粘质沙雷氏菌
烟草花叶病毒
微尺度热泳
金属蛋白酶
化学
蛋白酶
微生物学
生物化学
酶
生物
病毒
病毒学
大肠杆菌
基因
作者
Yuanxia Qin,Jie Wang,Fenglong Wang,Lili Song,Haixiang Zhou,Hangjun Sun,Kaiqiang Hao,Liyun Song,Zhi Zhou,Chaoqun Zhang,Yuanhua Wu,Jinguang Yang
标识
DOI:10.1021/acs.jafc.8b06909
摘要
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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