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

文献类型： 外文期刊

第一作者： Zhang, Ruo-Nan

作者： Zhang, Ruo-Nan;Ren, Fei-Fei;Zhou, Cheng-Bo;Xu, Jun-Feng;Yi, Hui-Yu;Deng, Xiao-Juan;Cao, Yang;Yang, Wan-Ying;Yu, Xiao-Qiang;Yu, Xiao-Qiang;Ye, Ming-Qiang

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关键词： BmEsr16; Lipopolysaccharide; Antibacterial; MD-2; Bombyx mori

期刊名称：DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY （ 影响因子：3.636； 五年影响因子：3.654 ）

ISSN： 0145-305X

年卷期： 2018 年 88 卷

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收录情况： SCI

摘要： Lipopolysaccharide (LPS) is a common component of the outermost cell wall in Gram-negative bacteria. In mammals, LPS serves as an endotoxin that can be recognized by a receptor complex of TLR4 (Toll-like receptor 4) and MD-2 (myeloid differentiation-2) and subsequently induce a strong immune response to signal the release of tumor necrosis factor (TNF). In Drosophila melanogaster, no receptors for LPS have been identified, and LPS cannot activate immune responses. Here, we report a protein, BmEsr16, which contains an ML (MD-2-related lipid-recognition) domain, may function as an LPS receptor in the silkworm Bombyx mori. We showed that antibacterial activity in the hemolymph of B. mori larvae was induced by Escherichia coli, peptidoglycan (PGN) and LPS and that the expression of antimicrobial peptide genes was also induced by LPS. Furthermore, both the expression of BmEsr16 mRNA in the fat body and the expression of BmEsr16 protein in the hemolymph were induced by LPS. Recombinant BmEsr16 bound to LPS and lipid A, as well as to PGN, lipoteichoic acid, but not to laminarin or mannan. More importantly, LPS-induced immune responses in the hemolymph of B. mori larvae were blocked when the endogenous BmEsr16 protein was neutralized by polyclonal antibody specific to BmEsr16. Our results suggest that BmEsr16 may function as a key accessory protein for LPS signaling in B. mori.

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