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Polyamine-metabolizing enzymes are activated to promote the proper assembly of rice stripe mosaic virus in insect vectors
Both viruses and host cells compete for intracellular polyamines for efficient propagation. Currently, how the key polyamine-metabolizing enzymes, including ornithine decarboxylase 1 (ODC1) and its antizyme 1 (OAZ1), are activated to co-ordinate viral propagation and polyamine biosynthesis remains u...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Springer Nature Singapore
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10441986/ https://www.ncbi.nlm.nih.gov/pubmed/37676339 http://dx.doi.org/10.1007/s44154-021-00032-z |
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author | Jia, Dongsheng Liu, Huan Zhang, Jian Wan, Wenqiang Wang, Zongwen Zhang, Xiaofeng Chen, Qian Wei, Taiyun |
author_facet | Jia, Dongsheng Liu, Huan Zhang, Jian Wan, Wenqiang Wang, Zongwen Zhang, Xiaofeng Chen, Qian Wei, Taiyun |
author_sort | Jia, Dongsheng |
collection | PubMed |
description | Both viruses and host cells compete for intracellular polyamines for efficient propagation. Currently, how the key polyamine-metabolizing enzymes, including ornithine decarboxylase 1 (ODC1) and its antizyme 1 (OAZ1), are activated to co-ordinate viral propagation and polyamine biosynthesis remains unknown. Here, we report that the matrix protein of rice stripe mosaic virus (RSMV), a cytorhabdovirus, directly hijacks OAZ1 to ensure the proper assembly of rigid bacilliform non-enveloped virions in leafhopper vector. Viral matrix protein effectively competes with ODC1 to bind to OAZ1, and thus, the ability of OAZ1 to target and mediate the degradation of ODC1 is significantly inhibited during viral propagation, which finally promotes polyamines production. Thus, OAZ1 and ODC1 are activated to synergistically promote viral persistent propagation and polyamine biosynthesis in viruliferous vectors. Our data suggest that it is a novel mechanism for rhabdovirus to exploit OAZ1 for facilitating viral assembly. SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1007/s44154-021-00032-z. |
format | Online Article Text |
id | pubmed-10441986 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | Springer Nature Singapore |
record_format | MEDLINE/PubMed |
spelling | pubmed-104419862023-08-28 Polyamine-metabolizing enzymes are activated to promote the proper assembly of rice stripe mosaic virus in insect vectors Jia, Dongsheng Liu, Huan Zhang, Jian Wan, Wenqiang Wang, Zongwen Zhang, Xiaofeng Chen, Qian Wei, Taiyun Stress Biol Original Paper Both viruses and host cells compete for intracellular polyamines for efficient propagation. Currently, how the key polyamine-metabolizing enzymes, including ornithine decarboxylase 1 (ODC1) and its antizyme 1 (OAZ1), are activated to co-ordinate viral propagation and polyamine biosynthesis remains unknown. Here, we report that the matrix protein of rice stripe mosaic virus (RSMV), a cytorhabdovirus, directly hijacks OAZ1 to ensure the proper assembly of rigid bacilliform non-enveloped virions in leafhopper vector. Viral matrix protein effectively competes with ODC1 to bind to OAZ1, and thus, the ability of OAZ1 to target and mediate the degradation of ODC1 is significantly inhibited during viral propagation, which finally promotes polyamines production. Thus, OAZ1 and ODC1 are activated to synergistically promote viral persistent propagation and polyamine biosynthesis in viruliferous vectors. Our data suggest that it is a novel mechanism for rhabdovirus to exploit OAZ1 for facilitating viral assembly. SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1007/s44154-021-00032-z. Springer Nature Singapore 2022-04-15 /pmc/articles/PMC10441986/ /pubmed/37676339 http://dx.doi.org/10.1007/s44154-021-00032-z Text en © The Author(s) 2022 https://creativecommons.org/licenses/by/4.0/Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) . |
spellingShingle | Original Paper Jia, Dongsheng Liu, Huan Zhang, Jian Wan, Wenqiang Wang, Zongwen Zhang, Xiaofeng Chen, Qian Wei, Taiyun Polyamine-metabolizing enzymes are activated to promote the proper assembly of rice stripe mosaic virus in insect vectors |
title | Polyamine-metabolizing enzymes are activated to promote the proper assembly of rice stripe mosaic virus in insect vectors |
title_full | Polyamine-metabolizing enzymes are activated to promote the proper assembly of rice stripe mosaic virus in insect vectors |
title_fullStr | Polyamine-metabolizing enzymes are activated to promote the proper assembly of rice stripe mosaic virus in insect vectors |
title_full_unstemmed | Polyamine-metabolizing enzymes are activated to promote the proper assembly of rice stripe mosaic virus in insect vectors |
title_short | Polyamine-metabolizing enzymes are activated to promote the proper assembly of rice stripe mosaic virus in insect vectors |
title_sort | polyamine-metabolizing enzymes are activated to promote the proper assembly of rice stripe mosaic virus in insect vectors |
topic | Original Paper |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10441986/ https://www.ncbi.nlm.nih.gov/pubmed/37676339 http://dx.doi.org/10.1007/s44154-021-00032-z |
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