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Interaction between Movement Proteins of Hibiscus green spot virus.
Atabekova, Anastasia K; Lazareva, Ekaterina A; Lezzhov, Alexander A; Solovieva, Anna D; Golyshev, Sergei A; Skulachev, Boris I; Solovyev, Ilya D; Savitsky, Alexander P; Heinlein, Manfred; Morozov, Sergey Y; Solovyev, Andrey G.
Affiliation
  • Atabekova AK; A. N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, 119992 Moscow, Russia.
  • Lazareva EA; Department of Virology, Biological Faculty, Moscow State University, 119234 Moscow, Russia.
  • Lezzhov AA; Department of Virology, Biological Faculty, Moscow State University, 119234 Moscow, Russia.
  • Solovieva AD; A. N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, 119992 Moscow, Russia.
  • Golyshev SA; Department of Virology, Biological Faculty, Moscow State University, 119234 Moscow, Russia.
  • Skulachev BI; A. N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, 119992 Moscow, Russia.
  • Solovyev ID; Department of Virology, Biological Faculty, Moscow State University, 119234 Moscow, Russia.
  • Savitsky AP; A. N. Bach Institute of Biochemistry, Research Center of Biotechnology of the Russian Academy of Sciences, 119071 Moscow, Russia.
  • Heinlein M; A. N. Bach Institute of Biochemistry, Research Center of Biotechnology of the Russian Academy of Sciences, 119071 Moscow, Russia.
  • Morozov SY; Institute for Plant Molecular Biology (IBMP-CNRS), University of Strasbourg, 67000 Strasbourg, France.
  • Solovyev AG; A. N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, 119992 Moscow, Russia.
Viruses ; 14(12)2022 12 08.
Article in En | MEDLINE | ID: mdl-36560746
ABSTRACT
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. Hibiscus green spot virus 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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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Plant Viruses / RNA Viruses / Hibiscus Language: En Journal: Viruses Year: 2022 Document type: Article Affiliation country: RUSSIA Country of publication: CH / SUIZA / SUÍÇA / SWITZERLAND

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Plant Viruses / RNA Viruses / Hibiscus Language: En Journal: Viruses Year: 2022 Document type: Article Affiliation country: RUSSIA Country of publication: CH / SUIZA / SUÍÇA / SWITZERLAND