Interaction and Assembly of Two Novel Proteins in the Spore Wall of the Microsporidian Species Nosema bombycis and Their Roles in Adherence to and Infection of Host Cells
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- 英文论文题名：Interaction and Assembly of Two Novel Proteins in the Spore Wall of the Microsporidian Species Nosema bombycis and Their Roles in Adherence to and Infection of Host Cells
- 论文作者：杨东林 ; Guoqing Pan ; Xiaoqun Dang ; Yawei Shi ; Chunfeng Li ; Pai Peng ; Bo Luo ; Maofei Biana ; Yue Song ; Cheng Ma ; Jie Chen ; Zhengang Ma ; Lina Geng ; Zhi Li ; Rui Tian ; Cuifang Wei ; 周泽扬
- 英文论文作者：Donglin Yang ; Guoqing Pan ; Xiaoqun Dang ; Yawei Shi ; Chunfeng Li ; Pai Peng ; Bo Luo ; Maofei Biana ; Yue Song ; Cheng Ma ; Jie Chen ; Zhengang Ma ; Lina Geng ; Zhi Li ; Rui Tian ; Cuifang Wei ; Zeyang Zhou ; State Key Laboratory of Silkworm Genome Biology ; Southwest University ; Institute of Biotechnology ; Key Laboratory of Chemical Biology and Molecular Engineering of Ministry of Education ; Shanxi University ; Key Laboratory for Sericulture Functional Genomics and Biotechnology of Agricultural Ministry ; Southwest University ; College of Life Sciences ; Chongqing Normal University ; Chongqing Three Gorges Medical College ; Chongqing Tobacco Science Research Institute ; Southwest University
- 年：2016
- 作者机构：State Key Laboratory of Silkworm Genome Biology, Southwest University;Institute of Biotechnology, Key Laboratory of Chemical Biology and Molecular Engineering of Ministry of Education, Shanxi University;Key Laboratory for Sericulture Functional Genomics and Biotechnology of Agricultural Ministry, Southwest University;College of Life Sciences, Chongqing Normal University;Chongqing Three Gorges Medical College;Chongqing Tobacco Science Research Institute, Southwest University;
- 会议召开时间：2016-07-01
- 会议录名称：第十二届家（柞）蚕遗传育种暨良种繁育学术研讨会论文集（摘要汇编）
- 语种：英文
- 分类号：S884.21
- 学会代码：ZGCU
- 会议名称：第十二届家（柞）蚕遗传育种暨良种繁育学术研讨会
- 会议地点：中国重庆
- 主办单位：中国蚕学会、国家蚕桑产业技术体系
- 学会名称：中国蚕学会
- 页数：1
- 文件大小：500k
- 原文格式：D
- 会议级别：全国
摘要
Microsporidia are obligate intracellular parasites with rigid spore walls that protect against various environmental pressures. Despite an extensive description of the spore wall, little is known regarding the mechanism by which it is deposited or the role it plays in cell adhesion and infection. In this study, we report the identification and characterization of two novel spore wall proteins, SWP7 and SWP9, in the microsporidian species Nosema bombycis. SWP7 and SWP9 are mainly localized to the exospore and endospore of mature spores and the cytoplasm of sporonts, respectively. In addition, a portion of SWP9 is targeted to the spore wall of sporoblasts earlier than SWP7 is. Both SWP7 and SWP9 are specifically colocalized to the spore wall in mature spores. Furthermore, immunoprecipitation, far-Western blotting, unreduced SDS-PAGE, and yeast two-hybrid data demonstrated that SWP7 interacted with SWP9. The chitin binding assay showed that, within the total spore protein, SWP9 and SWP7 can bind to the deproteinated chitin spore coats(DCSCs) of N. bombycis. However, binding of the recombinant protein r SWP7-His to the DCSCs is dependent on the combination of r SWP9–glutathione S-transferase(GST) with the DCSCs. Finally, r SWP9-GST, anti-SWP9, and anti-SWP7 antibodies decreased spore adhesion and infection of the host cell. In conclusion, SWP7 and SWP9 may have important structural capacities and play significant roles in modulating host cell adherence and infection in vitro. A possible major function of SWP9 is as a scaffolding protein that supports other proteins(such as SWP7) that form the integrated spore wall of N. bombycis.
Microsporidia are obligate intracellular parasites with rigid spore walls that protect against various environmental pressures. Despite an extensive description of the spore wall, little is known regarding the mechanism by which it is deposited or the role it plays in cell adhesion and infection. In this study, we report the identification and characterization of two novel spore wall proteins, SWP7 and SWP9, in the microsporidian species Nosema bombycis. SWP7 and SWP9 are mainly localized to the exospore and endospore of mature spores and the cytoplasm of sporonts, respectively. In addition, a portion of SWP9 is targeted to the spore wall of sporoblasts earlier than SWP7 is. Both SWP7 and SWP9 are specifically colocalized to the spore wall in mature spores. Furthermore, immunoprecipitation, far-Western blotting, unreduced SDS-PAGE, and yeast two-hybrid data demonstrated that SWP7 interacted with SWP9. The chitin binding assay showed that, within the total spore protein, SWP9 and SWP7 can bind to the deproteinated chitin spore coats(DCSCs) of N. bombycis. However, binding of the recombinant protein r SWP7-His to the DCSCs is dependent on the combination of r SWP9–glutathione S-transferase(GST) with the DCSCs. Finally, r SWP9-GST, anti-SWP9, and anti-SWP7 antibodies decreased spore adhesion and infection of the host cell. In conclusion, SWP7 and SWP9 may have important structural capacities and play significant roles in modulating host cell adherence and infection in vitro. A possible major function of SWP9 is as a scaffolding protein that supports other proteins(such as SWP7) that form the integrated spore wall of N. bombycis.
Microsporidia are obligate intracellular parasites with rigid spore walls that protect against various environmental pressures. Despite an extensive description of the spore wall, little is known regarding the mechanism by which it is deposited or the role it plays in cell adhesion and infection. In this study, we report the identification and characterization of two novel spore wall proteins, SWP7 and SWP9, in the microsporidian species Nosema bombycis. SWP7 and SWP9 are mainly localized to the exospore and endospore of mature spores and the cytoplasm of sporonts, respectively. In addition, a portion of SWP9 is targeted to the spore wall of sporoblasts earlier than SWP7 is. Both SWP7 and SWP9 are specifically colocalized to the spore wall in mature spores. Furthermore, immunoprecipitation, far-Western blotting, unreduced SDS-PAGE, and yeast two-hybrid data demonstrated that SWP7 interacted with SWP9. The chitin binding assay showed that, within the total spore protein, SWP9 and SWP7 can bind to the deproteinated chitin spore coats(DCSCs) of N. bombycis. However, binding of the recombinant protein r SWP7-His to the DCSCs is dependent on the combination of r SWP9–glutathione S-transferase(GST) with the DCSCs. Finally, r SWP9-GST, anti-SWP9, and anti-SWP7 antibodies decreased spore adhesion and infection of the host cell. In conclusion, SWP7 and SWP9 may have important structural capacities and play significant roles in modulating host cell adherence and infection in vitro. A possible major function of SWP9 is as a scaffolding protein that supports other proteins(such as SWP7) that form the integrated spore wall of N. bombycis.
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