Abstract
// Yan Ding 1 , Xiangyang Li 1 , Kai Chen 1 , Guoping Zhang 1 , Liangzhi Luo 1 , Deyu Hu 1 and Baoan Song 1 1 State Key Laboratory Breeding Base of Green Pesticide and Agricultural Bioengineering, Key Laboratory of Green Pesticide and Agricultural Bioengineering, Ministry of Education, Guizhou University, Huaxi District, Guiyang 550025, PR China Correspondence to: Baoan Song, email: basong@gzu.edu.cn Xiangyang Li, email: xyli1@gzu.edu.cn Keywords: targets; SRBSDV P9-1; octamers; bind to; α-amino phosphonate derivatives Received: October 17, 2017 Accepted: December 05, 2017 Published: January 13, 2018 ABSTRACT Southern rice black-streaked dwarf virus (SRBSDV) P9-1 octameric protein accumulates viroplasms in SRBSDV-infected plant and insect cells, our previous studies found α-amino phosphonate drug—dufulin had a micromole affinity with SRBSDV P9-1. Now we focus our studies on the SRBSDV P9-1 crystal structure and use it as the target for α-amino phosphonate derivatives. The structure of the SRBSDV P9-1 cylindrical octamer was determined to a 2.2 Å resolution using X-ray crystallography, this structure was composed of nine α-helices, nine β -sheets and a series of interconnecting loops. The structures of all eight subunits were nearly identical, except for some differences in the β -sheet core. There were six different sites (R20K, V109D, F164T, V123L, C124L and V128T) present between the SRBSDV P9-1 and the previously reported RBSDV P9-1 crystal structure. Fluorescence titration, isothermal calorimetry and microscale thermophoresis experiments showed that α-amino phosphonate derivatives GUFCC-013 and GUFCC-023 bound to SRBSDV P9-1 with micromole binding affinities. These results will provide important help for the further improvement of the lead compound and develop the potential anti-SRBSDV drugs.
Highlights
The formation of viroplasms (Vps) is a feature of the genus fijivirus
The GST-tagged was cut overnight at 4°C by prescission protease, and the dealt proteins were loaded in size exclusion chromatography (SEC) column, in a buffer containing 10 mM Tris-HCl and 100 mM sodium chloride pH 7.5, the retention time of the Southern rice black-streaked dwarf virus (SRBSDV) P9-1 protein was determined with octameric formation (Supplementary Figure 1) [31]
In the crystal structure of SRBSDV P9-1 determined in the present study, 16 main interactions among subunits form an octamer
Summary
The formation of viroplasms (Vps) is a feature of the genus fijivirus. This formation is intrinsic to viral particle functioning in virus-infected plants and insect cells [1,2,3]. Southern rice black-streaked dwarf virus (SRBSDV), a newly discovered member of the genus fijivirus [4, 5], causes the devastating southern rice black-streaked dwarf and maize rough dwarf diseases in crops, which lead to severe yield losses in crops in China and Southeast Asia [6, 7]. The virus is transmitted by an insect vector, the white-backed planthopper sogatella furcifera (Hemiptera: delphacidae) [8]. The genomic segment of SRBSDV is similar to rice black-streaked dwarf virus (RBSDV) and Mal de Río Cuarto virus (MRCV) [9,10,11].
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