Identification of multiple ferritin genes in Macrobrachium nipponense and their involvement in redox homeostasis and innate immunity.
Identification of multiple ferritin genes in Macrobrachium nipponense and their involvement in redox homeostasis and innate immunity.
复制标题
日本沼虾中多个铁蛋白基因的鉴定及其与氧化还原稳态和先天免疫的关系。
DOI:
10.1016/j.fsi.2019.04.050
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发表时间:
2019
期刊:
影响因子:
--
通讯作者:
Liu Fengsong
中科院分区:
文献类型:
--
作者:
Tang Ting;Yang Zilan;Li Jing;Yuan Fengyu;Xie Song;Liu Fengsong
Based on the transcriptome database, we screened out four ferritin subunit genes (MnFer2-5) from the oriental river prawn Macrobrachium nipponense, which encode two non-secretory and two secretory peptides. MnFer2 and 4 possess a strictly conserved ferroxidase site, and MnFer3 has a non-typical ferroxidase site. MnFer5 seems to be a number of ferritin families, which has a distinct dinuclear metal binding motif, but lacks an iron ion channel, a ferroxidase site and a nucleation site. Diverse tissue-specific transcriptions of the four genes indicate their functional diversity in the prawn. Among them, MnFer2 is mainly expressed in hepatopancreas and intestines, MnFer3 and 4 are predominantly expressed in gills, and MnFer5 is widely expressed in various tissues with high presence in intestines, hepatopancreas and haemocytes. The transcription of all the four MnFer genes can be strongly induced by doxorubicin, indicating the involvement of these ferritin subunits in protection from oxidative stress. Upon Aeromonas hydrophila infection, only MnFer5 is persistently up-regulated, while other subunits including MnFer2-4 are down-regulated during the early stage, followed by recovery and even a slight increase at 48 h post bacterial challenge. Moreover, the iron binding capacity of recombinant MnFer2 is also demonstrated in vitro. TheE. coliexpressing MnFer2 displays increased resistance to hydrogen peroxidase cytotoxicity. These results suggest a protective role of ferritins fromM. nipponensein iron homeostasis, redox biology and antibacterial immunity and shed light on the molecule evolution of crustacean ferritin subunits.