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Viruses
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Plant Viruses: Pirates of Cellular Pathways, 2nd Edition
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Plant Viruses: Pirates of Cellular Pathways, 2nd Edition

A special issue of Viruses (ISSN 1999-4915). This special issue belongs to the section "Viruses of Plants, Fungi and Protozoa".

Deadline for manuscript submissions: 31 August 2024 | Viewed by 1619

Special Issue Editors

Prof. Dr. Michael Taliansky

E-Mail Website
Guest Editor
The James Hutton Institute, Invergowrie, Dundee DD2 5DA, UK
Interests: plant–virus interactions; cell nucleus and subnuclear structures; bionanotechnology
Special Issues, Collections and Topics in MDPI journals
Prof. Dr. Andrew J. Love

E-Mail Website
Guest Editor
Cell and Molecular Sciences, The James Hutton Institute, Errol Road, Invergowrie, Dundee DD2 5DA, UK
Interests: biotechnology; plant–virus interactions; cell nucleus; defence signalling pathways
Special Issues, Collections and Topics in MDPI journals
Dr. Alex M. Murphy

E-Mail Website
Guest Editor
Department of Plant Sciences, University of Cambridge, Cambridge CB2 3EA, UK
Interests: plant pathology
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

We would like to invite you to submit review and original research articles to the Special Issue of Viruses, “Plant Viruses: Pirates of Cellular Pathways, 2nd Edition”. Although viruses are very constrained with regard to genome size and the number of proteins they encode relative to other pathogens, they are remarkably efficient at subverting host cellular processes to control their own replication, spread, and dissemination in the environment. At the molecular level, it is astonishing that the few genes encoded by viruses and associated untranslated regions can trigger profound alterations in host cell signalling pathways, modulate the turnover/stability of host proteins, change the profiles of regulatory RNA species, vary cellular metabolic processes, and induce the redistribution of cellular components. Understanding these orchestrated programmed events triggered by virus infection are key to uncovering interventions, which may reduce or block the invasion by these pirates of cellular processes. We welcome papers related to the molecular, genetic, and biochemical bases controlling virus manipulation of host–virus–vector interactions. We also extend this invitation to researchers who exploit viruses as tools for biotechnology.

Prof. Dr. Michael Taliansky
Dr. Andrew J. Love
Dr. Alex M. Murphy
Guest Editors

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Viruses is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2600 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • virus–plant interactions
  • virus–host–vector interactions
  • virus replication
  • virus replication
  • virus evolution

Related Special Issue

Published Papers (2 papers)

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Research

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23 pages, 6645 KiB  
Article
Investigating the Interactions of the Cucumber Mosaic Virus 2b Protein with the Viral 1a Replicase Component and the Cellular RNA Silencing Factor Argonaute 1
by Sam Crawshaw, Alex M. Murphy, Pamela J. E. Rowling, Daniel Nietlispach, Laura S. Itzhaki and John P. Carr
Viruses 2024, 16(5), 676; https://doi.org/10.3390/v16050676 - 25 Apr 2024
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Abstract
The cucumber mosaic virus (CMV) 2b protein is a suppressor of plant defenses and a pathogenicity determinant. Amongst the 2b protein’s host targets is the RNA silencing factor Argonaute 1 (AGO1), which it binds to and inhibits. In Arabidopsis thaliana, if 2b-induced [...] Read more.
The cucumber mosaic virus (CMV) 2b protein is a suppressor of plant defenses and a pathogenicity determinant. Amongst the 2b protein’s host targets is the RNA silencing factor Argonaute 1 (AGO1), which it binds to and inhibits. In Arabidopsis thaliana, if 2b-induced inhibition of AGO1 is too efficient, it induces reinforcement of antiviral silencing by AGO2 and triggers increased resistance against aphids, CMV’s insect vectors. These effects would be deleterious to CMV replication and transmission, respectively, but are moderated by the CMV 1a protein, which sequesters sufficient 2b protein molecules into P-bodies to prevent excessive inhibition of AGO1. Mutant 2b protein variants were generated, and red and green fluorescent protein fusions were used to investigate subcellular colocalization with AGO1 and the 1a protein. The effects of mutations on complex formation with the 1a protein and AGO1 were investigated using bimolecular fluorescence complementation and co-immunoprecipitation assays. Although we found that residues 56–60 influenced the 2b protein’s interactions with the 1a protein and AGO1, it appears unlikely that any single residue or sequence domain is solely responsible. In silico predictions of intrinsic disorder within the 2b protein secondary structure were supported by circular dichroism (CD) but not by nuclear magnetic resonance (NMR) spectroscopy. Intrinsic disorder provides a plausible model to explain the 2b protein’s ability to interact with AGO1, the 1a protein, and other factors. However, the reasons for the conflicting conclusions provided by CD and NMR must first be resolved. Full article
(This article belongs to the Special Issue Plant Viruses: Pirates of Cellular Pathways, 2nd Edition)

Review

Jump to: Research

19 pages, 2644 KiB  
Review
Structural Insights into Plant Viruses Revealed by Small-Angle X-ray Scattering and Atomic Force Microscopy
by Eleonora V. Shtykova, Evgeniy V. Dubrovin, Alexander L. Ksenofontov, Polina K. Gifer, Maxim V. Petoukhov, Valeriy K. Tokhtar, Irina M. Sapozhnikova, Andrey N. Stavrianidi, Larisa V. Kordyukova and Oleg V. Batishchev
Viruses 2024, 16(3), 427; https://doi.org/10.3390/v16030427 - 10 Mar 2024
Viewed by 1025
Abstract
The structural study of plant viruses is of great importance to reduce the damage caused by these agricultural pathogens and to support their biotechnological applications. Nowadays, X-ray crystallography, NMR spectroscopy and cryo-electron microscopy are well accepted methods to obtain the 3D protein structure [...] Read more.
The structural study of plant viruses is of great importance to reduce the damage caused by these agricultural pathogens and to support their biotechnological applications. Nowadays, X-ray crystallography, NMR spectroscopy and cryo-electron microscopy are well accepted methods to obtain the 3D protein structure with the best resolution. However, for large and complex supramolecular structures such as plant viruses, especially flexible filamentous ones, there are a number of technical limitations to resolving their native structure in solution. In addition, they do not allow us to obtain structural information about dynamics and interactions with physiological partners. For these purposes, small-angle X-ray scattering (SAXS) and atomic force microscopy (AFM) are well established. In this review, we have outlined the main principles of these two methods and demonstrated their advantages for structural studies of plant viruses of different shapes with relatively high spatial resolution. In addition, we have demonstrated the ability of AFM to obtain information on the mechanical properties of the virus particles that are inaccessible to other experimental techniques. We believe that these under-appreciated approaches, especially when used in combination, are valuable tools for studying a wide variety of helical plant viruses, many of which cannot be resolved by classical structural methods. Full article
(This article belongs to the Special Issue Plant Viruses: Pirates of Cellular Pathways, 2nd Edition)
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