Isolation of ferritin and its interaction with BmNPV in the silkworm, Bombyx mori
Isolation of ferritin and its interaction with BmNPV in the silkworm, Bombyx mori
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家蚕中铁蛋白的分离及其与 BmNPV 的相互作用
DOI：
10.1016/j.dci.2018.05.012
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发表时间：
2018-09-01
影响因子：
2.9
通讯作者：
Shahzad, Toufeeq
中科院分区：
文献类型：
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作者：
Fei, Dong-qiong;Yu, Hai-zhong;Shahzad, Toufeeq
铁蛋白是一种普遍存在的铁储存蛋白，在宿主防御病原体感染中起重要作用。采用非变性聚丙烯酰胺凝胶电泳（native-PAGE）和十二烷基硫酸钠-聚丙烯酰胺凝胶电泳（SDS-PAGE）从家蚕血淋巴中分离出非变性铁蛋白。结果表明，铁蛋白由两个亚基组成，命名为BmFerHCH和BmFerLCH。先前整合的转录组和iTRAQ数据显示，BmNPV感染后，这两个亚基在抗性家蚕品系BC 9中表达下调，而在敏感家蚕品系P50中表达水平没有明显变化。病毒覆盖试验显示B.以杂聚体形式存在的桑铁蛋白与B有相互作用。家蚕核型多角体病毒（BmNPV）的蛋白质，但解聚后不能与BmNPV相互作用。反转录定量PCR（RTqPCR）分析表明，BmFerHCH和BmFerLCH可以被细菌、病毒和铁诱导产生。这是第一个提取B的研究。并证实了它们在BmNPV感染过程中的作用。这些结果为进一步研究B的功能奠定了基础。桑铁蛋白
Ferritin is a ubiquitous iron storage protein that plays an important role in host defence against pathogen infections. In the present study, native ferritin was isolated from the hemolymph of Bombyx mori using native-polyacrylamide gel electrophoresis (native-PAGE) and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The results revealed that ferritin consisted of two subunits, designated as BmFerHCH and BmFerLCH. Previously integrated previous transcriptome and iTRAQ data showed that the two subunits were down-regulated in resistant silkworm strain BC9 and there was no obvious change in the expression levels of the subunits in susceptible silkworm strain P50 after BmNPV infection. Virus overlay assays revealed that B. mori ferritin as the form of heteropolymer had an interaction with B. mori nucleopolyhedrovirus (BmNPV), but it can't interact with BmNPV after depolymerisation. What's more, reverse transcription quantitative PCR (RTqPCR) analysis suggested that BmFerHCH and BmFerLCH could be induced by bacteria, virus and iron. This is the first study to extract B. mori ferritin successfully and confirms their roles in the process of BmNPV infection. All these results will lay a foundation for further research the function of B. mori ferritin.