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The Journal of Immunology, Vol 141, Issue 10 3523-3531, Copyright © 1988 by American Association of Immunologists
ARTICLES |
VL Tesh and DC Morrison
Department of Microbiology and Immunology, Emory University School of Medicine, Atlanta, GA 30322.
As a result of the incubation of Escherichia coli in normal human serum, a finite fraction of LPS is released from the bacterial membrane. Approximately half of the LPS released by the action of serum (S-LPS) exists in association with serum proteins in a lower m.w. form than that manifest in phenol-water extracted LPS preparations. The two major LPS-serum protein complexes have apparent Mr of 68 and 32 kDa. The LPS subunit heterogeneity of S-LPS, however, does not appear to differ significantly from LPS retained on the bacteria after serum treatment, or from LPS derived by lysis of whole cells. The biologic activities of S-LPS and phenol-water extracted LPS examined in these studies, differed significantly. In contrast to phenol-water extracted LPS, S-LPS was 1) reduced in lethal toxicity for sensitized mice; 2) reduced in Limulus reactivity; 3) a more potent murine splenocyte mitogen; 4) reduced in the capacity to elicit extracellular, but not membrane-associated IL-1; and 5) reduced in the ability to mediate TNF production. These data suggest that humoral "detoxification" of LPS may involve, in part, the formation of LPS-serum protein complexes with reduced capacities to elicit extracellular cytokine production, whereas the immunomodulatory effects of LPS appear to be enhanced.
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