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Taxonomic group: bacteria / Proteobacteria (Phylum: Proteobacteria)
Associated disease: infection due to Escherichia coli [ICD11: XN6P4

]

NCBI PubMed ID: 23316371
Publication DOI: 10.1155/2012/475153
Journal NLM ID: 101553819
Publisher: Cairo: Hindawi Pub Corp
Correspondence: Tony Velkov <tony.velkov

monash.edu.au>
Institutions: Institute for Molecular Bioscience, The University of Queensland, 306 Carmody Road, St. Lucia, QLD 4072, Australia, Drug Development and Innovation, Drug Delivery, Disposition and Dynamics, Monash Institute of Pharmaceutical Sciences, Monash University, 381 Royal Parade, Parkville, VIC 3052, Australia, Medicinal Chemistry, Monash Institute of Pharmaceutical Sciences, Monash University, 381 Royal Parade, Parkville, VIC 3052, Australia, Priority Research Centre in Reproductive Science, School of Environmental and Life Sciences, University of Newcastle, Callaghan, NSW 2308, Australia

The ability of AGP to bind circulating lipopolysaccharide (LPS) in plasma is believed to help reduce the proinflammatory effect of bacterial lipid A molecules. Here, for the first time we have characterized human AGP binding characteristics of the LPS from a number of pathogenic Gram-negative bacteria: Escherichia coli, Salmonella typhimurium, Klebsiella pneumonia, Pseudomonas aeruginosa, and Serratia marcescens. The binding affinity and structure activity relationships (SAR) of the AGP-LPS interactions were characterized by surface plasma resonance (SPR). In order to dissect the contribution of the lipid A, core oligosaccharide and O-antigen polysaccharide components of LPS, the AGP binding affinity of LPS from smooth strains, were compared to lipid A, Kdo2-lipid A, R(a), R(d), and R(e) rough LPS mutants. The SAR analysis enabled by the binding data suggested that, in addition to the important role played by the lipid A and core components of LPS, it is predominately the unique species- and strain-specific carbohydrate structure of the O-antigen polysaccharide that largely determines the binding affinity for AGP. Together, these data are consistent with the role of AGP in the binding and transport of LPS in plasma during acute-phase inflammatory responses to invading Gram-negative bacteria.

O-antigen, lipid A, gram negative bacteria, lipopolysaccharide-binding, AGP binding, SPR

Structure type: oligomer
Location inside paper: p.3, table 1
Aglycon: lipid A
Trivial name: R3 core
Compound class: LPS
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130650,IEDB_130659,IEDB_130670,IEDB_133751,IEDB_136906,IEDB_137472,IEDB_140088,IEDB_141794,IEDB_141807,IEDB_142488,IEDB_144998,IEDB_146664,IEDB_151528,IEDB_151531,IEDB_190606,IEDB_2189047,IEDB_226811,IEDB_232584,IEDB_983931,SB_192,SB_7

Methods: molecular modeling, fluorescence spectroscopy, surface plasmon resonance (SPR)
3D data: 3D data

Related record ID(s): 27188, 28397, 28398, 28399, 28400, 28401, 28402, 28404, 28405, 28406, 28407, 28408, 28409, 28410, 28411
NCBI Taxonomy refs (TaxIDs): 1090940, 2170726
Reference(s) to other database(s): GTC:G36284VM
Show glycosyltransferases

There is only one chemically distinct structure:

NCCOP(=O)(O)OP(=O)(O)O[C@@H]1[C@@H]([C@@H](O)CO)O[C@H](O[C@@H]2[C@H](O[C@]3(C(=O)O)C[C@@H](O)[C@@H](O)[C@@H]([C@H](O)CO)O3)C[C@](O)(C(=O)O)O[C@@H]2[C@H](O)CO)[C@@H](O)[C@H]1O[C@H]1O[C@H]([C@@H](O)CO[C@H]2O[C@H]([C@@H](O)CO[C@H]3O[C@H](CO)[C@@H](O)[C@H](O)[C@H]3O)[C@@H](O)[C@H](O)[C@@H]2O)[C@@H](OP(=O)(O)O)[C@H](O[C@H]2O[C@H](CO)[C@@H](O)[C@H](O[C@H]3O[C@H](CO)[C@H](O)[C@H](O[C@H]4O[C@H](CO)[C@@H](O)[C@H](O)[C@H]4N)[C@H]3O[C@H]3O[C@H](CO)[C@@H](O)[C@H](O)[C@H]3O[C@H]3O[C@H](CO)[C@@H](O)[C@H](O)[C@H]3O)[C@H]2O)[C@@H]1O

SVG MW SMILES 3D mol Ionize