Identification and molecular characterization of a chitin deacetylase from Bombyx mori peritrophic membrane

Int J Mol Sci. 2014 Jan 27;15(2):1946-61. doi: 10.3390/ijms15021946.

Abstract

The insect midgut epithelium is generally lined with a unique chitin and protein structure, the peritrophic membrane (PM), which facilitates food digestion and protects the gut epithelium. PM proteins are important determinants for PM structure and formation. In this study, the silkworm Bombyx mori midgut PM protein BmCDA7 was identified by proteomic tools. The full-length BmCDA7 cDNA is 1357 bp; the deduced protein is composed of 379 amino acid residues and includes a 16 amino acid residue signal peptide, a putative polysaccharide deacetylase-like domain and 15 cysteine residues present in three clusters. The heterologously expressed proteins of the BmCDA7 gene in yeast displayed chitin deacetylase activity. Expression of B. mori BmCDA7 was detected in the midgut at both the transcriptional and translational levels. The BmCDA7 gene was expressed by the newly hatched silkworm larvae until day seven of the fifth instar and was expressed at a high level in the newly exuviated larvae of different instars. The functions and regulatory mechanism of BmCDA7, however, need further investigation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amidohydrolases / chemistry
  • Amidohydrolases / genetics*
  • Amidohydrolases / metabolism*
  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Bombyx / enzymology*
  • Bombyx / genetics*
  • Enzyme Activation
  • Gene Expression
  • Insect Proteins*
  • Molecular Sequence Data
  • Organ Specificity / genetics
  • Protein Transport
  • Proteomics
  • Recombinant Proteins

Substances

  • Insect Proteins
  • Recombinant Proteins
  • Amidohydrolases
  • chitin deacetylase