Requirements for the Packaging of Geminivirus Circular Single-Stranded DNA: Effect of DNA Length and Coat Protein Sequence

Geminivirus particles, consisting of a pair of twinned isometric structures, have one of the most distinctive capsids in the virological world. Until recently, there was little information as to how these structures are generated. To address this, we developed a system to produce capsid structures f...

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Main Authors: Keith Saunders, Jake Richardson, David M. Lawson, George P. Lomonossoff
Format: Article
Language:English
Published: MDPI AG 2020-10-01
Series:Viruses
Subjects:
Online Access:https://www.mdpi.com/1999-4915/12/11/1235
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author Keith Saunders
Jake Richardson
David M. Lawson
George P. Lomonossoff
author_facet Keith Saunders
Jake Richardson
David M. Lawson
George P. Lomonossoff
author_sort Keith Saunders
collection DOAJ
description Geminivirus particles, consisting of a pair of twinned isometric structures, have one of the most distinctive capsids in the virological world. Until recently, there was little information as to how these structures are generated. To address this, we developed a system to produce capsid structures following the delivery of geminivirus coat protein and replicating circular single-stranded DNA (cssDNA) by the infiltration of gene constructs into plant leaves. The transencapsidation of cssDNA of the <i>Begomovirus</i> genus by coat protein of different geminivirus genera was shown to occur with full-length but not half-length molecules. Double capsid structures, distinct from geminate capsid structures, were also generated in this expression system. By increasing the length of the encapsidated cssDNA, triple geminate capsid structures, consisting of straight, bent and condensed forms were generated. The straight geminate triple structures generated were similar in morphology to those recorded for a potato-infecting virus from Peru. These finding demonstrate that the length of encapsidated DNA controls both the size and stability of geminivirus particles.
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spelling doaj.art-ee587f6e5ee84ed3a07648c63ac9cd062023-11-20T19:11:51ZengMDPI AGViruses1999-49152020-10-011211123510.3390/v12111235Requirements for the Packaging of Geminivirus Circular Single-Stranded DNA: Effect of DNA Length and Coat Protein SequenceKeith Saunders0Jake Richardson1David M. Lawson2George P. Lomonossoff3Department of Biological Chemistry, John Innes Centre, Norwich Research Park, Norwich NR4 7UH, UKDepartment of Cell and Developmental Biology, John Innes Centre, Norwich Research Park, Norwich NR4 7UH, UKDepartment of Biological Chemistry, John Innes Centre, Norwich Research Park, Norwich NR4 7UH, UKDepartment of Biological Chemistry, John Innes Centre, Norwich Research Park, Norwich NR4 7UH, UKGeminivirus particles, consisting of a pair of twinned isometric structures, have one of the most distinctive capsids in the virological world. Until recently, there was little information as to how these structures are generated. To address this, we developed a system to produce capsid structures following the delivery of geminivirus coat protein and replicating circular single-stranded DNA (cssDNA) by the infiltration of gene constructs into plant leaves. The transencapsidation of cssDNA of the <i>Begomovirus</i> genus by coat protein of different geminivirus genera was shown to occur with full-length but not half-length molecules. Double capsid structures, distinct from geminate capsid structures, were also generated in this expression system. By increasing the length of the encapsidated cssDNA, triple geminate capsid structures, consisting of straight, bent and condensed forms were generated. The straight geminate triple structures generated were similar in morphology to those recorded for a potato-infecting virus from Peru. These finding demonstrate that the length of encapsidated DNA controls both the size and stability of geminivirus particles.https://www.mdpi.com/1999-4915/12/11/1235geminiviruscoat proteincapsid morphologyencapsidationAYVV
spellingShingle Keith Saunders
Jake Richardson
David M. Lawson
George P. Lomonossoff
Requirements for the Packaging of Geminivirus Circular Single-Stranded DNA: Effect of DNA Length and Coat Protein Sequence
Viruses
geminivirus
coat protein
capsid morphology
encapsidation
AYVV
title Requirements for the Packaging of Geminivirus Circular Single-Stranded DNA: Effect of DNA Length and Coat Protein Sequence
title_full Requirements for the Packaging of Geminivirus Circular Single-Stranded DNA: Effect of DNA Length and Coat Protein Sequence
title_fullStr Requirements for the Packaging of Geminivirus Circular Single-Stranded DNA: Effect of DNA Length and Coat Protein Sequence
title_full_unstemmed Requirements for the Packaging of Geminivirus Circular Single-Stranded DNA: Effect of DNA Length and Coat Protein Sequence
title_short Requirements for the Packaging of Geminivirus Circular Single-Stranded DNA: Effect of DNA Length and Coat Protein Sequence
title_sort requirements for the packaging of geminivirus circular single stranded dna effect of dna length and coat protein sequence
topic geminivirus
coat protein
capsid morphology
encapsidation
AYVV
url https://www.mdpi.com/1999-4915/12/11/1235
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