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Architect of Virus Assembly: the Portal Protein Nucleates Procapsid Assembly in Bacteriophage P22
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Zeitschriftentitel: | Journal of Virology |
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Personen und Körperschaften: | , |
In: | Journal of Virology, 93, 2019, 9 |
Format: | E-Article |
Sprache: | Englisch |
veröffentlicht: |
American Society for Microbiology
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Schlagwörter: |
author_facet |
Motwani, Tina Teschke, Carolyn M. Motwani, Tina Teschke, Carolyn M. |
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author |
Motwani, Tina Teschke, Carolyn M. |
spellingShingle |
Motwani, Tina Teschke, Carolyn M. Journal of Virology Architect of Virus Assembly: the Portal Protein Nucleates Procapsid Assembly in Bacteriophage P22 Virology Insect Science Immunology Microbiology |
author_sort |
motwani, tina |
spelling |
Motwani, Tina Teschke, Carolyn M. 0022-538X 1098-5514 American Society for Microbiology Virology Insect Science Immunology Microbiology http://dx.doi.org/10.1128/jvi.00187-19 <jats:p> The existence of a single portal ring is essential to the formation of infectious virions in the tailed double-stranded DNA (dsDNA) phages, herpesviruses, and adenoviruses and, as such, is a viable antiviral therapeutic target. How only one portal is selectively incorporated at a unique vertex is unclear. In many dsDNA viruses and phages, the portal protein acts as an assembly nucleator. However, early work on phage P22 assembly <jats:italic>in vivo</jats:italic> indicated that the portal protein did not function as a nucleator for procapsid (PC) assembly, leading to the suggestion that P22 uses a unique mechanism for portal incorporation. Here, we show that portal protein nucleates assembly of P22 procapsid-like particles (PLPs). Addition of portal rings to an assembly reaction increases the rate of formation and yield of particles and corrects improper particle morphology. Our data suggest that procapsid assembly may universally initiate with a nucleation complex composed minimally of portal and scaffolding proteins (SPs). </jats:p> Architect of Virus Assembly: the Portal Protein Nucleates Procapsid Assembly in Bacteriophage P22 Journal of Virology |
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American Society for Microbiology |
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title |
Architect of Virus Assembly: the Portal Protein Nucleates Procapsid Assembly in Bacteriophage P22 |
title_unstemmed |
Architect of Virus Assembly: the Portal Protein Nucleates Procapsid Assembly in Bacteriophage P22 |
title_full |
Architect of Virus Assembly: the Portal Protein Nucleates Procapsid Assembly in Bacteriophage P22 |
title_fullStr |
Architect of Virus Assembly: the Portal Protein Nucleates Procapsid Assembly in Bacteriophage P22 |
title_full_unstemmed |
Architect of Virus Assembly: the Portal Protein Nucleates Procapsid Assembly in Bacteriophage P22 |
title_short |
Architect of Virus Assembly: the Portal Protein Nucleates Procapsid Assembly in Bacteriophage P22 |
title_sort |
architect of virus assembly: the portal protein nucleates procapsid assembly in bacteriophage p22 |
topic |
Virology Insect Science Immunology Microbiology |
url |
http://dx.doi.org/10.1128/jvi.00187-19 |
publishDate |
2019 |
physical |
|
description |
<jats:p>
The existence of a single portal ring is essential to the formation of infectious virions in the tailed double-stranded DNA (dsDNA) phages, herpesviruses, and adenoviruses and, as such, is a viable antiviral therapeutic target. How only one portal is selectively incorporated at a unique vertex is unclear. In many dsDNA viruses and phages, the portal protein acts as an assembly nucleator. However, early work on phage P22 assembly
<jats:italic>in vivo</jats:italic>
indicated that the portal protein did not function as a nucleator for procapsid (PC) assembly, leading to the suggestion that P22 uses a unique mechanism for portal incorporation. Here, we show that portal protein nucleates assembly of P22 procapsid-like particles (PLPs). Addition of portal rings to an assembly reaction increases the rate of formation and yield of particles and corrects improper particle morphology. Our data suggest that procapsid assembly may universally initiate with a nucleation complex composed minimally of portal and scaffolding proteins (SPs).
</jats:p> |
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author | Motwani, Tina, Teschke, Carolyn M. |
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author_sort | motwani, tina |
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description | <jats:p> The existence of a single portal ring is essential to the formation of infectious virions in the tailed double-stranded DNA (dsDNA) phages, herpesviruses, and adenoviruses and, as such, is a viable antiviral therapeutic target. How only one portal is selectively incorporated at a unique vertex is unclear. In many dsDNA viruses and phages, the portal protein acts as an assembly nucleator. However, early work on phage P22 assembly <jats:italic>in vivo</jats:italic> indicated that the portal protein did not function as a nucleator for procapsid (PC) assembly, leading to the suggestion that P22 uses a unique mechanism for portal incorporation. Here, we show that portal protein nucleates assembly of P22 procapsid-like particles (PLPs). Addition of portal rings to an assembly reaction increases the rate of formation and yield of particles and corrects improper particle morphology. Our data suggest that procapsid assembly may universally initiate with a nucleation complex composed minimally of portal and scaffolding proteins (SPs). </jats:p> |
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spelling | Motwani, Tina Teschke, Carolyn M. 0022-538X 1098-5514 American Society for Microbiology Virology Insect Science Immunology Microbiology http://dx.doi.org/10.1128/jvi.00187-19 <jats:p> The existence of a single portal ring is essential to the formation of infectious virions in the tailed double-stranded DNA (dsDNA) phages, herpesviruses, and adenoviruses and, as such, is a viable antiviral therapeutic target. How only one portal is selectively incorporated at a unique vertex is unclear. In many dsDNA viruses and phages, the portal protein acts as an assembly nucleator. However, early work on phage P22 assembly <jats:italic>in vivo</jats:italic> indicated that the portal protein did not function as a nucleator for procapsid (PC) assembly, leading to the suggestion that P22 uses a unique mechanism for portal incorporation. Here, we show that portal protein nucleates assembly of P22 procapsid-like particles (PLPs). Addition of portal rings to an assembly reaction increases the rate of formation and yield of particles and corrects improper particle morphology. Our data suggest that procapsid assembly may universally initiate with a nucleation complex composed minimally of portal and scaffolding proteins (SPs). </jats:p> Architect of Virus Assembly: the Portal Protein Nucleates Procapsid Assembly in Bacteriophage P22 Journal of Virology |
spellingShingle | Motwani, Tina, Teschke, Carolyn M., Journal of Virology, Architect of Virus Assembly: the Portal Protein Nucleates Procapsid Assembly in Bacteriophage P22, Virology, Insect Science, Immunology, Microbiology |
title | Architect of Virus Assembly: the Portal Protein Nucleates Procapsid Assembly in Bacteriophage P22 |
title_full | Architect of Virus Assembly: the Portal Protein Nucleates Procapsid Assembly in Bacteriophage P22 |
title_fullStr | Architect of Virus Assembly: the Portal Protein Nucleates Procapsid Assembly in Bacteriophage P22 |
title_full_unstemmed | Architect of Virus Assembly: the Portal Protein Nucleates Procapsid Assembly in Bacteriophage P22 |
title_short | Architect of Virus Assembly: the Portal Protein Nucleates Procapsid Assembly in Bacteriophage P22 |
title_sort | architect of virus assembly: the portal protein nucleates procapsid assembly in bacteriophage p22 |
title_unstemmed | Architect of Virus Assembly: the Portal Protein Nucleates Procapsid Assembly in Bacteriophage P22 |
topic | Virology, Insect Science, Immunology, Microbiology |
url | http://dx.doi.org/10.1128/jvi.00187-19 |