Capsid Structure of dsRNA Fungal Viruses
Most fungal, double-stranded (ds) RNA viruses lack an extracellular life cycle stage and are transmitted by cytoplasmic interchange. dsRNA mycovirus capsids are based on a 120-subunit T = 1 capsid, with a dimer as the asymmetric unit. These capsids, which remain structurally undisturbed throughout t...
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doaj-99eeae18789a492d9876cf4db17f1ae62020-11-25T00:47:18ZengMDPI AGViruses1999-49152018-09-0110948110.3390/v10090481v10090481Capsid Structure of dsRNA Fungal VirusesDaniel Luque0Carlos P. Mata1Nobuhiro Suzuki2Said A. Ghabrial3José R. Castón4Department of Structure of Macromolecules, Centro Nacional de Biotecnología (CNB-CSIC), Campus Cantoblanco, 28049 Madrid, SpainDepartment of Structure of Macromolecules, Centro Nacional de Biotecnología (CNB-CSIC), Campus Cantoblanco, 28049 Madrid, SpainInstitute of Plant Science and Resources, Okayama University, Kurashiki 710-0046, JapanDepartment of Plant Pathology, University of Kentucky, Lexington, KY 40546, USADepartment of Structure of Macromolecules, Centro Nacional de Biotecnología (CNB-CSIC), Campus Cantoblanco, 28049 Madrid, SpainMost fungal, double-stranded (ds) RNA viruses lack an extracellular life cycle stage and are transmitted by cytoplasmic interchange. dsRNA mycovirus capsids are based on a 120-subunit T = 1 capsid, with a dimer as the asymmetric unit. These capsids, which remain structurally undisturbed throughout the viral cycle, nevertheless, are dynamic particles involved in the organization of the viral genome and the viral polymerase necessary for RNA synthesis. The atomic structure of the T = 1 capsids of four mycoviruses was resolved: the L-A virus of Saccharomyces cerevisiae (ScV-L-A), Penicillium chrysogenum virus (PcV), Penicillium stoloniferum virus F (PsV-F), and Rosellinia necatrix quadrivirus 1 (RnQV1). These capsids show structural variations of the same framework, with 60 asymmetric or symmetric homodimers for ScV-L-A and PsV-F, respectively, monomers with a duplicated similar domain for PcV, and heterodimers of two different proteins for RnQV1. Mycovirus capsid proteins (CP) share a conserved α-helical domain, although the latter may carry different peptides inserted at preferential hotspots. Insertions in the CP outer surface are likely associated with enzymatic activities. Within the capsid, fungal dsRNA viruses show a low degree of genome compaction compared to reoviruses, and contain one to two copies of the RNA-polymerase complex per virion.http://www.mdpi.com/1999-4915/10/9/481dsRNA virusmycoviruscapsid proteincapsid structurevirus evolutionviral lineageScV-L-APcVPsV-FRnQV1 |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Daniel Luque Carlos P. Mata Nobuhiro Suzuki Said A. Ghabrial José R. Castón |
spellingShingle |
Daniel Luque Carlos P. Mata Nobuhiro Suzuki Said A. Ghabrial José R. Castón Capsid Structure of dsRNA Fungal Viruses Viruses dsRNA virus mycovirus capsid protein capsid structure virus evolution viral lineage ScV-L-A PcV PsV-F RnQV1 |
author_facet |
Daniel Luque Carlos P. Mata Nobuhiro Suzuki Said A. Ghabrial José R. Castón |
author_sort |
Daniel Luque |
title |
Capsid Structure of dsRNA Fungal Viruses |
title_short |
Capsid Structure of dsRNA Fungal Viruses |
title_full |
Capsid Structure of dsRNA Fungal Viruses |
title_fullStr |
Capsid Structure of dsRNA Fungal Viruses |
title_full_unstemmed |
Capsid Structure of dsRNA Fungal Viruses |
title_sort |
capsid structure of dsrna fungal viruses |
publisher |
MDPI AG |
series |
Viruses |
issn |
1999-4915 |
publishDate |
2018-09-01 |
description |
Most fungal, double-stranded (ds) RNA viruses lack an extracellular life cycle stage and are transmitted by cytoplasmic interchange. dsRNA mycovirus capsids are based on a 120-subunit T = 1 capsid, with a dimer as the asymmetric unit. These capsids, which remain structurally undisturbed throughout the viral cycle, nevertheless, are dynamic particles involved in the organization of the viral genome and the viral polymerase necessary for RNA synthesis. The atomic structure of the T = 1 capsids of four mycoviruses was resolved: the L-A virus of Saccharomyces cerevisiae (ScV-L-A), Penicillium chrysogenum virus (PcV), Penicillium stoloniferum virus F (PsV-F), and Rosellinia necatrix quadrivirus 1 (RnQV1). These capsids show structural variations of the same framework, with 60 asymmetric or symmetric homodimers for ScV-L-A and PsV-F, respectively, monomers with a duplicated similar domain for PcV, and heterodimers of two different proteins for RnQV1. Mycovirus capsid proteins (CP) share a conserved α-helical domain, although the latter may carry different peptides inserted at preferential hotspots. Insertions in the CP outer surface are likely associated with enzymatic activities. Within the capsid, fungal dsRNA viruses show a low degree of genome compaction compared to reoviruses, and contain one to two copies of the RNA-polymerase complex per virion. |
topic |
dsRNA virus mycovirus capsid protein capsid structure virus evolution viral lineage ScV-L-A PcV PsV-F RnQV1 |
url |
http://www.mdpi.com/1999-4915/10/9/481 |
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