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Identification and functional analysis of an iron‐binding protein, ferritin heavy chain subunit, from the swallowtail butterfly, Papilio xuthus
Author(s) -
Lu ZhanJun,
Xie YanXin,
Yu HaiZhong,
Toufeeq Shahzad,
Wang Jie,
Huang YuLing,
Li NingYan,
Ouyang ZhiGang
Publication year - 2019
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.21592
Subject(s) - biology , ferritin , manduca sexta , protein subunit , biochemistry , hemolymph , recombinant dna , escherichia coli , gene , insect , botany
Ferritin, which is ubiquitous among all living organisms, plays a crucial role in maintaining iron homeostasis, immune response, and detoxification. In the present research, we identified an iron‐binding protein, ferritin heavy chain subunit, from Papilio xuthus and named PxFerHCH. The complete complementary DNA of PxFerHCH was 1,252 bp encoding a sequence of 211 amino acids, which includes an iron‐responsive element. Phylogenetic analysis showed that PxFerHCH is clustered with Manduca sexta and Galleria mellonella ferritin heavy chain subunits. Expression levels of PxFerHCH in various tissues were analyzed by reverse transcription quantitative polymerase chain reaction, and the results exhibited that PxFerHCH was expressed in all tissues with the highest expression in the fat body. The relative expression level of PxFerHCH in response to bacterial ( Escherichia coli and Staphylococcus aureus ) challenges sharply increased by about 12 hr postinfection (hpi) and then decreased at 24 hpi. In addition, the iron‐binding capacity and antioxidation activity of recombinant PxFerHCH protein were also investigated. These results reveal that PxFerHCH might play an important role in defense against bacterial infection.