The Journal of Immunology, Vol 137, Issue 11 3614-3619, Copyright © 1986 by American Association of Immunologists

ARTICLES

Analysis of the fine specificity and cross-reactivity of monoclonal anti-lipid A antibodies

TN Kirkland, DE Colwell, SM Michalek, JR McGhee and EJ Ziegler

We have investigated the fine specificity of anti-lipid A antibodies to identify conserved lipid A antigens. Because lipid A derived from many different Gram-negative bacteria has similar biologic activities, the conserved regions may be of particular importance for the immunostimulatory and toxic properties of lipid A. We found that five of nine antibodies bound to a wide variety of Gram-negative bacteria. All these widely cross-reactive antibodies bound to the same antigenic site within lipid A. Polymyxin B, an inhibitor of lipid A activity, bound to this site as well. The widely cross-reactive antibodies bound to native and base-hydrolyzed lipid A equally well, and also bound to the monosaccharide precursor lipid X. The less cross-reactive antibodies recognized base-hydrolyzed lipid A poorly, and did not recognize lipid X at all. Other investigators have shown that lipid X has some of the activities of lipid A in vitro and can inhibit the lethal toxicity of LPS in vivo. On the basis of this study, we suggest that lipid X contains a conserved lipid A epitope as well.

This article has been cited by other articles:

				S.E. Greisman and C.A. Johnston 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, April 1, 1997; 4(2): 123 - 153. [Abstract] [PDF]