4.5 Article

Molecular cloning, characterization and expression analysis of cathepsin O in silkworm Bombyx mori related to bacterial response

Journal

MOLECULAR IMMUNOLOGY
Volume 66, Issue 2, Pages 409-417

Publisher

PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.molimm.2015.04.008

Keywords

Silkworm; Molecular cloning; Cathepsin O; 20-Ecdysone; Infection

Funding

  1. National Basic Research Program of China [2012cb114603]
  2. Research Fund for the Doctoral Program of Higher Education of China [20130182110003]
  3. Natural Science Foundation of Chongqing [cstc2013jcyjys0007]
  4. Fundamental Research Funds for the Central Universities [XDJK2015D021, XDJK2013B020, SWU111014]

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Cathepsins are the main members of the cysteine family and play important roles in immune response in vertebrates. The Cathepsin O of Bombyx mori (BmCathepsin O) was cloned from the hemocytes by the rapid amplification of cDNA ends (RACE). The genomic DNA was 6131 bp long with a total of six exons and five introns. Its pre-mRNA was spliced to generate two spliceosomes. By comparisons with other reported cathepsins O, it was concluded that the identity between them ranged from 29 to 39%. Expression analysis indicated that BmCathepsin O was specific-expressed in hemocytes, and highly expressed at the 4th molting and metamorphosis stages. Immunofluorescence assay and qRT-PCR showed that BmCathepsin O was expressed in granulocytes and plasmatocytes. Interestingly, BmCathepsin O was significantly upregulated after stimulated by 20-hydroxyecdysone (20-E) in vivo, which suggested that BmCathepsin O may be regulated by 20E. Moreover, activation of BmCathepsin O was also observed in hemocytes challenged by Escherichia coli, indicating its potential involvement in the innate immune system of silkworm, B. mori. In summary, our studies provide a new insight into the functional features of Cathepsin O. (C) 2015 Elsevier Ltd. All rights reserved.

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