Properties of Plant Virus Protein Encoded by the 5′-Proximal Gene of Tetra-Cistron Movement Block

To move from cell to cell through plasmodesmata, many plant viruses require the concerted action of two or more movement proteins (MPs) encoded by transport gene modules of virus genomes. A tetra-cistron movement block (TCMB) is a newly discovered transport module comprising four genes. TCMB encodes...

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Bibliographic Details
Published in:International journal of molecular sciences 2023-09, Vol.24 (18), p.14144
Main Authors: Chergintsev, Denis A, Solovieva, Anna D, Atabekova, Anastasia K, Lezzhov, Alexander A, Golyshev, Sergei A, Morozov, Sergey Y, Solovyev, Andrey G
Format: Article
Language:English
Subjects:
Analysis
Antiviral agents
Bacterial proteins
Dihydrofolate reductase
E coli
Genes
Genomes
Genomics
Health aspects
Membranes
plant virus
Political aspects
Protein binding
Proteins
RNA
RNA silencing
RNA-binding protein
Viral infections
viral suppressor of RNA silencing
virus cell-to-cell movement
virus movement protein
Viruses
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Summary:To move from cell to cell through plasmodesmata, many plant viruses require the concerted action of two or more movement proteins (MPs) encoded by transport gene modules of virus genomes. A tetra-cistron movement block (TCMB) is a newly discovered transport module comprising four genes. TCMB encodes three proteins, which are similar to MPs of the transport module known as the “triple gene block”, and a protein unrelated to known viral MPs and containing a double-stranded RNA (dsRNA)-binding domain similar to that found in a family of cell proteins, including AtDRB4 and AtHYL1. Here, the latter TCMB protein, named vDRB for virus dsRNA-binding protein, is shown to bind both dsRNA and single-stranded RNA in vitro. In a turnip crinkle virus-based assay, vDRB exhibits the properties of a viral suppressor of RNA silencing (VSR). In the context of potato virus X infection, vDRB significantly decreases the number and size of “dark green islands”, regions of local antiviral silencing, supporting the VSR function of vDRB. Nevertheless, vDRB does not exhibit the VSR properties in non-viral transient expression assays. Taken together, the data presented here indicate that vDRB is an RNA-binding protein exhibiting VSR functions in the context of viral infection.
ISSN:1422-0067
1661-6596
1422-0067
DOI:10.3390/ijms241814144