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Infect Immun. 1988 January; 56(1): 204-212

Control of endotoxin activity and interleukin-1 production through regulation of lipopolysaccharide-lipoprotein binding by a macrophage factor.

Centre National de la Recherche Scientifique UA-579, Institut Pasteur, Paris, France.

ABSTRACT

Lipopolysaccharides (LPSs) extracted from gram-negative bacteria are much less active when bound to serum lipoproteins. We present evidence here that the binding of radiolabeled LPS extracted from Escherichia coli O113 and Salmonella typhimurium to lipoproteins in rabbit serum is increased 8 to 24 h after a single intravenous injection of homologous or heterologous LPS. Supernatants of activated macrophages containing interleukin-1 also stimulate increased binding. The isolated product of this binding does not induce the production of interleukin-1 by macrophages in vivo or in vitro and is unable itself to stimulate increased binding of LPS to lipoprotein. Normal rabbit sera spiked with lipoprotein fractions prepared from tolerant but not normal rabbit sera bind increased amounts of LPS. These data suggest that there may exist a self-regulated mechanism for decreasing the toxicity of LPS and the production of LPS-induced interleukin-1; this mechanism is controlled by a macrophage factor and functions through altering the binding of LPS to certain serum lipoproteins.

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• Greisman, S.E., Johnston, C.A. (1997). Review: Evidence against the hypothesis that antibodies to the inner core of lipopolysaccharides in antisera raised by immunization with enterobacterial deep-rough mutants confer broad-spectrum protection during Gram-negative bacterial sepsis. Innate Immunity 4: 123-153 [Abstract]