CLONING, EXPRESSION, AND CHARACTERIZATION OF PROPHENOLOXIDASE FROM Antheraea pernyi. Issue 1 (January 2015)

• Record Type: Journal Article
• Authors: Lu, Wang Xia; Yue, Du; Hai, Zhang Jing; Daihua, Wen; Yi, Zhao Ming; Fu, Wu Chun; Rong, Zhang; Luel Lee, Bok; Kawabata, Shun‐Ichiro; Wang, Chengshu
• Is Part Of: Archives of insect biochemistry and physiology. Volume 88:Issue 1(2015:Jan.)
• Page Start: 45
• Page End: 63
• Publication Date: 2015-01
• Subjects: Insects -- Physiology -- Periodicals; Insect biochemistry -- Periodicals; 595.701572
• DOI: 10.1002/arch.21219
• Languages: English
• ISSNs: 0739-4462

Abstract

<abstract abstract-type="main"> <title> <x xml:space="preserve">Abstract</x> </title> <p>Prophenoloxidase (PPO) is an essential enzyme in insect innate immunity because of its role in humoral defense. In this study, we have cloned a full‐length cDNA of <italic>Antheraea pernyi</italic> prophenoloxidase (ApPPO) with an open‐reading frame encoding 683 amino acids, and the deduced amino acid sequence of ApPPO exhibited a high similarity with those of lepidoptera. The expression of ApPPO was inducible so that the mRNA level was significantly upregulated in the microbial challenged tissues, including fat body, hemocytes, and midgut. To better investigate the enzymatic and immunological properties of ApPPO, recombinant ApPPO (rApPPO) was produced in <italic>Escherichia coli</italic>. Several functional verification experiments were performed after studying the enzymatic properties. It was found that rApPPO could be stimulated by the microbial challenged larvae hemolymph and then killed bacteria in the radial diffusion assay. Furthermore, rApPPO also induced the transcription of cecropins after injected into the larvae 24 h later.</p> </abstract>