Purification and Characterization of a Secretory Alkaline Metalloprotease with Highly Potent Antiviral Activity from Serratia marcescens Strain S3
journal contributionposted on 25.02.2019, 00:00 by Yuanxia Qin, Jie Wang, Fenglong Wang, Lili Shen, Haixiang Zhou, Hangjun Sun, Kaiqiang Hao, Liyun Song, Zhicheng Zhou, Chaoqun Zhang, Yuanhua Wu, Jinguang Yang
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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Serratia marcescens strain S 3hydrolytic metal proteaseMSTTMV coat proteinsdisease-controlling factorvirus particlesTEMsecretory proteinS 3marcescens metalloproteaseDLSanti-TMV mechanismSerratia marcescens Strain S 3SAMPTobacco mosaic virusmicroscale thermophoresisSubsequent mass spectrometryPotent Antiviral ActivitySecretory Alkaline MetalloproteaseTransmission electron microscopytobacco rhizosphere