Several self-defense proteins have been isolated from the silkworm, Bombyx mori and their amino acid sequences determined. These proteins include novel antibacterial proteins designated lebocin and moricin, and a novel lectin designated hemocytin, an insect homologue of mammalian von Willebrand factor. Antibacterial mechanisms of lebocin and moricin have been analyzed and their ability to form ion channels in bacterial membranes play an important role in defense against bacterial infection, cDNAs and genes encoding these proteins have been cloned to examine their induction mechanisms upon bacterial infection. Regulatory motifs such as the κB-like and GATA sequence have been identified in the B. mori antibacterial proteins. On the other hand, hemocytin gene expression was confirmed to occur upon bacterial infection and before pupation under naive conditions, suggesting that hemocytin plays an important role in both immunity and metamorphosis. Moreover, this review also describes the releasing mechanisms of a bacterial cell wall component, lipopolysaccharide (LPS), from intact bacteria, clearance of LPS from B. mori hemolymph and a possible signal transduction pathway for antibacterial protein gene expression.
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