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Toll-like receptors (TLRs) are evolutionarily conserved pattern-recognition molecules that recognize different microbial products during infection and serve as an important link between the innate and adaptive immune responses (1). The signaling of these TLRs is kept under tight control by the expression of endogenous inhibiting proteins such as RP105, a recently identified homolog of TLR4. This protein, in association with MD-1, interacts with and inhibits the TLR4/MD-2 signaling pathway (2). While MD-2 can directly bind to LPS, one of the activating molecules of TLR4, the function of MD-1 is less well-known. It has been suggested however, that the RP105/MD-1 complex influences antibody production mediated by both TLR4/MD-2 and TLR2 receptor complexes (4).