The Tobamovirus helicase plays an important role in virus proliferation and host interaction. They can also be targets for antiviral drugs. Tobacco mosaic virus (TMV) is well controlled by ningnanmycin (NNM), but whether it acts on other virus helicases of Tobamovirus virus is not clear. In this study, we expressed and purified several Tobamovirus virus helicase proteins and analyzed the three-dimensional structures of several Tobamovirus virus helicases. In addition, the binding of Tobamovirus helicase to NNM was also studied. The docking study reveals the interaction between NNM and Tobamovirus virus helicase. Microscale Thermophoresis (MST) experiments have shown that NNM binds to Tobamovirus helicase with a dissociation constant of 4.64-12.63 μM. Therefore, these data are of great significance for the design and synthesis of new effective anti-plant virus drugs.
Keywords: Binding studies; Docking studies; NNM; Protein purified; Tobamovirus helicase.
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