough mutant I-69 Rd−/b+ of Haemophilus influenzae (1997)
    Oxford BSL : Blackwell Science Ltd
    Molecular microbiology 23 (1997), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Monoclonal antibodies against the lipopolysaccharide (LPS) of the deep rough mutant I-69 Rd−/b+ of Haemophilus influenzae were obtained after immunization of mice with sheep erythrocytes which had been coated with de-O-acylated LPS. Characterization of antibodies was performed by enzyme immuno assay (EIA) using LPS or neoglycoconjugates containing partial structures of LPS as solid-phase antigens and by haemagglutination with sheep erythrocytes coated with de-O-acylated LPS. Binding data were confirmed by EIA inhibition experiments using deacylated LPS or synthetic partial structures thereof. Three antibodies were specific for 3-deoxy-d-manno-octulopyranosonic acid- (Kdo) 5-phosphate, one for Kdo-4-phosphate, and one required, in addition to a Kdo-phosphate, parts of the phosphorylated glucosamine backbone of lipid A. All antibodies also bound in (i) Western blots to bacterial whole-cell lysates or isolated LPS separated by SDS–PAGE, (ii) bacterial colony blots, and (iii) immunofluorescence with live bacteria. The latter result indicated that Kdo-4- and Kdo-5-phosphate are synthesized by the bacteria and are not the result of phosphate migration.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-2958.1997.d01-1877.x
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  • 5
    Electronic Resource
    Electronic Resource
    Germline antibody recognition of distinct carbohydrate epitopes (2003)
    [s.l.] : Nature Publishing Group
    Nature structural biology 10 (2003), S. 1019-1025 
    Details
    ISSN: 1072-8368
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Medicine
    Notes: [Auszug] High-resolution structures reveal how a germline antibody can recognize a range of clinically relevant carbohydrate epitopes. The germline response to a carbohydrate immunogen can be critical to survivability, with selection for antibody gene segments that both confer protection against common ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/nsb1014
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  • 6
    Electronic Resource
    Electronic Resource
    Über die Umsetzung von Dibenzylidensulfamiden mit Aminen (1981)
    Springer
    Monatshefte für Chemie 112 (1981), S. 489-500 
    Details
    ISSN: 1434-4475
    Keywords: Addition of amines to dibenzylidene sulfamide ; Intramolecular hydride transfer ; Sulfamoyl-benzamidines
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Addition of amines to dibenzylidene sulfamide1 a yields the correspondingSchiff bases3 a, b and monobenzylidene sulfamide2. Reaction of several dibenzylidene sulfamides1 with various lithium-amides gives N1-substituted N2-benzylsulfamoyl-benzamidines7 a-k via an intramolecular hydride transfer reaction, whereas by treatment of1 a with sodium amide 2-benzyl-3,5-diphenyl-3,4-dihydro-2H-1,2,4,6-thiatriazine-1,1-dioxide8 is obtained, which on hydrolysis yields9 and11. Alkylation products are described, the isomeric products12a/13a and12b/13b are isolated, their structures are confirmed by synthesis, IR and NMR-spectra.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00901828
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  • 7
    Electronic Resource
    Electronic Resource
    Über die Synthese von Dihydro-1,2,3,5-thiatriazol-1,1-dioxiden, 1. Mitt. (1985)
    Springer
    Monatshefte für Chemie 116 (1985), S. 1141-1151 
    Details
    ISSN: 1434-4475
    Keywords: N-Phenyl-benzenecarbohydrazonoylchloride ; Cycloaddition reaction with N-[[(Ethoxycarbonyl)amino]sulfonyl]-N,N-diethylethanaminium, hydroxide, inner salt
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract 2,5-Dihydro-1,2,3,5-thiatriazole-1,1-dioxides2 a–2 c were obtained on treating N1-acyl-sulfamoylhydrazides with PCl5, yielding the corresponding N2-sulfamoyl-carbohydrazonoylchlorides which cyclized after addition of KOH orn-butyllithium. Methylation of2 c yields2 b and the 2,3-isomer10 in a 1 : 1 ratio. Reaction of the nitrilimine11 with the N-sulfonylamine12 affords the tetrazine13 and the isomeric dihydrothiatriazole-1,1-dioxides14 and15 via 1,3-dipolar cycloaddition reaction, while the dihydro-1,2,3,5-thiatriazole-1,1-dioxid16 reacts with ethyl chloroformate to yield the isomers14 and17.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00811248
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  • 8
    Electronic Resource
    Electronic Resource
    Über die Synthese von Dihydro-1,2,3,5-thiatriazol-1,1-dioxiden, 2. Mitt. (1985)
    Springer
    Monatshefte für Chemie 116 (1985), S. 1321-1327 
    Details
    ISSN: 1434-4475
    Keywords: Reactions with SO2F2 ; N,N-Diethyl-N′-chlorosulfonyl-chloroformamidine, reaction with hydrazines
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract By reaction of several N-phenyl-benzamidrazones with SO2F2 2-phenyl-2,5-dihydro-1,2,3,5-thiatriazole-1,1-dioxides2 a–c are formed. By reaction of N,N-diethyl-N′-chlorosulfonyl-chloroformamidine8 with hydrazines the corresponding 4-diethylamino-substituted derivatives9 a–d are obtained. Methylation of2 b yields two isomeric products5 and6, whereas by methylation of9 d only one product9 b is obtained.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00811103
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  • 9
    Electronic Resource
    Electronic Resource
    Conformational analysis of a Chlamydia-specific disaccharide α-Kdo-(2→8)-α-Kdo-(2→O)-allyl in aqueous solution and bound to a monoclonal antibody: Observation of intermolecular transfer NOEs (1998)
    Springer
    Journal of biomolecular NMR 12 (1998), S. 123-133 
    Details
    ISSN: 1573-5001
    Keywords: HMQC-trNOESY ; Kdo ; monoclonal antibody ; QUIET-trNOESY ; trNOESY ; trROESY
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract The disaccharide α-Kdo-(2→8)-α-Kdo (Kdo: 3-deoxy-d-manno-oct-2-ulosonic acid) represents a genus-specific epitope of the lipopolysaccharide of the obligate intracellular human pathogen Chlamydia. The conformation of the synthetically derived disaccharide α-Kdo-(2→8)-α-Kdo-(2→O)-allyl was studied in aqueous solution, and complexed to a monoclonal antibody S25-2. Various NMR experiments based on the detection of NOEs (or transfer NOEs) and ROEs (or transfer ROEs) were performed. A major problem was the extensive overlap of almost all 1H NMR signals of α-Kdo-(2→8)-α-Kdo-(2→O)-allyl. To overcome this difficulty, HMQC-NOESY and HMQC-trNOESY experiments were employed. Spin diffusion effects were identified using trROESY experiments, QUIET-trNOESY experiments and MINSY experiments. It was found that protein protons contribute to the observed spin diffusion effects. At 800 MHz, intermolecular trNOEs were observed between ligand protons and aromatic protons in the antibody binding site. From NMR experiments and Metropolis Monte Carlo simulations, it was concluded that α-Kdo-(2→8)-α-Kdo-(2→O)-allyl in aqueous solution exists as a complex conformational mixture. Upon binding to the monoclonal antibody S25-2, only a limited range of conformations is available to α-Kdo-(2→8)-α-Kdo-(2→O)-allyl. These possible bound conformations were derived from a distance geometry analysis using transfer NOEs as experimental constraints. It is clear that a conformation is selected which lies within a part of the conformational space that is highly populated in solution. This conformational space also includes the conformation found in the crystal structure. Our results provide a basis for modeling studies of the antibody–disaccharide complex.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1016047602190
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  • 10
    Electronic Resource
    Electronic Resource
    Glycan structure of the S-layer glycoprotein ofBacillus sp. L420-91 (1995)
    Springer
    Glycoconjugate journal 12 (1995), S. 99-107 
    Details
    ISSN: 1573-4986
    Keywords: Eubacteria ; glycoprotein ; surface layer (S-layer) ; glycan structure ; 1H and13C-NMR
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Preliminary taxonomic characterization of isolate L420-91 has revealed that this organism is closely related to the speciesBacillus aneurinolyticus. The bacterium is covered by a squarely arranged crystalline surface layer composed of identical glycoprotein subunits with an apparent molecular mass in the range of 109 kDa. A total carbohydrate content of approximately 3.5% (wt/wt) was determined in the purified surface layer glycoprotein. Glycopeptides were obtained after exhaustive Pronase digestion and purification including gel filtration, ion exchange chromatography and HPLC. From the combined evidence of composition analysis, Smith degradation and nuclear magnetic resonance spectroscopy experiments we propose the following structure for the glycan chain of the surface layer glycoprotein: $$\begin{array}{*{20}c} { \to 3) - \alpha - D - Rhap - (1 \to 3) - \alpha - D - Rhap - (1 \to 2) - \alpha - D - Rhap - (1 \to 2) - \alpha - D - Rhap - (1 \to } \\ {\begin{array}{*{20}c} {\begin{array}{*{20}c} 2 \\ \uparrow \\ 1 \\ \end{array} } & {\begin{array}{*{20}c} 2 \\ \uparrow \\ 1 \\ \end{array} } \\ \end{array} } \\ {\alpha - D - Fucp3NAc \alpha - D - Fucp3NAc} \\ \end{array}$$
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00731875
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