Bombyx mori Serpin6 regulates prophenoloxidase activity and the expression of antimicrobial proteins

Gene. 2017 Apr 30:610:64-70. doi: 10.1016/j.gene.2017.02.011. Epub 2017 Feb 8.

Abstract

Serpins are a family of serine protease inhibitors that are found widely in insects. They play an important role in insect physiological responses, such as innate immunity and development. In this study, we obtained the Bombyx mori serpin6 (BmSerpin6) sequence from National Center for Biotechnology Information (NCBI) and the silkworm genome database (SilkDB). Reverse transcription PCR (RT-PCR) results showed that BmSerpin6 was expressed highly in hemocytes, the midgut, and the fat body. After challenging with Micrococcus luteus (Mi) and Serratia marcescens (Sm), the BmSerpin6 expression level was induced significantly. Transcript levels of gloverin2 and prophenoloxidase (PPO) activity were reduced significantly in the fat body and hemocytes after injecting the recombinant BmSerpin6 protein into silkworm larvae. A BmSerpin6 recombinant plasmid (BmSerpin6-pAC 5.1) was constructed successfully and transfected into Drosophila S2 cells, which resulted in significantly reduced expression of the drosomycin protein. These results indicated that BmSerpin6 might regulate silkworm immune responses.

Keywords: Antimicrobial peptides; Bombyx mori; Prophenoloxidase; Serpin6.

MeSH terms

  • Animals
  • Antimicrobial Cationic Peptides / genetics
  • Antimicrobial Cationic Peptides / immunology
  • Bombyx / immunology*
  • Bombyx / metabolism*
  • Bombyx / microbiology
  • Catechol Oxidase / metabolism
  • Cell Line
  • Drosophila / cytology
  • Drosophila Proteins
  • Enzyme Precursors / metabolism
  • Fat Body / metabolism
  • Hemocytes / metabolism
  • Immunity, Innate
  • Insect Proteins / genetics
  • Insect Proteins / metabolism*
  • Micrococcus luteus / physiology
  • Phylogeny
  • Serpins / metabolism*
  • Serratia marcescens / physiology

Substances

  • Antimicrobial Cationic Peptides
  • Drosophila Proteins
  • Enzyme Precursors
  • Insect Proteins
  • Serpins
  • DRS protein, Drosophila
  • pro-phenoloxidase
  • Catechol Oxidase