An ML protein from the silkworm Bombyx mori may function as a key accessory protein for lipopolysaccharide signaling

LPS is a common component of the outermost cell wall in Gram-negative bacteria. For mammals, LPS serves as an endotoxin to induce a strong immune response. In Drosophila melanogaster, no receptors for LPS have been identified and LPS can't activate immune responses. In this paper, we report a protein, BmEsr16, which contains an ML domain, may function as a receptor for LPS in the silkworm. Our results showed that LPS-induced immune responses in the hemolymph of B. mori larvae were blocked when endogenous BmEsr16 protein was neutralized by polyclonal antibody specific to BmEsr16.192