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Cloning and functional expression of a chitinase cDNA from the apple leaf miner moth Lithocolletis ringoniella.

Authors
  • Fan, Xiao-Jun
  • Mi, Yan-Xia
  • Ren, Hui
  • Zhang, Chang
  • Li, Yao
  • Xian, Xiao-Xiao
Type
Published Article
Journal
Biochemistry (Moscow)
Publisher
Pleiades Publishing
Publication Date
Feb 01, 2015
Volume
80
Issue
2
Pages
242–250
Identifiers
DOI: 10.1134/S000629791502011X
PMID: 25756539
Source
Medline
License
Unknown

Abstract

Insect chitinase plays essential roles in chitin catabolism involved in digestion and molting during insect development. In the current work, we cloned a chitinase cDNA, LrCht5, from the apple leaf miner moth Lithocolletis ringoniella and characterized its amino acid sequence and protein properties. The L. ringoniella chitinase cDNA was 2136 bp in length with an open reading frame of 1737 bp that encodes a polypeptide of 579 amino acid residues with a predicted molecular mass of 64.4 kDa and pI of 5.49. The catalytic domain has several phosphorylation and glycosylation sites. The recombinant LrCht5 was expressed in Escherichia coli and the Spodoptera frugiperda cell line Sf9, and the LrCht5 expressed in insect cells exhibited chitinolytic activity. LrCht5 was most stable at pH 6.0 and 45°C. This work has potential application in the development of novel and more specific synthetic chitinase inhibitors for use as bioinsecticides.

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