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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MDPI AG
2020-10-01
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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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issn | 1999-4915 |
language | English |
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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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