Identification of putative binding interface of PI(3,5)P-2 lipid on rice black-streaked dwarf virus (RBSDV) P10 protein
文献类型： 外文期刊
作者： Liu, Haoqiu 1 ; Peck, Xin Yi 1 ; Choong, Yeu Khai 2 ; Ng, Woei Shyuan 4 ; Engl, Wilfried 4 ; Raghuvamsi, Palur Venkata 2 ; Zhao, Ziqing Winston 4 ; Anand, Ganesh S. 2 ; Zhou, Yijun 1 ; Sivaraman, J. 2 ; Xu, Qiufang 1 ; Wong, Sek-Man 2 ;
作者机构： 1.Jiangsu Acad Agr Sci, Inst Plant Protect, Key Lab Food Qual & Safety Jiangsu Prov, State Key Lab Breeding Base, Nanjing 210014, Jiangsu, Peoples R China
2.Natl Univ Singapore, Dept Biol Sci, Fac Sci, Singapore 119543, Singapore
3.Natl Univ Singapore, Res Inst, Suzhou 215123, Jiangsu, Peoples R China
4.Natl Univ Singapore, Dept Chem, Fac Sci, Singapore 119543, Singapore
5.Natl Univ Singapore, Ctr BioImaging Sci CBIS, Fac Sci, Singapore 117557, Singapore
6.Natl Univ Singapore, Mech Inst MBI, Singapore 117411, Singapore
7.Penn State Univ, Eberly Coll Sci, Dept Chem, State Coll, PA 16802 USA
8.Temasek Life Sci Lab, Singapore 117604, Singapore
关键词： Lipid binding; Viral protein; Phosphatidylinositol phosphates; STORM; AlphaFold; HDXMS
期刊名称：VIROLOGY （ 影响因子：3.7； 五年影响因子：3.2 ）
ISSN： 0042-6822
年卷期： 2022 年 570 卷
页码：
收录情况： SCI
摘要： Rice black-streaked dwarf virus (RBSDV) is an important reovirus that infects both plants and its transmission vector small brown planthopper, causing severe crop loss. High affinity binding between RBSDV P10 and PI(3,5) P-2 lipid layer was measured using biolayer interferometry (BLI). Subcellular co-localization of PI(3,5)P-2 and RBSDV P10 was observed on membranous structures in insect cells with stochastic optical reconstruction microscopy (STORM) imaging. Putative interacting sites of PI(3,5)P-2 lipid on a computational predicted RBSDV P10 structure were mapped to its "C-domain" (250-470 aa), using HDXMS data. The BLI and STORM results showed binding and co-localization of RBSDV P10, and PI(3,5)P-2 on vesicle-like membranous structures were corroborated with the prediction of the binding interface. Understanding the lipid binding sites on viral proteins will lead to developing strategies to block viral-lipid interaction and disrupt viral pathogenesis in insect vectors and to block virus transmission and achieve disease control of crops in the field.
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