ABSTRACT
The cross-reactivity of the monoclonal antibodies (mAbs ) was confirmed using different experimental conditions and procedures, including enzyme-linked immunosorbent assay (ELISA) on purified LPS, ELISA on high-density lipoprotein (HDL)-LPS complexes, competitive ELISA, passive hemolysis assay and sodium deoxycholatepolyacrylamide gel electrophoresis (DOC-PAGE) and Western blotting of LPS. Moreover, heat treatment of the preparation abolished protection, and WN1 222-5 was not active against LPS to which it did not bind, indicating that induction of cross-tolerance was not responsible for the neutralizing properties of the Ab. As these models are dependent on the administration of purified LPS, it was relevant to analyze additional models in which LPS toxic effects are caused through a direct administration of the purified endotoxin. The study of Bahrami et al. is relevant in that it shows that the LPS-neutralizing properties of anticore LPS mAbs are not limited to purified and isolated LPS but extend to naturally occurring LPS, confirming previous data.
