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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 Antheraea pernyi 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 Escherichia coli. 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., (© 2014 Wiley Periodicals, Inc.)

A class of modular oxazolines and their derivatives 1-5 were synthesized with moderate to excellent yields using a simple one-pot method; 4 x 3 bis-oxazolines were obtained, as expected, from each of the three reactions of 1,4-dicyanobenzene, 1,3-dicyanobenzene, and 1,2-dicyanobenzene with optically active amino alcohols in chlorobenzene under dry, anaerobic conditions. ZnCl(2) was used as a Lewis acid catalyst. Direct condensation of 1, 2-bis(cyanomethyl) benzene or 2-cyanophenylacetonitrile did not yield the target products, but two series of novel compounds (4 and 5) were isolated and their structures were confirmed by X-Ray analysis. All products (1-5) were characterized by NMR, IR, and MS.