您好，欢迎访问中国农业科学院 机构知识库！

全部

  • 全部
  • 标题
  • 学者
  • 机构
  • 关键词

Characterization and functional analysis of the small heat shock protein HSP19.5 in Bombyx mori in response to Nosema bombycis infection

文献类型： 外文期刊

作者： Han, Zhenghao 1 ; Jiang, Shidong 2 ; Xie, Jingxian 1 ; Poupina, Ibouanga Sama Lucreche 1 ; Mo, Xiaoli 1 ; Sui, Li 1 ; Qian, Ping 1 ; Tang, Xudong 1 ;

作者机构： 1.Jiangsu Univ Sci & Technol, Sch Biotechnol, Jiangsu Key Lab Sericultural & Anim Biotechnol, Zhenjiang 212100, Peoples R China

2.Guangxi Key Lab Sericultural Genet Improvement & E, Nanning 530007, Peoples R China

3.Guangxi Zhuang Autonomous Reg Sericulture Technol, Nanning 530007, Peoples R China

4.Chinese Acad Agr Sci, Sericultural Sci Res Ctr, Key Lab Silkworm & Mulberry Genet Improvement, Minist Agr & Rural Affairs, Zhenjiang 212100, Peoples R China

5.Zhenjiang Zhongnong Biotechnol Co Ltd, Zhenjiang 212101, Peoples R China

关键词： Small heat shock proteins; Bombyx mori; Nosema bombycis; Apoptosis; Host-pathogen interaction

期刊名称：JOURNAL OF INVERTEBRATE PATHOLOGY （ 影响因子：2.4； 五年影响因子：3.0 ）

ISSN： 0022-2011

年卷期： 2025 年 210 卷

页码：

收录情况： SCI

摘要： Small heat shock proteins (sHSPs) are molecular chaperones known for their role in maintaining cellular homeostasis and protecting cells from various environmental stresses. This study focuses on the silkworm small heat shock protein HSP19.5 and its potential functions in the context of Nosema bombycis infection, a microsporidian pathogen causing severe disease in the sericulture industry. We cloned and characterized HSP19.5 and revealed its expression patterns in different silkworm tissues and developmental stages. Our results indicate that HSP19.5 expression is significantly up-regulated in response to N. bombycis infection, suggesting a role in the host stress response. Through a series of experiments, including RNA interference and overexpression analyses, we demonstrated that HSP19.5 promotes N. bombycis proliferation, possibly by inhibiting host cell apoptosis and regulating intracellular ROS levels. The cytoplasmic localization of HSP19.5 in silkworm cells is consistent with its function as a molecular chaperone. The results enhance our understanding of the complex host-pathogen interactions between silkworms and N. bombycis, and provides insights that may inform the development of novel strategies to control the pebrine disease.

  • 相关文献
作者其他论文 更多>>
置顶
购物车
反馈

© 京ICP备09089781号-29 主办单位：中国农业科学院

学术资源： 中国农业科学院 农业专业知识服务系统 农科联盟资源共建共享平台 中国农业科技文献与信息服务平台 中国农业期刊集成服务平台