Previously, we identified an 80 kDa membrane protein (LMP80) that is capabl
e of binding to LPS and lipid A in the presence of LBP and sCD14. LMP80 cou
ld also be detected after immuno-coprecipitation of cell membranes with LPS
and lipid A, indicating a physical contact of LMP80 and LPS/lipid A. Furth
er analysis and peptide sequencing revealed that LMP80 is identical to CD55
(decay accelerating factor, DAF), a regulatory molecule of the complement
cascade. Transfection of LPS-hyporesponsive Chinese hamster ovary (CHO) cel
ls with human CD55 resulted in the translocation of NF-kappaB upon stimulat
ion with LPS or lipid A. Our results demonstrate a new functional role of C
D55 as a molecule able to mediate LPS-induced activation of cells that may
be part of a multimeric LPS receptor complex.