Research Papers:

Ningnanmycin inhibits tobacco mosaic virus virulence by binding directly to its coat protein discs

Xiangyang Li, Gefei Hao, Qingmin Wang, Zhuo Chen _, Yan Ding, Lu Yu, Deyu Hu and Baoan Song

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Oncotarget. 2017; 8:82446-82458. https://doi.org/10.18632/oncotarget.19401

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Xiangyang Li1, Gefei Hao2, Qingmin Wang3, Zhuo Chen1, Yan Ding1, Lu Yu1, Deyu Hu1 and Baoan Song1

1State Key Laboratory Breeding Base of Green Pesticide and Agricultural Bioengineering, Key Laboratory of Green Pesticide and Agricultural Bioengineering, Ministry of Education, Guizhou University, Guiyang 550025, P. R. China

2Key Laboratory of Pesticide and Chemical Biology of Ministry of Education, College of Chemistry, Central China Normal University, Wuhan 430079, P. R. China

3State Key Laboratory of Elemento-Organic Chemistry, Nankai University, Tianjin 300071, P. R. China

Correspondence to:

Zhuo Chen, email: [email protected]

Baoan Song, email: [email protected]

Keywords: ningnanmycin, TMV CP, binding analysis, interaction studies

Received: April 26, 2017    Accepted: June 29, 2017    Published: July 19, 2017


Tobacco mosaic virus (TMV) causes severe plant diseases worldwide; however, effective antiviral agents for controlling TMV infections are not available. This lack of effective antiviral agents is mainly due to the poor understanding of potential targets associated with TMV infections. During infection, the coat protein (CP), which is delivered by viral particles into susceptible host cells, provides protection for viral RNA. Here, we found that Ningnanmycin (NNM), a commercially used plant antibacterial agent, inhibits the assembly of the CP by directly binding several residues. These interactions cause the disassembly of the CP from discs into monomers, leading to an almost complete loss of pathogenicity. Substitutions in the involved binding residues resulted in mutants that were significantly less sensitive to NNM. Thus, targeting the binding of viral CPs through small molecular agents offers an effective strategy to study the mechanism of NNM.

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