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Innate Immun ; 17(5): 427-38, 2011 Oct.
Article in English | MEDLINE | ID: mdl-20682588

ABSTRACT

Lipopolysaccharides (LPSs) from Gram-negative bacteria are strong elicitors of the human immune systems. There is strong evidence that aggregates and not monomers of LPS play a decisive role at least in the initial stages of cell activation of immune cells such as mononuclear cells. In previous reports, it was shown that the biologically most active part of enterobacterial LPS, hexa-acyl bisphosphorylated lipid A, adopts a particular supramolecular conformation, a cubic aggregate structure. However, little is known about the size and morphology of these aggregates, regarding the fact that LPS may have strong variations in the length of the saccharide chains (various rough mutant and smooth-form LPS). Thus, in the present paper, several techniques for the determination of details of the aggregate morphology such as freeze-fracture and cryo-electron microscopy, analytical ultracentrifugation, laser backscattering analysis, and small-angle X-ray scattering were applied for various endotoxin (lipid A and different LPS) preparations. The data show a variety of different morphologies not only for different endotoxins but also when comparing different applied techniques. The data are interpreted with respect to the suitability of the single techniques, in particular on the basis of available literature data.


Subject(s)
Biopolymers/metabolism , Lipid A/metabolism , Salmonella Infections/microbiology , Salmonella enterica/metabolism , Salmonella enterica/ultrastructure , Biopolymers/chemistry , Biopolymers/genetics , Carbohydrate Conformation , Cryoelectron Microscopy , Host-Pathogen Interactions/immunology , Humans , Lipid A/chemistry , Lipid A/genetics , Mutation/genetics , Salmonella Infections/immunology , Salmonella enterica/genetics , Salmonella enterica/pathogenicity , Structure-Activity Relationship , Ultracentrifugation , X-Ray Diffraction
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