Interaction between Movement Proteins of <i>Hibiscus green spot virus</i>
Movement proteins (MPs) of plant viruses enable the translocation of viral genomes from infected to healthy cells through plasmodesmata (PD). The MPs functions involve the increase of the PD permeability and routing of viral genome both to the PD entrance and through the modified PD. <i>Hibisc...
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2022-12-01
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author | Anastasia K. Atabekova Ekaterina A. Lazareva Alexander A. Lezzhov Anna D. Solovieva Sergei A. Golyshev Boris I. Skulachev Ilya D. Solovyev Alexander P. Savitsky Manfred Heinlein Sergey Y. Morozov Andrey G. Solovyev |
author_facet | Anastasia K. Atabekova Ekaterina A. Lazareva Alexander A. Lezzhov Anna D. Solovieva Sergei A. Golyshev Boris I. Skulachev Ilya D. Solovyev Alexander P. Savitsky Manfred Heinlein Sergey Y. Morozov Andrey G. Solovyev |
author_sort | Anastasia K. Atabekova |
collection | DOAJ |
description | Movement proteins (MPs) of plant viruses enable the translocation of viral genomes from infected to healthy cells through plasmodesmata (PD). The MPs functions involve the increase of the PD permeability and routing of viral genome both to the PD entrance and through the modified PD. <i>Hibiscus green spot virus</i> encodes two MPs, termed BMB1 and BMB2, which act in concert to accomplish virus cell-to-cell transport. BMB1, representing an NTPase/helicase domain-containing RNA-binding protein, localizes to the cytoplasm and the nucleoplasm. BMB2 is a small hydrophobic protein that interacts with the endoplasmic reticulum (ER) membranes and induces local constrictions of the ER tubules. In plant cells, BMB2 localizes to PD-associated membrane bodies (PAMBs) consisting of modified ER tubules and directs BMB1 to PAMBs. Here, we demonstrate that BMB1 and BMB2 interact in vitro and in vivo, and that their specific interaction is essential for BMB2-directed targeting of BMB1 to PAMBs. Using mutagenesis, we show that the interaction involves the C-terminal BMB1 region and the N-terminal region of BMB2. |
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id | doaj.art-65353c60106143519a64753728105c31 |
institution | Directory Open Access Journal |
issn | 1999-4915 |
language | English |
last_indexed | 2024-03-09T15:44:45Z |
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publisher | MDPI AG |
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series | Viruses |
spelling | doaj.art-65353c60106143519a64753728105c312023-11-24T18:38:51ZengMDPI AGViruses1999-49152022-12-011412274210.3390/v14122742Interaction between Movement Proteins of <i>Hibiscus green spot virus</i>Anastasia K. Atabekova0Ekaterina A. Lazareva1Alexander A. Lezzhov2Anna D. Solovieva3Sergei A. Golyshev4Boris I. Skulachev5Ilya D. Solovyev6Alexander P. Savitsky7Manfred Heinlein8Sergey Y. Morozov9Andrey G. Solovyev10A. N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, 119992 Moscow, RussiaDepartment of Virology, Biological Faculty, Moscow State University, 119234 Moscow, RussiaA. N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, 119992 Moscow, RussiaDepartment of Virology, Biological Faculty, Moscow State University, 119234 Moscow, RussiaA. N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, 119992 Moscow, RussiaDepartment of Virology, Biological Faculty, Moscow State University, 119234 Moscow, RussiaA. N. Bach Institute of Biochemistry, Research Center of Biotechnology of the Russian Academy of Sciences, 119071 Moscow, RussiaA. N. Bach Institute of Biochemistry, Research Center of Biotechnology of the Russian Academy of Sciences, 119071 Moscow, RussiaInstitute for Plant Molecular Biology (IBMP-CNRS), University of Strasbourg, 67000 Strasbourg, FranceA. N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, 119992 Moscow, RussiaA. N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, 119992 Moscow, RussiaMovement proteins (MPs) of plant viruses enable the translocation of viral genomes from infected to healthy cells through plasmodesmata (PD). The MPs functions involve the increase of the PD permeability and routing of viral genome both to the PD entrance and through the modified PD. <i>Hibiscus green spot virus</i> encodes two MPs, termed BMB1 and BMB2, which act in concert to accomplish virus cell-to-cell transport. BMB1, representing an NTPase/helicase domain-containing RNA-binding protein, localizes to the cytoplasm and the nucleoplasm. BMB2 is a small hydrophobic protein that interacts with the endoplasmic reticulum (ER) membranes and induces local constrictions of the ER tubules. In plant cells, BMB2 localizes to PD-associated membrane bodies (PAMBs) consisting of modified ER tubules and directs BMB1 to PAMBs. Here, we demonstrate that BMB1 and BMB2 interact in vitro and in vivo, and that their specific interaction is essential for BMB2-directed targeting of BMB1 to PAMBs. Using mutagenesis, we show that the interaction involves the C-terminal BMB1 region and the N-terminal region of BMB2.https://www.mdpi.com/1999-4915/14/12/2742plant virusvirus transportcell-to-cell movementmovement proteinplasmodesmataprotein-protein interaction |
spellingShingle | Anastasia K. Atabekova Ekaterina A. Lazareva Alexander A. Lezzhov Anna D. Solovieva Sergei A. Golyshev Boris I. Skulachev Ilya D. Solovyev Alexander P. Savitsky Manfred Heinlein Sergey Y. Morozov Andrey G. Solovyev Interaction between Movement Proteins of <i>Hibiscus green spot virus</i> Viruses plant virus virus transport cell-to-cell movement movement protein plasmodesmata protein-protein interaction |
title | Interaction between Movement Proteins of <i>Hibiscus green spot virus</i> |
title_full | Interaction between Movement Proteins of <i>Hibiscus green spot virus</i> |
title_fullStr | Interaction between Movement Proteins of <i>Hibiscus green spot virus</i> |
title_full_unstemmed | Interaction between Movement Proteins of <i>Hibiscus green spot virus</i> |
title_short | Interaction between Movement Proteins of <i>Hibiscus green spot virus</i> |
title_sort | interaction between movement proteins of i hibiscus green spot virus i |
topic | plant virus virus transport cell-to-cell movement movement protein plasmodesmata protein-protein interaction |
url | https://www.mdpi.com/1999-4915/14/12/2742 |
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