Preparation and characterization of truncated human lipopolysaccharide-binding protein in Escherichia coli

2006 ◽  
Vol 49 (2) ◽  
pp. 276-283 ◽  
Author(s):  
Jun Kohara ◽  
Naoko Tsuneyoshi ◽  
Jean-François Gauchat ◽  
Masao Kimoto ◽  
Kenji Fukudome
Keyword(s):  
Escherichia Coli ◽  
Binding Protein ◽  
Lipopolysaccharide Binding Protein ◽  
Lipopolysaccharide Binding

Lipopolysaccharide-Binding Protein Accelerates and Augments Escherichia coli Phagocytosis by Alveolar Macrophages

2000 ◽  
Vol 94 (2) ◽  
pp. 159-166 ◽  
Author(s):  
Richard D Klein ◽  
Grace L Su ◽  
Carl Schmidt ◽  
Alireza Aminlari ◽  
Lars Steinstraesser ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Alveolar Macrophages ◽  
Binding Protein ◽  
Lipopolysaccharide Binding Protein ◽  
Lipopolysaccharide Binding

scholarly journals Purification and characterization of murine lipopolysaccharide-binding protein.

1993 ◽  
Vol 61 (2) ◽  
pp. 378-383 ◽  
Author(s):  
P Gallay ◽  
S Carrel ◽  
M P Glauser ◽  
C Barras ◽  
R J Ulevitch ◽  
...  
Keyword(s):  
Binding Protein ◽  
Lipopolysaccharide Binding Protein ◽  
Purification And Characterization ◽  
Lipopolysaccharide Binding

scholarly journals Lactoferrin Inhibits the Endotoxin Interaction with CD14 by Competition with the Lipopolysaccharide-Binding Protein

1998 ◽  
Vol 66 (2) ◽  
pp. 486-491 ◽  
Author(s):  
Elisabeth Elass-Rochard ◽  
Dominique Legrand ◽  
Valerie Salmon ◽  
Anca Roseanu ◽  
Mihaela Trif ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Binding Sites ◽  
Lipid A ◽  
Binding Protein ◽  
Amino Acid Residues ◽  
Lipopolysaccharide Binding Protein ◽  
Maximal Inhibition ◽  
Acute Phase Serum ◽  
Lipopolysaccharide Binding ◽  
Lps Binding

ABSTRACT Human lactoferrin (hLf), a glycoprotein released from neutrophil granules during inflammation, and the lipopolysaccharide (LPS)-binding protein (LBP), an acute-phase serum protein, are known to bind to the lipid A of LPS. The LPS-binding sites are located in the N-terminal regions of both proteins, at amino acid residues 28 to 34 of hLf and 91 to 108 of LBP. Both of these proteins modulate endotoxin activities, but they possess biologically antagonistic properties. In this study, we have investigated the competition between hLf and recombinant human LBP (rhLBP) for the binding of Escherichia coli 055:B5 LPS to the differentiated monocytic THP-1 cell line. Our studies revealed that hLf prevented the rhLBP-mediated binding of LPS to the CD14 receptor on cells. Maximal inhibition of LPS-cell interactions by hLf was raised when both hLf and rhLBP were simultaneously added to LPS or when hLf and LPS were mixed with cells 30 min prior to the incubation with rhLBP. However, when hLf was added 30 min after the interaction of rhLBP with LPS, the binding of the rhLPS-LBP complex to CD14 could not be reversed. These observations indicate that hLf competes with rhLBP for the LPS binding and therefore interferes with the interaction of LPS with CD14. Furthermore, experiments involving competitive binding of the rhLBP-LPS complex to cells with two recombinant mutated hLfs show that in addition to residues 28 to 34, another basic cluster which contains residues 1 to 5 of hLf competes for the binding to LPS. Basic sequences homologous to residues 28 to 34 of hLf were evidenced on LPS-binding proteins such as LBP, bactericidal/permeability-increasing protein, and Limulus anti-LPS factor.

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