Uwe Mamat

TL;DR: The biological analysis of synthetic lipid A partial structures proved that the expression of endotoxic activity depends on a unique primary structure and a peculiar endotoxic conformation, and molecular and submolecular details of the specificity of the interaction of lipid A with responsive host cells are determined.

TL;DR: Endotoxins, due to their various potent biological activities soon attracted worldwide scientific interest, were first found to be produced by Vibrio cholerae bacteria and later by Salmonella and Serratia.

TL;DR: Biological analysis of synthetic lipid A partial structures proved that the expression of endotoxic activity depends on a unique structural arrangement and conformation and analyses have provided insight into the determinants required for lipid A binding to and activation of human target cells.

TL;DR: The preparation and characterization of endotoxin-free E. coli strains are described, the direct production of recombinant proteins with negligible endotoxin contamination is demonstrated, and Lipid IVA does not trigger an endotoxic response in humans typical of bacterial LPS chemotypes.

TL;DR: These results challenge the established E. coli Kdo2-lipid A dogma, indicating that the previously observed and well-documented dependence of cell viability on the synthesis of Kdo stems from a lethal pleiotropy precipitated after the depletion of the carbohydrate, rather than an inherent need for the Kdo molecule itself as an indispensable structural component of the OM LPS layer.