Multiple functions for ORF75c in murid herpesvirus-4 infection.
All gamma-herpesviruses encode at least one homolog of the cellular enzyme formyl-glycineamide-phosphoribosyl-amidotransferase. Murid herpesvirus-4 (MuHV-4) encodes 3 (ORFs 75a, 75b and 75c), suggesting that at least some copies have acquired new functions. Here we show that the corresponding protei...
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| Format: | Article |
| Language: | English |
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Public Library of Science (PLoS)
2008-07-01
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| Series: | PLoS ONE |
| Online Access: | https://journals.plos.org/plosone/article/file?id=10.1371/journal.pone.0002781&type=printable |
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| author | Miguel Gaspar Michael B Gill Jens-Bernhard Lösing Janet S May Philip G Stevenson |
| author_facet | Miguel Gaspar Michael B Gill Jens-Bernhard Lösing Janet S May Philip G Stevenson |
| author_sort | Miguel Gaspar |
| collection | DOAJ |
| description | All gamma-herpesviruses encode at least one homolog of the cellular enzyme formyl-glycineamide-phosphoribosyl-amidotransferase. Murid herpesvirus-4 (MuHV-4) encodes 3 (ORFs 75a, 75b and 75c), suggesting that at least some copies have acquired new functions. Here we show that the corresponding proteins are all present in virions and localize to infected cell nuclei. Despite these common features, ORFs 75a and 75b did not substitute functionally for a lack of ORF75c, as ORF75c virus knockouts were severely impaired for lytic replication in vitro and for host colonization in vivo. They showed 2 defects: incoming capsids failed to migrate to the nuclear margin following membrane fusion, and genomes that did reach the nucleus failed to initiate normal gene expression. The latter defect was associated with a failure of in-coming virions to disassemble PML bodies. The capsid transport deficit seemed to be functionally more important, since ORF75c(-) MuHV-4 infected both PML(+) and PML(-) cells poorly. The original host enzyme has therefore evolved into a set of distinct and multi-functional viral tegument proteins. One important function is moving incoming capsids to the nuclear margin for viral genome delivery. |
| format | Article |
| id | doaj-art-8d7407b7b40947dc823855860ac299fe |
| institution | OA Journals |
| issn | 1932-6203 |
| language | English |
| publishDate | 2008-07-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj-art-8d7407b7b40947dc823855860ac299fe2025-08-20T02:17:21ZengPublic Library of Science (PLoS)PLoS ONE1932-62032008-07-0137e278110.1371/journal.pone.0002781Multiple functions for ORF75c in murid herpesvirus-4 infection.Miguel GasparMichael B GillJens-Bernhard LösingJanet S MayPhilip G StevensonAll gamma-herpesviruses encode at least one homolog of the cellular enzyme formyl-glycineamide-phosphoribosyl-amidotransferase. Murid herpesvirus-4 (MuHV-4) encodes 3 (ORFs 75a, 75b and 75c), suggesting that at least some copies have acquired new functions. Here we show that the corresponding proteins are all present in virions and localize to infected cell nuclei. Despite these common features, ORFs 75a and 75b did not substitute functionally for a lack of ORF75c, as ORF75c virus knockouts were severely impaired for lytic replication in vitro and for host colonization in vivo. They showed 2 defects: incoming capsids failed to migrate to the nuclear margin following membrane fusion, and genomes that did reach the nucleus failed to initiate normal gene expression. The latter defect was associated with a failure of in-coming virions to disassemble PML bodies. The capsid transport deficit seemed to be functionally more important, since ORF75c(-) MuHV-4 infected both PML(+) and PML(-) cells poorly. The original host enzyme has therefore evolved into a set of distinct and multi-functional viral tegument proteins. One important function is moving incoming capsids to the nuclear margin for viral genome delivery.https://journals.plos.org/plosone/article/file?id=10.1371/journal.pone.0002781&type=printable |
| spellingShingle | Miguel Gaspar Michael B Gill Jens-Bernhard Lösing Janet S May Philip G Stevenson Multiple functions for ORF75c in murid herpesvirus-4 infection. PLoS ONE |
| title | Multiple functions for ORF75c in murid herpesvirus-4 infection. |
| title_full | Multiple functions for ORF75c in murid herpesvirus-4 infection. |
| title_fullStr | Multiple functions for ORF75c in murid herpesvirus-4 infection. |
| title_full_unstemmed | Multiple functions for ORF75c in murid herpesvirus-4 infection. |
| title_short | Multiple functions for ORF75c in murid herpesvirus-4 infection. |
| title_sort | multiple functions for orf75c in murid herpesvirus 4 infection |
| url | https://journals.plos.org/plosone/article/file?id=10.1371/journal.pone.0002781&type=printable |
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