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A novel hexamerin with an unexpected contribution to the prophenoloxidase activation system of the Chinese oak silkworm, Antheraea pernyi
Author(s) -
Liu Chengbao,
Zhu Jinye,
Ma Jingjing,
Zhang Jinghai,
Wang Xialu,
Zhang Rong
Publication year - 2020
Publication title -
archives of insect biochemistry and physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.576
H-Index - 66
eISSN - 1520-6327
pISSN - 0739-4462
DOI - 10.1002/arch.21648
Subject(s) - prophenoloxidase , antheraea pernyi , hemolymph , biology , storage protein , biochemistry , innate immune system , gene , receptor
Hexamerin was originally identified as a storage protein but later confirmed to be involved in many physiological processes. In the present study, we cloned and characterized a novel hexamerin complementary DNA sequence from the Chinese oak silkworm, Antheraea pernyi ( Ap ‐hexamerin), which shows high homology with reported insect methionine‐rich hexamerins. The tissue distribution and time course of expression demonstrated that Ap ‐hexamerin was predominantly synthesized in the fat body and the expression level was significantly increased in response to the microbial challenge, suggesting the relevance of Ap ‐hexamerin to immune responses. In further immune functional studies, Ap ‐hexamerin was confirmed to take part in the upregulation of prophenoloxidase (PPO) activation in A. pernyi haemolymph triggered by pathogen‐associated molecular patterns (PAMPs). Additional molecular interaction analysis revealed that Ap ‐hexamerin is capable of binding the PAMPs used in the phenoloxidase assay, suggesting hexamerin in A. pernyi may positively regulate haemolymph PPO activation, acting as a pattern recognition protein.