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The role of Bombyx mori Bmtutl-519 protein in the infection of BmN cells by Nosema bombycis

文献类型： 外文期刊

作者： Zhu, Feng 1 ; Tang, Xudong 2 ; Xiao, Shengyan 1 ; Wang, Hongliang 4 ; Zhang, Yonghong 1 ; Shao, Yulan 1 ; Tang, Fenfen 1 ;

作者机构： 1.Yunnan Acad Agr Sci, Inst Sericulture & Apiculture, Mengzi 661101, Yunnan, Peoples R China

2.Jiangsu Univ Sci & Techno, Zhenjiang 212018, Jiangsu, Peoples R China

3.Chinese Acad Agr Sci, Sericultural Res Inst, Zhenjiang 212018, Jiangsu, Peoples R China

4.Tengzhou 1 Middle Sch Shangdong Prov, Zhenjian 212018, Jiangsu, Peoples R China

关键词： Silkworm; Nosema bombycis; Bmtud-519; NbSWP26; Heparin-binding motif (HBM)

期刊名称：DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY （ 影响因子：3.636； 五年影响因子：3.654 ）

ISSN： 0145-305X

年卷期： 2019 年 92 卷

页码：

收录情况： SCI

摘要： Bmtutl-519 is an isoform of the Bombyx Turtle protein and a member of the immunoglobulin superfamily (IgSF). The relative expression level of Brand-519 was significantly upregulated when BmN cells were infected by Nosema bombycis. The subcellular localization of Bmtutl-519 was studied using an indirect immunoinfluscent assay (IFA), Co-localization assay, Western blotting, and enhanced green fluorescent protein (EGFP) fusion constructs expressed in BmN cells transfected with a Smtut1-519 expression plasmid. The results indicate that Bmtutl-519 is distributed in both the cytoplasm and the cell membrane of BmN cells. Bmtutl-519 may be involved in the infection process of N. bombycis as a cell surface receptor or regulatory factor. Interaction analysis of Bmtutl-519 with NbSWP26, a spore wall protein of N. bombycis involved in host cell adherence and infection, showed that the C-terminal heparin-binding motif (HBM) of NbSWP26 mediates the interaction between these two proteins. Mutation of the NbSWP26 HBM at K208G, K209G, K210G, and K213G led to a loss of the ability to bind the Bmtutl-519 protein. Spore adherence and infection assays showed that Bmtutl-519 enhances the binding ability of N. bombycis to the host cell surface, but this did not enhance host cell infection by N. bombycis. In contrast, the sustained high expression of Bmtutl-519 in BmN cells inhibited the proliferation of N. bombycis spores.

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