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Article ; Online: Minding the message: tactics controlling RNA decay, modification, and translation in virus-infected cells.

Burgess, Hannah M / Vink, Elizabeth I / Mohr, Ian

2022 Volume 36, Issue 3-4, Page(s) 108–132

Abstract: With their categorical requirement for host ribosomes to translate mRNA, viruses provide a wealth of genetically tractable models to investigate how gene expression is remodeled post-transcriptionally by infection-triggered biological stress. By co- ... ...

Abstract	With their categorical requirement for host ribosomes to translate mRNA, viruses provide a wealth of genetically tractable models to investigate how gene expression is remodeled post-transcriptionally by infection-triggered biological stress. By co-opting and subverting cellular pathways that control mRNA decay, modification, and translation, the global landscape of post-transcriptional processes is swiftly reshaped by virus-encoded factors. Concurrent host cell-intrinsic countermeasures likewise conscript post-transcriptional strategies to mobilize critical innate immune defenses. Here we review strategies and mechanisms that control mRNA decay, modification, and translation in animal virus-infected cells. Besides settling infection outcomes, post-transcriptional gene regulation in virus-infected cells epitomizes fundamental physiological stress responses in health and disease.
MeSH term(s)	Animals ; Host-Pathogen Interactions/genetics ; Protein Biosynthesis ; RNA Stability/genetics ; Ribosomes/genetics ; Viruses/genetics ; Viruses/metabolism
Language	English
Publishing date	2022-02-22
Publishing country	United States
Document type	Journal Article ; Review ; Research Support, N.I.H., Extramural
ZDB-ID	806684-x
ISSN	1549-5477 ; 0890-9369
ISSN (online)	1549-5477
ISSN	0890-9369
DOI	10.1101/gad.349276.121
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Zs.MG 54: Show issues

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Article ; Online: An eIF3d-dependent switch regulates HCMV replication by remodeling the infected cell translation landscape to mimic chronic ER stress.

Thompson, Letitia / Depledge, Daniel P / Burgess, Hannah M / Mohr, Ian

Cell reports

2022 Volume 39, Issue 5, Page(s) 110767

Abstract: Regulated loading of eIF3-bound 40S ribosomes on capped mRNA is generally dependent upon the translation initiation factor eIF4E; however, mRNA translation often proceeds during physiological stress, such as virus infection, when eIF4E availability and ... ...

Abstract	Regulated loading of eIF3-bound 40S ribosomes on capped mRNA is generally dependent upon the translation initiation factor eIF4E; however, mRNA translation often proceeds during physiological stress, such as virus infection, when eIF4E availability and activity are limiting. It remains poorly understood how translation of virus and host mRNAs are regulated during infection stress. While initially sensitive to mTOR inhibition, which limits eIF4E-dependent translation, we show that protein synthesis in human cytomegalovirus (HCMV)-infected cells unexpectedly becomes progressively reliant upon eIF3d. Targeting eIF3d selectively inhibits HCMV replication, reduces polyribosome abundance, and interferes with expression of essential virus genes and a host gene expression signature indicative of chronic ER stress that fosters HCMV reproduction. This reveals a strategy whereby cellular eIF3d-dependent protein production is hijacked to exploit virus-induced ER stress. Moreover, it establishes how switching between eIF4E and eIF3d-responsive cap-dependent translation can differentially tune virus and host gene expression in infected cells.
MeSH term(s)	Cytomegalovirus/physiology ; Eukaryotic Initiation Factor-3/genetics ; Eukaryotic Initiation Factor-3/metabolism ; Eukaryotic Initiation Factor-4E/metabolism ; Humans ; Polyribosomes/metabolism ; Protein Biosynthesis ; RNA, Messenger/genetics ; RNA, Messenger/metabolism ; Virus Replication
Chemical Substances	EIF3D protein, human ; Eukaryotic Initiation Factor-3 ; Eukaryotic Initiation Factor-4E ; RNA, Messenger
Language	English
Publishing date	2022-04-25
Publishing country	United States
Document type	Journal Article
ZDB-ID	2649101-1
ISSN	2211-1247 ; 2211-1247
ISSN (online)	2211-1247
ISSN	2211-1247
DOI	10.1016/j.celrep.2022.110767
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Article ; Online: Defining the Role of Stress Granules in Innate Immune Suppression by the Herpes Simplex Virus 1 Endoribonuclease VHS.

Burgess, Hannah M / Mohr, Ian

Journal of virology

2018 Volume 92, Issue 15

Abstract: In response to virus-induced shutoff host protein synthesis, dynamic aggregates containing mRNA, RNA-binding proteins and translation factors termed stress granules (SGs) often accumulate within the cytoplasm. SGs typically form following phosphorylation ...

Abstract	In response to virus-induced shutoff host protein synthesis, dynamic aggregates containing mRNA, RNA-binding proteins and translation factors termed stress granules (SGs) often accumulate within the cytoplasm. SGs typically form following phosphorylation and inactivation of the eukaryotic translation initiation factor 2α (eIF2α), a substrate of the double-stranded RNA (dsRNA)-activated kinase protein kinase R (PKR). The detection of innate immune sensors and effectors like PKR at SGs suggests a role in pathogen nucleic acid sensing. However, the functional importance of SGs in host innate responses is unclear and has primarily been examined in response to infection with select RNA viruses. During infection with the DNA virus herpes simplex virus 1 (HSV-1), the virus-encoded virion host shutoff (VHS) endoribonuclease is required to restrict interferon production, PKR activation, and SG formation, although the relationship between these activities remains incompletely understood. Here, we show that in cells infected with a VHS-deficient HSV-1 (ΔVHS) dsRNA accumulated and localized to SGs. Surprisingly, formation of dsRNA and its concentration at SGs was not required for beta interferon mRNA induction, indicating that suppression of type I interferon induction by VHS does not stem from its control of dsRNA accumulation. Instead, STING signaling downstream of cGMP-AMP synthase (cGAS)-dependent DNA sensing is required for beta interferon induction. In contrast, significantly less PKR activation is observed when SG assembly is disrupted by ISRIB, an inhibitor of phosphorylated eIF2α-mediated translation repression, or depleting SG scaffolding proteins G3BP1 or TIA1. This demonstrates that PKR activation is intimately linked to SG formation and that SGs form important hubs to potentiate PKR activation during infection.
MeSH term(s)	Cells, Cultured ; Cytoplasmic Granules/enzymology ; Cytoplasmic Granules/genetics ; Cytoplasmic Granules/immunology ; Fibroblasts/immunology ; Fibroblasts/metabolism ; Fibroblasts/virology ; Herpesvirus 1, Human/enzymology ; Herpesvirus 1, Human/genetics ; Herpesvirus 1, Human/immunology ; Humans ; Immunity, Innate ; Membrane Proteins/genetics ; Membrane Proteins/immunology ; Membrane Proteins/metabolism ; Nucleotidyltransferases/genetics ; Nucleotidyltransferases/immunology ; Nucleotidyltransferases/metabolism ; RNA, Double-Stranded/genetics ; RNA, Double-Stranded/immunology ; RNA, Double-Stranded/metabolism ; RNA, Viral/genetics ; RNA, Viral/immunology ; RNA, Viral/metabolism ; Ribonucleases/genetics ; Ribonucleases/immunology ; Ribonucleases/metabolism ; Signal Transduction/genetics ; Signal Transduction/immunology ; Viral Proteins/genetics ; Viral Proteins/immunology ; Viral Proteins/metabolism
Chemical Substances	Membrane Proteins ; RNA, Double-Stranded ; RNA, Viral ; STING1 protein, human ; Viral Proteins ; virion host shutoff protein, Simplexvirus (118367-50-3) ; Nucleotidyltransferases (EC 2.7.7.-) ; cGAS protein, human (EC 2.7.7.-) ; Ribonucleases (EC 3.1.-)
Language	English
Publishing date	2018-07-17
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	80174-4
ISSN	1098-5514 ; 0022-538X
ISSN (online)	1098-5514
ISSN	0022-538X
DOI	10.1128/JVI.00829-18
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Article ; Online: Vaccinia virus D10 has broad decapping activity that is regulated by mRNA splicing.

Ly, Michael / Burgess, Hannah M / Shah, Sahil B / Mohr, Ian / Glaunsinger, Britt A

PLoS pathogens

2022 Volume 18, Issue 2, Page(s) e1010099

Abstract: The mRNA 5' cap structure serves both to protect transcripts from degradation and promote their translation. Cap removal is thus an integral component of mRNA turnover that is carried out by cellular decapping enzymes, whose activity is tightly regulated ...

Abstract	The mRNA 5' cap structure serves both to protect transcripts from degradation and promote their translation. Cap removal is thus an integral component of mRNA turnover that is carried out by cellular decapping enzymes, whose activity is tightly regulated and coupled to other stages of the mRNA decay pathway. The poxvirus vaccinia virus (VACV) encodes its own decapping enzymes, D9 and D10, that act on cellular and viral mRNA, but may be regulated differently than their cellular counterparts. Here, we evaluated the targeting potential of these viral enzymes using RNA sequencing from cells infected with wild-type and decapping mutant versions of VACV as well as in uninfected cells expressing D10. We found that D9 and D10 target an overlapping subset of viral transcripts but that D10 plays a dominant role in depleting the vast majority of human transcripts, although not in an indiscriminate manner. Unexpectedly, the splicing architecture of a gene influences how robustly its corresponding transcript is targeted by D10, as transcripts derived from intronless genes are less susceptible to enzymatic decapping by D10. As all VACV genes are intronless, preferential decapping of transcripts from intron-containing genes provides an unanticipated mechanism for the virus to disproportionately deplete host transcripts and remodel the infected cell transcriptome.
MeSH term(s)	Endoribonucleases/metabolism ; Humans ; Poxviridae/genetics ; RNA Caps/genetics ; RNA Caps/metabolism ; RNA, Messenger/genetics ; RNA, Messenger/metabolism ; Vaccinia virus/genetics ; Vaccinia virus/metabolism ; Viral Proteins/metabolism
Chemical Substances	RNA Caps ; RNA, Messenger ; Viral Proteins ; Endoribonucleases (EC 3.1.-)
Language	English
Publishing date	2022-02-24
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2205412-1
ISSN	1553-7374 ; 1553-7374
ISSN (online)	1553-7374
ISSN	1553-7374
DOI	10.1371/journal.ppat.1010099
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Article ; Online: CCR4-NOT differentially controls host versus virus poly(a)-tail length and regulates HCMV infection.

Burgess, Hannah M / Grande, Rebecca / Riccio, Sofia / Dinesh, Ikshitaa / Winkler, Gerlof Sebastiaan / Depledge, Daniel P / Mohr, Ian

EMBO reports

2023 Volume 24, Issue 12, Page(s) e56327

Abstract: Unlike most RNA and DNA viruses that broadly stimulate mRNA decay and interfere with host gene expression, human cytomegalovirus (HCMV) extensively remodels the host translatome without producing an mRNA decay enzyme. By performing a targeted loss-of- ... ...

Abstract	Unlike most RNA and DNA viruses that broadly stimulate mRNA decay and interfere with host gene expression, human cytomegalovirus (HCMV) extensively remodels the host translatome without producing an mRNA decay enzyme. By performing a targeted loss-of-function screen in primary human fibroblasts, we here identify the host CCR4-NOT deadenylase complex members CNOT1 and CNOT3 as unexpected pro-viral host factors that selectively regulate HCMV reproduction. We find that the scaffold subunit CNOT1 is specifically required for late viral gene expression and genome-wide host responses in CCR4-NOT-disrupted cells. By profiling poly(A)-tail lengths of individual HCMV and host mRNAs using nanopore direct RNA sequencing, we reveal poly(A)-tails of viral messages to be markedly longer than those of cellular mRNAs and significantly less sensitive to CCR4-NOT disruption. Our data establish that mRNA deadenylation by host CCR4-NOT is critical for productive HCMV replication and define a new mechanism whereby herpesvirus infection subverts cellular mRNA metabolism to remodel the gene expression landscape of the infected cell. Moreover, we expose an unanticipated host factor with potential to become a therapeutic anti-HCMV target.
MeSH term(s)	Humans ; Transcription Factors/genetics ; Transcription Factors/metabolism ; RNA, Messenger/genetics ; RNA, Messenger/metabolism ; Herpesviridae Infections ; Receptors, CCR4/genetics ; Receptors, CCR4/metabolism
Chemical Substances	Transcription Factors ; RNA, Messenger ; CNOT3 protein, human ; CCR4 protein, human ; Receptors, CCR4 ; CNOT1 protein, human
Language	English
Publishing date	2023-10-17
Publishing country	England
Document type	Journal Article
ZDB-ID	2020896-0
ISSN	1469-3178 ; 1469-221X
ISSN (online)	1469-3178
ISSN	1469-221X
DOI	10.15252/embr.202256327
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Zs.A 5433: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
Zs.MG 41: Show issues

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Article ; Online: Evolutionary clash between myxoma virus and rabbit PKR in Australia.

Burgess, Hannah M / Mohr, Ian

Proceedings of the National Academy of Sciences of the United States of America

2016 Volume 113, Issue 15, Page(s) 3912–3914

MeSH term(s)	Animals ; Australia ; Biological Evolution ; Myxoma virus ; Rabbits
Language	English
Publishing date	2016-04-12
Publishing country	United States
Document type	Editorial ; Comment
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.1602063113
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Zs.A 1148: Show issues

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Article ; Online: Cellular 5'-3' mRNA exonuclease Xrn1 controls double-stranded RNA accumulation and anti-viral responses.

Burgess, Hannah M / Mohr, Ian

Cell host & microbe

2015 Volume 17, Issue 3, Page(s) 332–344

Abstract: By accelerating global mRNA decay, many viruses impair host protein synthesis, limiting host defenses and stimulating virus mRNA translation. Vaccinia virus (VacV) encodes two decapping enzymes (D9, D10) that remove protective 5' caps on mRNAs, ... ...

Abstract	By accelerating global mRNA decay, many viruses impair host protein synthesis, limiting host defenses and stimulating virus mRNA translation. Vaccinia virus (VacV) encodes two decapping enzymes (D9, D10) that remove protective 5' caps on mRNAs, presumably generating substrates for degradation by the host exonuclease Xrn1. Surprisingly, we find VacV infection of Xrn1-depleted cells inhibits protein synthesis, compromising virus growth. These effects are aggravated by D9 deficiency and dependent upon a virus transcription factor required for intermediate and late mRNA biogenesis. Considerable double-stranded RNA (dsRNA) accumulation in Xrn1-depleted cells is accompanied by activation of host dsRNA-responsive defenses controlled by PKR and 2'-5' oligoadenylate synthetase (OAS), which respectively inactivate the translation initiation factor eIF2 and stimulate RNA cleavage by RNase L. This proceeds despite VacV-encoded PKR and RNase L antagonists being present. Moreover, Xrn1 depletion sensitizes uninfected cells to dsRNA treatment. Thus, Xrn1 is a cellular factor regulating dsRNA accumulation and dsRNA-responsive innate immune effectors.
MeSH term(s)	Cells, Cultured ; Exoribonucleases/metabolism ; Fibroblasts/immunology ; Fibroblasts/virology ; Host-Pathogen Interactions ; Humans ; Immunity, Innate ; Microtubule-Associated Proteins/metabolism ; RNA, Double-Stranded/metabolism ; Vaccinia virus/immunology ; Vaccinia virus/physiology ; Virus Replication
Chemical Substances	Microtubule-Associated Proteins ; RNA, Double-Stranded ; Exoribonucleases (EC 3.1.-) ; XRN1 protein, human (EC 3.1.13.1)
Keywords	covid19
Language	English
Publishing date	2015-02-27
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2278004-X
ISSN	1934-6069 ; 1931-3128
ISSN (online)	1934-6069
ISSN	1931-3128
DOI	10.1016/j.chom.2015.02.003
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Zs.A 6578: Show issues

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Article ; Online: An integrated model for the nucleo-cytoplasmic transport of cytoplasmic poly(A)-binding proteins.

Burgess, Hannah M / Gray, Nicola K

Communicative & integrative biology

2012 Volume 5, Issue 3, Page(s) 243–247

Abstract: Cytoplasmic poly(A)-binding proteins (PABPs) regulate mRNA stability and translation. Although predominantly localized in the cytoplasm, PABP proteins also cycle through the nucleus. Recent work has established that their steady-state localization can be ...

Abstract	Cytoplasmic poly(A)-binding proteins (PABPs) regulate mRNA stability and translation. Although predominantly localized in the cytoplasm, PABP proteins also cycle through the nucleus. Recent work has established that their steady-state localization can be altered by cellular stresses such as ultraviolet (UV) radiation, and infection by several viruses, resulting in nuclear accumulation of PABPs. Here, we present further evidence that their interaction with and release from mRNA and translation complexes are important in determining their sub-cellular distribution and propose an integrated model for regulated nucleo-cytoplasmic transport of PABPs.
Language	English
Publishing date	2012-08-15
Publishing country	United States
Document type	Journal Article
ZDB-ID	2451097-X
ISSN	1942-0889 ; 1942-0889
ISSN (online)	1942-0889
ISSN	1942-0889
DOI	10.4161/cib.19347
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Article: Targeting Poxvirus Decapping Enzymes and mRNA Decay to Generate an Effective Oncolytic Virus.

Burgess, Hannah M / Pourchet, Aldo / Hajdu, Cristina H / Chiriboga, Luis / Frey, Alan B / Mohr, Ian

Molecular therapy oncolytics

2018 Volume 8, Page(s) 71–81

Abstract: Through the action of two virus-encoded decapping enzymes (D9 and D10) that remove protective caps from mRNA 5'-termini, Vaccinia virus (VACV) accelerates mRNA decay and limits activation of host defenses. D9- or D10-deficient VACV are markedly ... ...

Abstract	Through the action of two virus-encoded decapping enzymes (D9 and D10) that remove protective caps from mRNA 5'-termini, Vaccinia virus (VACV) accelerates mRNA decay and limits activation of host defenses. D9- or D10-deficient VACV are markedly attenuated in mice and fail to counter cellular double-stranded RNA-responsive innate immune effectors, including PKR. Here, we capitalize upon this phenotype and demonstrate that VACV deficient in either decapping enzyme are effective oncolytic viruses. Significantly, D9- or D10-deficient VACV displayed anti-tumor activity against syngeneic mouse tumors of different genetic backgrounds and human hepatocellular carcinoma xenografts. Furthermore, D9- and D10-deficient VACV hyperactivated the host anti-viral enzyme PKR in non-tumorigenic cells compared to wild-type virus. This establishes a new genetic platform for oncolytic VACV development that is deficient for a major pathogenesis determinant while retaining viral genes that support robust productive replication like those required for nucleotide metabolism. It further demonstrates how VACV mutants unable to execute a fundamental step in virus-induced mRNA decay can be unexpectedly translated into a powerful anti-tumor therapy.
Language	English
Publishing date	2018-01-31
Publishing country	United States
Document type	Journal Article
ISSN	2372-7705
ISSN	2372-7705
DOI	10.1016/j.omto.2018.01.001
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Article ; Online: mRNA-specific regulation of translation by poly(A)-binding proteins.

Burgess, Hannah M / Gray, Nicola K

Biochemical Society transactions

2010 Volume 38, Issue 6, Page(s) 1517–1522

Abstract: The regulation of translation has emerged as a major determinant of gene expression and is critical for both normal cellular function and the development of disease. Numerous studies have highlighted the diverse, and sometimes related, mechanisms which ... ...

Abstract	The regulation of translation has emerged as a major determinant of gene expression and is critical for both normal cellular function and the development of disease. Numerous studies have highlighted the diverse, and sometimes related, mechanisms which underlie the regulation of global translation rates and the translational control of specific mRNAs. In the present paper, we discuss the emerging roles of the basal translation factor PABP [poly(A)-binding protein] in mRNA-specific translational control in metazoa which suggest that PABP function is more complex than first recognized.
MeSH term(s)	Animals ; Gene Expression Regulation ; Poly A/genetics ; Poly A/metabolism ; Poly(A)-Binding Proteins/genetics ; Poly(A)-Binding Proteins/metabolism ; Protein Biosynthesis ; Protein Isoforms/genetics ; Protein Isoforms/metabolism ; RNA, Messenger/genetics ; RNA, Messenger/metabolism
Chemical Substances	Poly(A)-Binding Proteins ; Protein Isoforms ; RNA, Messenger ; Poly A (24937-83-5)
Language	English
Publishing date	2010-12-23
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	184237-7
ISSN	1470-8752 ; 0300-5127
ISSN (online)	1470-8752
ISSN	0300-5127
DOI	10.1042/BST0381517
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