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A Novel Rice Curl Dwarf-Associated Picornavirus Encodes a 3C Serine Protease Recognizing Uncommon EPT/S Cleavage Sites

Picornaviruses cause diseases in a wide range of vertebrates, invertebrates and plants. Here, a novel picornavirus was identified by RNA-seq technology from rice plants showing dwarfing and curling symptoms, and the name rice curl dwarf-associated virus (RCDaV) is tentatively proposed. The RCDaV gen...

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Autores principales: Zhang, Tianze, Li, Chenyang, Cao, Mengji, Wang, Dan, Wang, Qi, Xie, Yi, Gao, Shibo, Fu, Shuai, Zhou, Xueping, Wu, Jianxiang
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8549817/
https://www.ncbi.nlm.nih.gov/pubmed/34721366
http://dx.doi.org/10.3389/fmicb.2021.757451
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author Zhang, Tianze
Li, Chenyang
Cao, Mengji
Wang, Dan
Wang, Qi
Xie, Yi
Gao, Shibo
Fu, Shuai
Zhou, Xueping
Wu, Jianxiang
author_facet Zhang, Tianze
Li, Chenyang
Cao, Mengji
Wang, Dan
Wang, Qi
Xie, Yi
Gao, Shibo
Fu, Shuai
Zhou, Xueping
Wu, Jianxiang
author_sort Zhang, Tianze
collection PubMed
description Picornaviruses cause diseases in a wide range of vertebrates, invertebrates and plants. Here, a novel picornavirus was identified by RNA-seq technology from rice plants showing dwarfing and curling symptoms, and the name rice curl dwarf-associated virus (RCDaV) is tentatively proposed. The RCDaV genome consists of an 8,987 nt positive-stranded RNA molecule, excluding a poly(A) tail, that encodes two large polyproteins. Using in vitro cleavage assays, we have identified that the RCDaV 3C protease (3Cpro) as a serine protease recognizes the conserved EPT/S cleavage site which differs from the classic Q(E)/G(S) sites cleaved by most picornaviral 3C chymotrypsin-like cysteine proteases. Therefore, we comprehensively deciphered the RCDaV genome organization and showed that the two polyproteins of RCDaV can be cleaved into 12 mature proteins. We found that seven unclassified picornaviruses also encode a 3Cpro similar to RCDaV, and use the highly conserved EPT/S as the cleavage site. The precise genome organizations of these viruses were illustrated. Moreover, RCDaV and the seven unclassified picornaviruses share high sequence identities and similar genome organizations, and cluster into a distinct clade in the order Picornavirales. Our study provides valuable information for the understanding of picornaviral 3Cpros, deciphers the genome organization of a few relatively obscure picornaviruses, and lays the foundation for further pathogenesis research on these viruses.
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spelling pubmed-85498172021-10-28 A Novel Rice Curl Dwarf-Associated Picornavirus Encodes a 3C Serine Protease Recognizing Uncommon EPT/S Cleavage Sites Zhang, Tianze Li, Chenyang Cao, Mengji Wang, Dan Wang, Qi Xie, Yi Gao, Shibo Fu, Shuai Zhou, Xueping Wu, Jianxiang Front Microbiol Microbiology Picornaviruses cause diseases in a wide range of vertebrates, invertebrates and plants. Here, a novel picornavirus was identified by RNA-seq technology from rice plants showing dwarfing and curling symptoms, and the name rice curl dwarf-associated virus (RCDaV) is tentatively proposed. The RCDaV genome consists of an 8,987 nt positive-stranded RNA molecule, excluding a poly(A) tail, that encodes two large polyproteins. Using in vitro cleavage assays, we have identified that the RCDaV 3C protease (3Cpro) as a serine protease recognizes the conserved EPT/S cleavage site which differs from the classic Q(E)/G(S) sites cleaved by most picornaviral 3C chymotrypsin-like cysteine proteases. Therefore, we comprehensively deciphered the RCDaV genome organization and showed that the two polyproteins of RCDaV can be cleaved into 12 mature proteins. We found that seven unclassified picornaviruses also encode a 3Cpro similar to RCDaV, and use the highly conserved EPT/S as the cleavage site. The precise genome organizations of these viruses were illustrated. Moreover, RCDaV and the seven unclassified picornaviruses share high sequence identities and similar genome organizations, and cluster into a distinct clade in the order Picornavirales. Our study provides valuable information for the understanding of picornaviral 3Cpros, deciphers the genome organization of a few relatively obscure picornaviruses, and lays the foundation for further pathogenesis research on these viruses. Frontiers Media S.A. 2021-10-13 /pmc/articles/PMC8549817/ /pubmed/34721366 http://dx.doi.org/10.3389/fmicb.2021.757451 Text en Copyright © 2021 Zhang, Li, Cao, Wang, Wang, Xie, Gao, Fu, Zhou and Wu. https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Microbiology
Zhang, Tianze
Li, Chenyang
Cao, Mengji
Wang, Dan
Wang, Qi
Xie, Yi
Gao, Shibo
Fu, Shuai
Zhou, Xueping
Wu, Jianxiang
A Novel Rice Curl Dwarf-Associated Picornavirus Encodes a 3C Serine Protease Recognizing Uncommon EPT/S Cleavage Sites
title A Novel Rice Curl Dwarf-Associated Picornavirus Encodes a 3C Serine Protease Recognizing Uncommon EPT/S Cleavage Sites
title_full A Novel Rice Curl Dwarf-Associated Picornavirus Encodes a 3C Serine Protease Recognizing Uncommon EPT/S Cleavage Sites
title_fullStr A Novel Rice Curl Dwarf-Associated Picornavirus Encodes a 3C Serine Protease Recognizing Uncommon EPT/S Cleavage Sites
title_full_unstemmed A Novel Rice Curl Dwarf-Associated Picornavirus Encodes a 3C Serine Protease Recognizing Uncommon EPT/S Cleavage Sites
title_short A Novel Rice Curl Dwarf-Associated Picornavirus Encodes a 3C Serine Protease Recognizing Uncommon EPT/S Cleavage Sites
title_sort novel rice curl dwarf-associated picornavirus encodes a 3c serine protease recognizing uncommon ept/s cleavage sites
topic Microbiology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8549817/
https://www.ncbi.nlm.nih.gov/pubmed/34721366
http://dx.doi.org/10.3389/fmicb.2021.757451
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