A pentameric protein ring with novel architecture is required for herpesviral packaging
Genome packaging in large double-stranded DNA viruses requires a powerful molecular motor to force the viral genome into nascent capsids, which involves essential accessory factors that are poorly understood. Here, we present structures of two such accessory factors from the oncogenic herpesviruses...
| Main Authors: | , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
eLife Sciences Publications Ltd
2021-02-01
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| Series: | eLife |
| Subjects: | |
| Online Access: | https://elifesciences.org/articles/62261 |
| _version_ | 1811236105415032832 |
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| author | Allison L Didychuk Stephanie N Gates Matthew R Gardner Lisa M Strong Andreas Martin Britt A Glaunsinger |
| author_facet | Allison L Didychuk Stephanie N Gates Matthew R Gardner Lisa M Strong Andreas Martin Britt A Glaunsinger |
| author_sort | Allison L Didychuk |
| collection | DOAJ |
| description | Genome packaging in large double-stranded DNA viruses requires a powerful molecular motor to force the viral genome into nascent capsids, which involves essential accessory factors that are poorly understood. Here, we present structures of two such accessory factors from the oncogenic herpesviruses Kaposi’s sarcoma-associated herpesvirus (KSHV; ORF68) and Epstein–Barr virus (EBV; BFLF1). These homologous proteins form highly similar homopentameric rings with a positively charged central channel that binds double-stranded DNA. Mutation of individual positively charged residues within but not outside the channel ablates DNA binding, and in the context of KSHV infection, these mutants fail to package the viral genome or produce progeny virions. Thus, we propose a model in which ORF68 facilitates the transfer of newly replicated viral genomes to the packaging motor. |
| first_indexed | 2024-04-12T12:03:11Z |
| format | Article |
| id | doaj.art-15f852b90be240649007f66750a4e52d |
| institution | Directory Open Access Journal |
| issn | 2050-084X |
| language | English |
| last_indexed | 2024-04-12T12:03:11Z |
| publishDate | 2021-02-01 |
| publisher | eLife Sciences Publications Ltd |
| record_format | Article |
| series | eLife |
| spelling | doaj.art-15f852b90be240649007f66750a4e52d2022-12-22T03:33:46ZengeLife Sciences Publications LtdeLife2050-084X2021-02-011010.7554/eLife.62261A pentameric protein ring with novel architecture is required for herpesviral packagingAllison L Didychuk0https://orcid.org/0000-0001-7277-5233Stephanie N Gates1https://orcid.org/0000-0002-4312-2900Matthew R Gardner2https://orcid.org/0000-0003-1334-5879Lisa M Strong3https://orcid.org/0000-0002-4293-8131Andreas Martin4https://orcid.org/0000-0003-0923-3284Britt A Glaunsinger5https://orcid.org/0000-0003-0479-9377Department of Plant and Microbial Biology, University of California, Berkeley, Berkeley, United StatesDepartment of Molecular and Cell Biology, University of California, Berkeley, Berkeley, United States; California Institute for Quantitative Biosciences, University of California, Berkeley, Berkeley, United States; Howard Hughes Medical Institute, University of California, Berkeley, Berkeley, United StatesDepartment of Plant and Microbial Biology, University of California, Berkeley, Berkeley, United StatesDepartment of Molecular and Cell Biology, University of California, Berkeley, Berkeley, United StatesDepartment of Molecular and Cell Biology, University of California, Berkeley, Berkeley, United States; California Institute for Quantitative Biosciences, University of California, Berkeley, Berkeley, United States; Howard Hughes Medical Institute, University of California, Berkeley, Berkeley, United StatesDepartment of Plant and Microbial Biology, University of California, Berkeley, Berkeley, United States; Department of Molecular and Cell Biology, University of California, Berkeley, Berkeley, United States; California Institute for Quantitative Biosciences, University of California, Berkeley, Berkeley, United States; Howard Hughes Medical Institute, University of California, Berkeley, Berkeley, United StatesGenome packaging in large double-stranded DNA viruses requires a powerful molecular motor to force the viral genome into nascent capsids, which involves essential accessory factors that are poorly understood. Here, we present structures of two such accessory factors from the oncogenic herpesviruses Kaposi’s sarcoma-associated herpesvirus (KSHV; ORF68) and Epstein–Barr virus (EBV; BFLF1). These homologous proteins form highly similar homopentameric rings with a positively charged central channel that binds double-stranded DNA. Mutation of individual positively charged residues within but not outside the channel ablates DNA binding, and in the context of KSHV infection, these mutants fail to package the viral genome or produce progeny virions. Thus, we propose a model in which ORF68 facilitates the transfer of newly replicated viral genomes to the packaging motor.https://elifesciences.org/articles/62261Kaposi's sarcoma-associated herpesvirusKSHVEpstein-Barr virusEBVherpesviruspackaging |
| spellingShingle | Allison L Didychuk Stephanie N Gates Matthew R Gardner Lisa M Strong Andreas Martin Britt A Glaunsinger A pentameric protein ring with novel architecture is required for herpesviral packaging eLife Kaposi's sarcoma-associated herpesvirus KSHV Epstein-Barr virus EBV herpesvirus packaging |
| title | A pentameric protein ring with novel architecture is required for herpesviral packaging |
| title_full | A pentameric protein ring with novel architecture is required for herpesviral packaging |
| title_fullStr | A pentameric protein ring with novel architecture is required for herpesviral packaging |
| title_full_unstemmed | A pentameric protein ring with novel architecture is required for herpesviral packaging |
| title_short | A pentameric protein ring with novel architecture is required for herpesviral packaging |
| title_sort | pentameric protein ring with novel architecture is required for herpesviral packaging |
| topic | Kaposi's sarcoma-associated herpesvirus KSHV Epstein-Barr virus EBV herpesvirus packaging |
| url | https://elifesciences.org/articles/62261 |
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