Cloning and Tissue-Specific Expression of a Chitin Deacetylase Gene from Helicoverpa armigera (Lepidoptera: Noctuidae) and Its Response to Bacillus thuringiensis

Chitin deacetylases (CDAs) convert chitin into chitosan, the N-deacetylated form of chitin, which influences the mechanical and permeability properties of structures such as the cuticle and peritrophic matrices. In this article, a new CDA encoding gene, Hacda2, was cloned by reverse transcription-polymerase chain reaction method in Helicoverpa armigera (Hubner) (Lepidoptera: Noctuidae), with an open reading frame of 1,611 bp. The deduced protein composed of 536 amino acid residues with a signal peptide, a chitin-binding domain, a low-density lipoprotein receptor class A domain, and a polysaccharide deacetylase-like catalytic domain. The highest expression level of Hacda2 was detected in fat body among tissues tested in the fifth-instar larvae using real-time quantitative polymerase chain reaction method. Feeding of Bacillus thuringiensis (Bt) (Bacillales: Bacillaceae) diet changed the expression level of Hacda1, Hacda2, Hacda5a, and Hacda5b significantly and differentially in the third-instar larvae. Hacda5a and Hacda5b expression were initially down-regulated and then up-regulated, whereas, the expression level of Hacda1 and Hacda2 was suppressed constantly postfeeding on Bt diet. These results suggested that HaCDAs may be involved in the response of H. armigera larvae to Bt and may be helpful to elucidate the roles of HaCDAs in the action of Bt cry toxin. The potential of HaCDAs to be used as synergists of Bt insecticidal protein needs to be further tested.