Caspase-1 from the silkworm, Bombyx mori, is involved in Bombyx mori nucleopolyhedrovirus infection

Z Naturforsch C J Biosci. 2017 Mar 1;72(3-4):147-153. doi: 10.1515/znc-2016-0133.

Abstract

Caspase-1 is one of the effector caspases in mammals that plays a central role in apoptosis. However, the lepidopteran caspase-1, especially the Bombyx mori caspase-1 (Bm-caspase-1), has not been investigated in detail. In this study, Bm-caspase-1 was identified from an expressed sequence tag database in B. mori by BLAST search. The open reading frame of Bm-caspase-1 contained 879 nucleotides and encoded 293 amino acids with a predicted molecular mass of 33 kDa. Bm-caspase-1 contained two consensus amino acid motifs of caspase cleavage sites, DEGDA and TETDG. Caspase activity assays revealed significant proteolytic activity of the Ac-DEVD-pNA substrate. Bm-caspase-1 can be detected in all tissues and developmental stages by a semi quantitative polymerase chain reaction assay. More importantly, the expression level of Bm-caspase-1 is increased upon baculovirus infection and up-regulated in BmNPV-resistant silkworms. Taken together, these results indicate that Bm-caspase-1 plays an important role during baculovirus infection.

MeSH terms

  • Amino Acid Motifs
  • Animals
  • Bombyx / enzymology
  • Bombyx / genetics*
  • Bombyx / immunology
  • Bombyx / virology
  • Caspase 1 / genetics*
  • Caspase 1 / metabolism
  • Gene Expression Regulation
  • Host-Pathogen Interactions*
  • Insect Proteins / genetics*
  • Insect Proteins / metabolism
  • Larva / enzymology
  • Larva / genetics*
  • Larva / immunology
  • Larva / virology
  • Molecular Weight
  • Nucleopolyhedroviruses / genetics*
  • Nucleopolyhedroviruses / growth & development
  • Nucleopolyhedroviruses / metabolism
  • Open Reading Frames
  • Phylogeny
  • Sequence Alignment
  • Sequence Homology, Amino Acid

Substances

  • Insect Proteins
  • Caspase 1