Taxonomic group: bacteria / Chlamydiae
(Phylum: Chlamydiae)
Associated disease: infection due to Chlamydia [ICD11:
XN27H 
]
NCBI PubMed ID: 11041842Journal NLM ID: 0370623Publisher: American Chemical Society
Correspondence: thomas.peters
chemie.mu-luebeck.de
Institutions: Institut fur Chemie, Medizinische Universitat Lubeck, Ratzeburger Allee 160, D-23538 Lubeck, Germany, Institut fur Chemie der Universitat fur Bodenkultur Wien, A-1190 Wien, Austria, Forschungszentrum Borstel, Zentrum fur Medizin und Biowissenschaften, Borstel, Germany
A NMR study of the binding of the synthetic disaccharides α-Kdo-(2→4)-α-Kdo-(2→O)-allyl 1 (Kdo, 3-deoxy-D-manno-oct-2-ulopyranosonic acid) and α-Kdo-(2→8)-α-Kdo-(2→O)-allyl 2, representing partial structures of the lipopolysaccharide epitope of the intracellular bacteria Chlamydia, to corresponding monoclonal antibodies (mAbs) S23-24, S25-39, and S25-2 is presented. The conformations of 1 bound to mAbs S25-39 and of 2 bound to mAbs S23-24 and S25-39 were analyzed by employing transfer-NOESY (trNOESY) and QUIET-trNOESY experiments. A quantitative analysis of QUIET-trNOESY buildup curves clearly showed that S25-39 recognized a conformation of 1 that was similar to the global energy minimum of 1, and significantly deviated from the conformation of 1 bound to mAb S25-2. For disaccharide 2, only a qualitative analysis was possible because of severe spectral overlap. Nevertheless, the analysis showed that all mAbs most likely bound to only one conformational family of 2. Saturation transfer difference (STD) NMR experiments were then employed to analyze the binding epitopes of the disaccharide ligands 1 and 2 when binding to mAbs S23-24, S25-39, and S25-2. It was found that the nonreducing pyranose unit was the major binding epitope, irrespective of the mAb and the disaccharide that were employed. Individual differences were related to the engagement of other portions of the disaccharide ligands.
Lipopolysaccharide, NMR, antibodies, antibody, epitope, Chlamydia, epitopes, disaccharide, binding, Synthetic, disaccharides, chlamydial, mapping
Structure type: oligomer
Location inside paper: abstract
Compound class: LPS
Contained glycoepitopes: IEDB_130650,IEDB_130659
Biological activity: biological activity data
Biosynthesis and genetic data: genetic data
Synthetic data: chemical
3D data: 3D data
Related record ID(s): 496, 3235, 4142, 116696
NCBI Taxonomy refs (TaxIDs): 810Reference(s) to other database(s): GlycomeDB:
5576
Show glycosyltransferases
There is only one chemically distinct structure:
Found 
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