Identification and characterization of a prophenoloxidase‐1 (PPO1) cDNA in the cabbage butterfly Pieris rapae L
Phenoloxidase (PO) is a melanin‐synthesizing enzyme widely distributed in animals, plants and microorganisms. It plays an important role in insect immune response. Here we report the cloning of a prophenoloxidase (PPO) cDNA from Pieris rapae, prophenoloxidase‐1 (PrPPO1). The full‐length cDNA consist...
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Published in | Entomological science Vol. 18; no. 1; pp. 94 - 103 |
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Main Authors | , , , , , |
Format | Journal Article |
Language | English |
Published |
Blackwell Pub
2015
Blackwell Publishing Ltd |
Subjects | |
Online Access | Get full text |
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Summary: | Phenoloxidase (PO) is a melanin‐synthesizing enzyme widely distributed in animals, plants and microorganisms. It plays an important role in insect immune response. Here we report the cloning of a prophenoloxidase (PPO) cDNA from Pieris rapae, prophenoloxidase‐1 (PrPPO1). The full‐length cDNA consisted of 3338 bp, containing an open reading frame of 2049 bp encoding 682 amino acid (aa) residues. Two putative copper‐binding sites, a proteolytic activation site, three conserved hemocyanin domains and a thiolester motif, but no signal sequence, were found in the deduced aa sequence. A BLASTp search and neighbor‐joining analysis showed the deduced aa sequence had high identity to the published sequence of PPO1 from other lepidopteran insects, ranging from 71.31 to 73.15%. The results of real‐time polymerase chain reaction (PCR) showed that the highest expression of PrPPO1 was in the 4th instar larvae and the highest density of oenocytoids was observed in the 4th instar larvae also. PrPPO1 transcripts in the 4th instar larvae were significantly decreased at 6 h and 12 h with Beauveria bassiana infection; however, they were sharply increased at 72 h. PrPPO1 transcriptional level in the 5th instar larvae showed no significant changes compared with the control at 4 h with quercetin injection; however it was significantly increased at 12 h. The expression level of PrPPO1 was mainly related to the treatment time of the quercetin, but not the dose. |
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Bibliography: | http://dx.doi.org/10.1111/ens.12094 istex:4B1B1F152DDA5DB858FDED60F3971249FFC0CBD7 Figure S1 Nucleotide and deduced amino acid sequence of P. rapae PPO1. Figure S2 Multiple sequence alignment of the two copper binding sites (CuA and CuB) regions of arthropod PPOs. Expert National Ministry of Education Foundation of China - No. 20103702120006 ark:/67375/WNG-WCJFT0QQ-X National Natural Science Foundation of China - No. 31301730 Shandong Excellent Young Scientist Awarded Foundation - No. BS2010NY016 ArticleID:ENS12094 ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 1343-8786 1479-8298 |
DOI: | 10.1111/ens.12094 |