Journal
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
Volume 67, Issue 11, Pages 3168-3178Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.jafc.8b06909
Keywords
Serratia marcescens; secretory alkaline metalloprotease; Tobacco mosaic virus; antiviral activity
Funding
- State Tobacco Monopoly Bureau [110201601024(LS-04)]
- Development of Rapid Detection Method for Tobacco Virus [SCYC201804]
- Hunan Tobacco Science Institute [201743010020088]
- Science Foundation for Young Scholars of Tobacco Research Institute of Chinese Academy of Agricultural Sciences [2017A02]
- Jiangxi Institute of Tobacco Leaf Science [201701002]
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In this study we report a secretory protein that was purified from Serratia marcescens strain S3 isolated from soil from the tobacco rhizosphere. Subsequent mass spectrometry and annotation characterized the protein as secretory alkaline metalloprotease (SAMP). SAMP plays a crucial role in inhibiting Tobacco mosaic virus (TMV). Transmission electron microscopy (TEM), dynamic light scattering (DLS), confocal microscopy, and microscale thermophoresis (MST) were employed to investigate the anti-TMV mechanism of SAMP. Our results demonstrated that SAMP, as a hydrolytic metal protease, combined and hydrolyzed TMV coat proteins to destroy the virus particles. This study is the first to investigate the antiviral effects of a S. marcescens metalloprotease, and our finding suggests that S. marcescens-S3 may be agronomically useful as a disease-controlling factor active against Tobacco mosaic virus.
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