Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
Associated disease: infection due to Escherichia coli [ICD11:
XN6P4 
]
NCBI PubMed ID: 7768599Journal NLM ID: 0246127WWW link: http://iai.asm.org/content/63/6/2201.full.pdfPublisher: American Society for Microbiology
Institutions: Sepsis Research Department, XOMA Corporation, Berkeley, California 947101, Neurocrine Biosciences, San Diego, California 921212, Department of Health and Human Services, Center for Biologics Evaluation and Research, Food and Drug Administration, Bethesda, MD, USA3, and Departments of Biochemistry and Chemistry, Michigan State University, East Lansing, Michigan 48824
Both human bactericidal/permeability-increasing protein (BPI) and a recombinant amino-terminal fragment of BPI (rBPI23) have been shown to bind with high affinity to the lipid A region of lipopolysaccharide (LPS) (H. Gazzano-Santoro, J. B. Parent, L. Grinna, A. Horwitz, T. Parsons, G. Theofan, P. Elsbach, J. Weiss, and P. J. Conlon, Infect. Immun. 60:4754-4761, 1992). In the present study, lipid A preparations derived from bacterial LPS as well as synthetic lipid A's and various lipid A analogs were used to determine the structural elements required for rBPI23 binding. rBPI23 bound in vitro to a variety of synthetic and natural lipid A preparations (both mono- and diphosphoryl forms), including lipid A's prepared from Escherichia coli and Salmonella, Neisseria, and Rhizobium species. Binding does not require that the origin of negative charge be phosphate, since rBPI23 bound with high affinity to lipid A's isolated from Rhizobium species that contain carboxylate (Rhizobium trifolii) or sulfate (Rhizobium meliloti) anionic groups and lack phosphate. Lipid A acyl chains are important, since rBPI23 did not bind to four synthetic variants of the β(1-6)-linked D-glucosamine disaccharide lipid A head group, all devoid of acyl chains. rBPI23 also bound weakly to lipid X, a monosaccharide lipid precursor of LPS corresponding to the reducing half of lipid A. Lipid IVA, a precursor identical to E. coli lipid A except that it lacks the 2' and 3' acyl chains, was the simplest structure identified in this study that rBPI23 bound with high affinity. These results demonstrate that rBPI23 has a binding specificity for the lipid A region of LPS and binding involves both electrostatic and hydrophobic components.
structural, characterization, lipid, lipid A, protein, fragment, binding, recombinant, bactericidal/permeability increasing protein
Structure type: oligomer
Location inside paper: p.3655, fig.1, E. coli
Trivial name: lipid IVA
Compound class: LOS, lipid A, glycolipid
Contained glycoepitopes: IEDB_135394,IEDB_135515,IEDB_141807,IEDB_151531,IEDB_176772,IEDB_534864
Methods: radiolabeling, serological methods
Related record ID(s): 31307, 31308
NCBI Taxonomy refs (TaxIDs): 562Reference(s) to other database(s): GlycomeDB:
7396
Show glycosyltransferases
There is only one chemically distinct structure:
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