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Dynamin-related protein 2 interacts with the membrane-associated methyltransferase domain of plantago asiatica mosaic virus replicase and promotes viral replication

Positive-strand RNA viruses replicate their RNA in the viral replication complex, a spherical structure formed by remodeling of host intracellular membranes. This process also requires the interaction between viral membrane-associated replication proteins and host factors. We previously identified t...

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Autores principales: Shinji, Haruka, Sasaki, Nobumitsu, Hamim, Islam, Itoh, Yoshiyuki, Taku, Kazuo, Hayashi, Yuho, Minato, Nami, Moriyama, Hiromitsu, Arie, Tsutomu, Komatsu, Ken
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10345747/
https://www.ncbi.nlm.nih.gov/pubmed/37149224
http://dx.doi.org/10.1016/j.virusres.2023.199128
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author Shinji, Haruka
Sasaki, Nobumitsu
Hamim, Islam
Itoh, Yoshiyuki
Taku, Kazuo
Hayashi, Yuho
Minato, Nami
Moriyama, Hiromitsu
Arie, Tsutomu
Komatsu, Ken
author_facet Shinji, Haruka
Sasaki, Nobumitsu
Hamim, Islam
Itoh, Yoshiyuki
Taku, Kazuo
Hayashi, Yuho
Minato, Nami
Moriyama, Hiromitsu
Arie, Tsutomu
Komatsu, Ken
author_sort Shinji, Haruka
collection PubMed
description Positive-strand RNA viruses replicate their RNA in the viral replication complex, a spherical structure formed by remodeling of host intracellular membranes. This process also requires the interaction between viral membrane-associated replication proteins and host factors. We previously identified the membrane-associated determinant of the replicase of plantago asiatica mosaic virus (PlAMV), a positive-strand RNA virus of the genus Potexvirus, in its methyltransferase (MET) domain, and suggested that its interaction with host factors is required to establish viral replication. Here we identified Nicotiana benthamiana dynamin-related protein 2 (NbDRP2) as an interactor of the MET domain of the PlAMV replicase by co-immunoprecipitation (Co-IP) and mass spectrometry analysis. NbDRP2 is closely related to the DRP2 subfamily proteins in Arabidopsis thaliana, AtDRP2A and AtDRP2B. Confocal microscopy observation and Co-IP confirmed the interaction between the MET domain and NbDRP2. Also, the expression of NbDRP2 was induced by PlAMV infection. PlAMV accumulation was reduced when the expression of NbDRP2 gene was suppressed by virus-induced gene silencing. In addition, PlAMV accumulation was reduced in protoplasts treated with dynamin inhibitor. These results indicate a proviral role of the interaction of NbDRP2 with the MET domain in PlAMV replication.
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spelling pubmed-103457472023-07-15 Dynamin-related protein 2 interacts with the membrane-associated methyltransferase domain of plantago asiatica mosaic virus replicase and promotes viral replication Shinji, Haruka Sasaki, Nobumitsu Hamim, Islam Itoh, Yoshiyuki Taku, Kazuo Hayashi, Yuho Minato, Nami Moriyama, Hiromitsu Arie, Tsutomu Komatsu, Ken Virus Res Article Positive-strand RNA viruses replicate their RNA in the viral replication complex, a spherical structure formed by remodeling of host intracellular membranes. This process also requires the interaction between viral membrane-associated replication proteins and host factors. We previously identified the membrane-associated determinant of the replicase of plantago asiatica mosaic virus (PlAMV), a positive-strand RNA virus of the genus Potexvirus, in its methyltransferase (MET) domain, and suggested that its interaction with host factors is required to establish viral replication. Here we identified Nicotiana benthamiana dynamin-related protein 2 (NbDRP2) as an interactor of the MET domain of the PlAMV replicase by co-immunoprecipitation (Co-IP) and mass spectrometry analysis. NbDRP2 is closely related to the DRP2 subfamily proteins in Arabidopsis thaliana, AtDRP2A and AtDRP2B. Confocal microscopy observation and Co-IP confirmed the interaction between the MET domain and NbDRP2. Also, the expression of NbDRP2 was induced by PlAMV infection. PlAMV accumulation was reduced when the expression of NbDRP2 gene was suppressed by virus-induced gene silencing. In addition, PlAMV accumulation was reduced in protoplasts treated with dynamin inhibitor. These results indicate a proviral role of the interaction of NbDRP2 with the MET domain in PlAMV replication. Elsevier 2023-05-14 /pmc/articles/PMC10345747/ /pubmed/37149224 http://dx.doi.org/10.1016/j.virusres.2023.199128 Text en © 2023 The Authors. Published by Elsevier B.V. https://creativecommons.org/licenses/by/4.0/This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Shinji, Haruka
Sasaki, Nobumitsu
Hamim, Islam
Itoh, Yoshiyuki
Taku, Kazuo
Hayashi, Yuho
Minato, Nami
Moriyama, Hiromitsu
Arie, Tsutomu
Komatsu, Ken
Dynamin-related protein 2 interacts with the membrane-associated methyltransferase domain of plantago asiatica mosaic virus replicase and promotes viral replication
title Dynamin-related protein 2 interacts with the membrane-associated methyltransferase domain of plantago asiatica mosaic virus replicase and promotes viral replication
title_full Dynamin-related protein 2 interacts with the membrane-associated methyltransferase domain of plantago asiatica mosaic virus replicase and promotes viral replication
title_fullStr Dynamin-related protein 2 interacts with the membrane-associated methyltransferase domain of plantago asiatica mosaic virus replicase and promotes viral replication
title_full_unstemmed Dynamin-related protein 2 interacts with the membrane-associated methyltransferase domain of plantago asiatica mosaic virus replicase and promotes viral replication
title_short Dynamin-related protein 2 interacts with the membrane-associated methyltransferase domain of plantago asiatica mosaic virus replicase and promotes viral replication
title_sort dynamin-related protein 2 interacts with the membrane-associated methyltransferase domain of plantago asiatica mosaic virus replicase and promotes viral replication
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10345747/
https://www.ncbi.nlm.nih.gov/pubmed/37149224
http://dx.doi.org/10.1016/j.virusres.2023.199128
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