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

Ruo-Nan Zhang1, Fei-Fei Ren1, Cheng-Bo Zhou1

  • 1Laboratory of Insect Molecular Biology and Biotechnology, Guangdong Provincial Key Laboratory of Agro-animal Genomics and Molecular Breeding, College of Animal Science, South China Agricultural University, Guangzhou 510642, China.

Developmental and Comparative Immunology
|July 17, 2018
PubMed

Insights

Researchers identified BmEsr16, a protein in silkworms (Bombyx mori), that may act as a lipopolysaccharide (LPS) receptor. This discovery is crucial for understanding insect immunity and LPS signaling pathways in invertebrates.

Area of Science:

  • Insect immunology
  • Molecular biology
  • Biochemistry

Background:

  • Lipopolysaccharide (LPS) is a Gram-negative bacterial cell wall component recognized by Toll-like receptor 4 (TLR4) and myeloid differentiation-2 (MD-2) in mammals, triggering immune responses.
  • Unlike in mammals, LPS does not activate immune responses in Drosophila melanogaster due to unidentified receptors.

Purpose of the Study:

  • To investigate the potential role of the ML domain-containing protein BmEsr16 as an LPS receptor in the silkworm Bombyx mori.
  • To elucidate the mechanism of LPS-induced immune responses in Bombyx mori.

Main Methods:

  • Induction of antibacterial activity and antimicrobial peptide gene expression by LPS in Bombyx mori larvae.
  • Analysis of BmEsr16 mRNA and protein expression levels following LPS stimulation.
  • Binding assays using recombinant BmEsr16 with various bacterial and fungal components.
  • Neutralization of endogenous BmEsr16 using specific polyclonal antibodies to assess its role in LPS-induced immune responses.

Main Results:

  • LPS induced antibacterial activity and antimicrobial peptide gene expression in Bombyx mori larvae.
  • LPS upregulated both BmEsr16 mRNA and protein expression.
  • Recombinant BmEsr16 demonstrated binding to LPS, lipid A, peptidoglycan (PGN), and lipoteichoic acid.
  • Neutralization of BmEsr16 blocked LPS-induced immune responses in silkworm larvae.

Conclusions:

  • BmEsr16 may function as a key accessory protein for lipopolysaccharide (LPS) signaling in Bombyx mori.
  • This study identifies a potential LPS receptor in insects, expanding our understanding of innate immunity.
  • BmEsr16's ability to bind multiple bacterial components suggests a broad role in recognizing microbial invaders.
Keywords:
AntibacterialBmEsr16Bombyx moriLipopolysaccharideMD-2

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