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Serratia marcescens‐S3 inhibits Potato virus Y by activating ubiquitination of molecular chaperone proteins NbHsc70‐2 in Nicotiana benthamiana

The potato virus Y (PVY) is a plant virus that causes massive crop losses globally, especially in Solanaceae crops. A strain of the plant growth‐promoting rhizobacterium (PGPR), Serratia marcescens‐S3 was found to inhibit PVY replication in Nicotiana benthamiana. However, there have been no in‐depth...

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Autores principales: Ge, Ming, Gong, Mingyue, Jiao, Yubing, Li, Ying, Shen, Lili, Li, Bin, Wang, Yujie, Wang, Fenglong, Zhang, Songbai, Yang, Jinguang
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8966008/
https://www.ncbi.nlm.nih.gov/pubmed/34788498
http://dx.doi.org/10.1111/1751-7915.13964
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author Ge, Ming
Gong, Mingyue
Jiao, Yubing
Li, Ying
Shen, Lili
Li, Bin
Wang, Yujie
Wang, Fenglong
Zhang, Songbai
Yang, Jinguang
author_facet Ge, Ming
Gong, Mingyue
Jiao, Yubing
Li, Ying
Shen, Lili
Li, Bin
Wang, Yujie
Wang, Fenglong
Zhang, Songbai
Yang, Jinguang
author_sort Ge, Ming
collection PubMed
description The potato virus Y (PVY) is a plant virus that causes massive crop losses globally, especially in Solanaceae crops. A strain of the plant growth‐promoting rhizobacterium (PGPR), Serratia marcescens‐S3 was found to inhibit PVY replication in Nicotiana benthamiana. However, there have been no in‐depth studies demonstrating the underlying mechanism. In the current study, we found that ubiquitination of NbHsc70‐2 is an important way for Serratia marcescens‐S3 to trigger induced systemic resistance (ISR). After the treatment with S. marcescens‐S3, the protein level of NbHsc70‐2 reduced significantly. Inhibiting of ubiquitination increased the accumulation of NbHsc70‐2 in plants and reduced S. marcescens‐S3‐mediated resistance to PVY. Furthermore, transgenic engineered Nicotiana benthamiana NbHsc70‐2(KO) and NbHsc70‐2(USM) were constructed using CRISPR‐Cas9‐mediated NbHsc70‐2 knock‐out and ubiquitination respectively. S. marcescens‐S3 significantly reduced the inhibition of NbHsc70‐2 protein accumulation in NbHsc70‐2(KO) and NbHsc70‐2(USM) . The virulence of PVY was stronger in NbHsc70‐2(USM) than the wild‐type plants. These results showed that S. marcescens‐S3 increases the ubiquitination of NbHsc70‐2 to inhibit the recruitment of molecular chaperone NbHsc70‐2 to reduce its replication and infection of PVY.
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spelling pubmed-89660082022-04-05 Serratia marcescens‐S3 inhibits Potato virus Y by activating ubiquitination of molecular chaperone proteins NbHsc70‐2 in Nicotiana benthamiana Ge, Ming Gong, Mingyue Jiao, Yubing Li, Ying Shen, Lili Li, Bin Wang, Yujie Wang, Fenglong Zhang, Songbai Yang, Jinguang Microb Biotechnol Research Articles The potato virus Y (PVY) is a plant virus that causes massive crop losses globally, especially in Solanaceae crops. A strain of the plant growth‐promoting rhizobacterium (PGPR), Serratia marcescens‐S3 was found to inhibit PVY replication in Nicotiana benthamiana. However, there have been no in‐depth studies demonstrating the underlying mechanism. In the current study, we found that ubiquitination of NbHsc70‐2 is an important way for Serratia marcescens‐S3 to trigger induced systemic resistance (ISR). After the treatment with S. marcescens‐S3, the protein level of NbHsc70‐2 reduced significantly. Inhibiting of ubiquitination increased the accumulation of NbHsc70‐2 in plants and reduced S. marcescens‐S3‐mediated resistance to PVY. Furthermore, transgenic engineered Nicotiana benthamiana NbHsc70‐2(KO) and NbHsc70‐2(USM) were constructed using CRISPR‐Cas9‐mediated NbHsc70‐2 knock‐out and ubiquitination respectively. S. marcescens‐S3 significantly reduced the inhibition of NbHsc70‐2 protein accumulation in NbHsc70‐2(KO) and NbHsc70‐2(USM) . The virulence of PVY was stronger in NbHsc70‐2(USM) than the wild‐type plants. These results showed that S. marcescens‐S3 increases the ubiquitination of NbHsc70‐2 to inhibit the recruitment of molecular chaperone NbHsc70‐2 to reduce its replication and infection of PVY. John Wiley and Sons Inc. 2021-11-17 /pmc/articles/PMC8966008/ /pubmed/34788498 http://dx.doi.org/10.1111/1751-7915.13964 Text en © 2021 The Authors. Microbial Biotechnology published by Society for Applied Microbiology and John Wiley & Sons Ltd. https://creativecommons.org/licenses/by-nc-nd/4.0/This is an open access article under the terms of the http://creativecommons.org/licenses/by-nc-nd/4.0/ (https://creativecommons.org/licenses/by-nc-nd/4.0/) License, which permits use and distribution in any medium, provided the original work is properly cited, the use is non‐commercial and no modifications or adaptations are made.
spellingShingle Research Articles
Ge, Ming
Gong, Mingyue
Jiao, Yubing
Li, Ying
Shen, Lili
Li, Bin
Wang, Yujie
Wang, Fenglong
Zhang, Songbai
Yang, Jinguang
Serratia marcescens‐S3 inhibits Potato virus Y by activating ubiquitination of molecular chaperone proteins NbHsc70‐2 in Nicotiana benthamiana
title Serratia marcescens‐S3 inhibits Potato virus Y by activating ubiquitination of molecular chaperone proteins NbHsc70‐2 in Nicotiana benthamiana
title_full Serratia marcescens‐S3 inhibits Potato virus Y by activating ubiquitination of molecular chaperone proteins NbHsc70‐2 in Nicotiana benthamiana
title_fullStr Serratia marcescens‐S3 inhibits Potato virus Y by activating ubiquitination of molecular chaperone proteins NbHsc70‐2 in Nicotiana benthamiana
title_full_unstemmed Serratia marcescens‐S3 inhibits Potato virus Y by activating ubiquitination of molecular chaperone proteins NbHsc70‐2 in Nicotiana benthamiana
title_short Serratia marcescens‐S3 inhibits Potato virus Y by activating ubiquitination of molecular chaperone proteins NbHsc70‐2 in Nicotiana benthamiana
title_sort serratia marcescens‐s3 inhibits potato virus y by activating ubiquitination of molecular chaperone proteins nbhsc70‐2 in nicotiana benthamiana
topic Research Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8966008/
https://www.ncbi.nlm.nih.gov/pubmed/34788498
http://dx.doi.org/10.1111/1751-7915.13964
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