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Article ; Online: SIRT5 is a proviral factor that interacts with SARS-CoV-2 Nsp14 protein.

Walter, Marius / Chen, Irene P / Vallejo-Gracia, Albert / Kim, Ik-Jung / Bielska, Olga / Lam, Victor L / Hayashi, Jennifer M / Cruz, Andrew / Shah, Samah / Soveg, Frank W / Gross, John D / Krogan, Nevan J / Jerome, Keith R / Schilling, Birgit / Ott, Melanie / Verdin, Eric

PLoS pathogens

2022 Volume 18, Issue 9, Page(s) e1010811

Abstract: SARS-CoV-2 non-structural protein Nsp14 is a highly conserved enzyme necessary for viral replication. Nsp14 forms a stable complex with non-structural protein Nsp10 and exhibits exoribonuclease and N7-methyltransferase activities. Protein-interactome ... ...

Abstract	SARS-CoV-2 non-structural protein Nsp14 is a highly conserved enzyme necessary for viral replication. Nsp14 forms a stable complex with non-structural protein Nsp10 and exhibits exoribonuclease and N7-methyltransferase activities. Protein-interactome studies identified human sirtuin 5 (SIRT5) as a putative binding partner of Nsp14. SIRT5 is an NAD-dependent protein deacylase critical for cellular metabolism that removes succinyl and malonyl groups from lysine residues. Here we investigated the nature of this interaction and the role of SIRT5 during SARS-CoV-2 infection. We showed that SIRT5 interacts with Nsp14, but not with Nsp10, suggesting that SIRT5 and Nsp10 are parts of separate complexes. We found that SIRT5 catalytic domain is necessary for the interaction with Nsp14, but that Nsp14 does not appear to be directly deacylated by SIRT5. Furthermore, knock-out of SIRT5 or treatment with specific SIRT5 inhibitors reduced SARS-CoV-2 viral levels in cell-culture experiments. SIRT5 knock-out cells expressed higher basal levels of innate immunity markers and mounted a stronger antiviral response, independently of the Mitochondrial Antiviral Signaling Protein MAVS. Our results indicate that SIRT5 is a proviral factor necessary for efficient viral replication, which opens novel avenues for therapeutic interventions.
MeSH term(s)	Antiviral Agents ; COVID-19 ; Exoribonucleases/metabolism ; Humans ; Lysine ; Methyltransferases/metabolism ; NAD ; Proviruses ; RNA, Viral/metabolism ; SARS-CoV-2 ; Sirtuins/genetics ; Viral Nonstructural Proteins/metabolism
Chemical Substances	Antiviral Agents ; RNA, Viral ; Viral Nonstructural Proteins ; NAD (0U46U6E8UK) ; Methyltransferases (EC 2.1.1.-) ; Exoribonucleases (EC 3.1.-) ; SIRT5 protein, human (EC 3.5.1.-) ; Sirtuins (EC 3.5.1.-) ; Lysine (K3Z4F929H6)
Language	English
Publishing date	2022-09-12
Publishing country	United States
Document type	Journal Article
ZDB-ID	2205412-1
ISSN	1553-7374 ; 1553-7374
ISSN (online)	1553-7374
ISSN	1553-7374
DOI	10.1371/journal.ppat.1010811
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Article ; Online: Viral E protein neutralizes BET protein-mediated post-entry antagonism of SARS-CoV-2.

Cell reports

2022 Volume 40, Issue 3, Page(s) 111088

Abstract: Inhibitors of bromodomain and extraterminal domain (BET) proteins are possible anti-severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) prophylactics as they downregulate angiotensin-converting enzyme 2 (ACE2). Here we show that BET proteins ... ...

Abstract	Inhibitors of bromodomain and extraterminal domain (BET) proteins are possible anti-severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) prophylactics as they downregulate angiotensin-converting enzyme 2 (ACE2). Here we show that BET proteins should not be inactivated therapeutically because they are critical antiviral factors at the post-entry level. Depletion of BRD3 or BRD4 in cells overexpressing ACE2 exacerbates SARS-CoV-2 infection; the same is observed when cells with endogenous ACE2 expression are treated with BET inhibitors during infection and not before. Viral replication and mortality are also enhanced in BET inhibitor-treated mice overexpressing ACE2. BET inactivation suppresses interferon production induced by SARS-CoV-2, a process phenocopied by the envelope (E) protein previously identified as a possible "histone mimetic." E protein, in an acetylated form, directly binds the second bromodomain of BRD4. Our data support a model where SARS-CoV-2 E protein evolved to antagonize interferon responses via BET protein inhibition; this neutralization should not be further enhanced with BET inhibitor treatment.
MeSH term(s)	Angiotensin-Converting Enzyme 2 ; Animals ; Antiviral Agents/pharmacology ; COVID-19 ; Interferons ; Mice ; Nuclear Proteins ; SARS-CoV-2 ; Transcription Factors ; Viral Proteins
Chemical Substances	Antiviral Agents ; Nuclear Proteins ; Transcription Factors ; Viral Proteins ; Interferons (9008-11-1) ; Angiotensin-Converting Enzyme 2 (EC 3.4.17.23)
Language	English
Publishing date	2022-06-27
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
ZDB-ID	2649101-1
ISSN	2211-1247 ; 2211-1247
ISSN (online)	2211-1247
ISSN	2211-1247
DOI	10.1016/j.celrep.2022.111088
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Article ; Online: Flavivirus Nonstructural Protein NS5 Dysregulates HSP90 to Broadly Inhibit JAK/STAT Signaling.

Roby, Justin A / Esser-Nobis, Katharina / Dewey-Verstelle, Elyse C / Fairgrieve, Marian R / Schwerk, Johannes / Lu, Amy Y / Soveg, Frank W / Hemann, Emily A / Hatfield, Lauren D / Keller, Brian C / Shapiro, Alexander / Forero, Adriana / Stencel-Baerenwald, Jennifer E / Savan, Ram / Gale, Michael

Cells

2020 Volume 9, Issue 4

Abstract: Pathogenic flaviviruses antagonize host cell Janus kinase/signal transducer and activator of transcription (JAK/STAT) signaling downstream of interferons α/β. Here, we show that flaviviruses inhibit JAK/STAT signaling induced by a wide range of cytokines ...

Abstract	Pathogenic flaviviruses antagonize host cell Janus kinase/signal transducer and activator of transcription (JAK/STAT) signaling downstream of interferons α/β. Here, we show that flaviviruses inhibit JAK/STAT signaling induced by a wide range of cytokines beyond interferon, including interleukins. This broad inhibition was mapped to viral nonstructural protein 5 (NS5) binding to cellular heat shock protein 90 (HSP90), resulting in reduced Janus kinase-HSP90 interaction and thus destabilization of unchaperoned JAKs (and other kinase clients) of HSP90 during infection by
MeSH term(s)	Animals ; Cell Line ; Flavivirus/metabolism ; HSP90 Heat-Shock Proteins/metabolism ; Humans ; Signal Transduction ; Transfection ; Viral Nonstructural Proteins/metabolism ; Zika Virus/metabolism ; Zika Virus Infection/metabolism ; Zika Virus Infection/virology
Chemical Substances	HSP90 Heat-Shock Proteins ; NS5 protein, flavivirus ; Viral Nonstructural Proteins
Language	English
Publishing date	2020-04-07
Publishing country	Switzerland
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2661518-6
ISSN	2073-4409 ; 2073-4409
ISSN (online)	2073-4409
ISSN	2073-4409
DOI	10.3390/cells9040899
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Article ; Online: RNA-binding protein isoforms ZAP-S and ZAP-L have distinct antiviral and immune resolution functions.

Schwerk, Johannes / Soveg, Frank W / Ryan, Andrew P / Thomas, Kerri R / Hatfield, Lauren D / Ozarkar, Snehal / Forero, Adriana / Kell, Alison M / Roby, Justin A / So, Lomon / Hyde, Jennifer L / Gale, Michael / Daugherty, Matthew D / Savan, Ram

Nature immunology

2019 Volume 20, Issue 12, Page(s) 1610–1620

Abstract: The initial response to viral infection is anticipatory, with host antiviral restriction factors and pathogen sensors constantly surveying the cell to rapidly mount an antiviral response through the synthesis and downstream activity of interferons. After ...

Abstract	The initial response to viral infection is anticipatory, with host antiviral restriction factors and pathogen sensors constantly surveying the cell to rapidly mount an antiviral response through the synthesis and downstream activity of interferons. After pathogen clearance, the host's ability to resolve this antiviral response and return to homeostasis is critical. Here, we found that isoforms of the RNA-binding protein ZAP functioned as both a direct antiviral restriction factor and an interferon-resolution factor. The short isoform of ZAP bound to and mediated the degradation of several host interferon messenger RNAs, and thus acted as a negative feedback regulator of the interferon response. In contrast, the long isoform of ZAP had antiviral functions and did not regulate interferon. The two isoforms contained identical RNA-targeting domains, but differences in their intracellular localization modulated specificity for host versus viral RNA, which resulted in disparate effects on viral replication during the innate immune response.
MeSH term(s)	Alphavirus Infections/genetics ; Alphavirus Infections/immunology ; Feedback, Physiological ; HEK293 Cells ; Hep G2 Cells ; Homeostasis ; Humans ; Immunity, Innate ; Interferon Regulatory Factor-3/genetics ; Interferon Regulatory Factor-3/metabolism ; Interferons/genetics ; Protein Binding ; Protein Isoforms/genetics ; Protein Isoforms/metabolism ; RNA/genetics ; RNA/metabolism ; RNA, Small Interfering/genetics ; RNA-Binding Proteins/genetics ; RNA-Binding Proteins/metabolism ; Repressor Proteins/genetics ; Repressor Proteins/metabolism ; Sindbis Virus/physiology ; Virus Replication
Chemical Substances	IRF3 protein, human ; Interferon Regulatory Factor-3 ; Protein Isoforms ; RNA, Small Interfering ; RNA-Binding Proteins ; Repressor Proteins ; YLPM1 protein, human ; RNA (63231-63-0) ; Interferons (9008-11-1)
Language	English
Publishing date	2019-11-18
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2016987-5
ISSN	1529-2916 ; 1529-2908
ISSN (online)	1529-2916
ISSN	1529-2908
DOI	10.1038/s41590-019-0527-6
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Article: Viral E Protein Neutralizes BET Protein-Mediated Post-Entry Antagonism of SARS-CoV-2.

bioRxiv : the preprint server for biology

2021

Abstract: Inhibitors of Bromodomain and Extra-terminal domain (BET) proteins are possible anti-SARS-CoV-2 prophylactics as they downregulate angiotensin-converting enzyme 2 (ACE2). Here, we show that BET proteins should not be inactivated therapeutically as they ... ...

Abstract	Inhibitors of Bromodomain and Extra-terminal domain (BET) proteins are possible anti-SARS-CoV-2 prophylactics as they downregulate angiotensin-converting enzyme 2 (ACE2). Here, we show that BET proteins should not be inactivated therapeutically as they are critical antiviral factors at the post-entry level. Knockouts of BRD3 or BRD4 in cells overexpressing ACE2 exacerbate SARS-CoV-2 infection; the same is observed when cells with endogenous ACE2 expression are treated with BET inhibitors during infection, and not before. Viral replication and mortality are also enhanced in BET inhibitor-treated mice overexpressing ACE2. BET inactivation suppresses interferon production induced by SARS-CoV-2, a process phenocopied by the envelope (E) protein previously identified as a possible "histone mimetic." E protein, in an acetylated form, directly binds the second bromodomain of BRD4. Our data support a model where SARS-CoV-2 E protein evolved to antagonize interferon responses via BET protein inhibition; this neutralization should not be further enhanced with BET inhibitor treatment.
Language	English
Publishing date	2021-11-15
Publishing country	United States
Document type	Preprint
DOI	10.1101/2021.11.14.468537
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Article ; Online: α-Tocopherol supplementation of allergic female mice inhibits development of CD11c+CD11b+ dendritic cells in utero and allergic inflammation in neonates.

Abdala-Valencia, Hiam / Berdnikovs, Sergejs / Soveg, Frank W / Cook-Mills, Joan M

American journal of physiology. Lung cellular and molecular physiology

2014 Volume 307, Issue 6, Page(s) L482–96

Abstract: α-Tocopherol blocks responses to allergen challenge in allergic adult mice, but it is not known whether α-tocopherol regulates the development of allergic disease. Development of allergic disease often occurs early in life. In clinical studies and animal ...

Abstract	α-Tocopherol blocks responses to allergen challenge in allergic adult mice, but it is not known whether α-tocopherol regulates the development of allergic disease. Development of allergic disease often occurs early in life. In clinical studies and animal models, offspring of allergic mothers have increased responsiveness to allergen challenge. Therefore, we determined whether α-tocopherol blocked development of allergic responses in offspring of allergic female mice. Allergic female mice were supplemented with α-tocopherol starting at mating. The pups from allergic mothers developed allergic lung responses, whereas pups from saline-treated mothers did not respond to the allergen challenge, and α-tocopherol supplementation of allergic female mice resulted in a dose-dependent reduction in eosinophils in the pup bronchoalveolar lavage and lungs after allergen challenge. There was also a reduction in pup lung CD11b(+) dendritic cell subsets that are critical to development of allergic responses, but there was no change in several CD11b(-) dendritic cell subsets. Furthermore, maternal supplementation with α-tocopherol reduced the number of fetal liver CD11b(+) dendritic cells in utero. In the pups, there was reduced allergen-induced lung mRNA expression of IL-4, IL-33, TSLP, CCL11, and CCL24. Cross-fostering pups at the time of birth demonstrated that α-tocopherol had a regulatory function in utero. In conclusion, maternal supplementation with α-tocopherol reduced fetal development of subsets of dendritic cells that are critical for allergic responses and reduced development of allergic responses in pups from allergic mothers. These results have implications for supplementation of allergic mothers with α-tocopherol.
MeSH term(s)	Animals ; Animals, Newborn ; Antioxidants/pharmacology ; CD11b Antigen/immunology ; CD11c Antigen/immunology ; Cytokines/immunology ; Dendritic Cells/immunology ; Dendritic Cells/pathology ; Dietary Supplements ; Female ; Hypersensitivity/drug therapy ; Hypersensitivity/immunology ; Hypersensitivity/pathology ; Mice ; Pregnancy ; Prenatal Exposure Delayed Effects/drug therapy ; Prenatal Exposure Delayed Effects/immunology ; Prenatal Exposure Delayed Effects/pathology ; alpha-Tocopherol/pharmacology
Chemical Substances	Antioxidants ; CD11b Antigen ; CD11c Antigen ; Cytokines ; alpha-Tocopherol (H4N855PNZ1)
Language	English
Publishing date	2014-07-11
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	1013184-x
ISSN	1522-1504 ; 1040-0605
ISSN (online)	1522-1504
ISSN	1040-0605
DOI	10.1152/ajplung.00132.2014
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Article ; Online: Endomembrane targeting of human OAS1 p46 augments antiviral activity.

Soveg, Frank W / Schwerk, Johannes / Gokhale, Nandan S / Cerosaletti, Karen / Smith, Julian R / Pairo-Castineira, Erola / Kell, Alison M / Forero, Adriana / Zaver, Shivam A / Esser-Nobis, Katharina / Roby, Justin A / Hsiang, Tien-Ying / Ozarkar, Snehal / Clingan, Jonathan M / McAnarney, Eileen T / Stone, Amy El / Malhotra, Uma / Speake, Cate / Perez, Joseph /

Balu, Chiraag / Allenspach, Eric J / Hyde, Jennifer L / Menachery, Vineet D / Sarkar, Saumendra N / Woodward, Joshua J / Stetson, Daniel B / Baillie, John Kenneth / Buckner, Jane H / Gale, Michael / Savan, Ram

eLife

2021 Volume 10

Abstract: Many host RNA sensors are positioned in the cytosol to detect viral RNA during infection. However, most positive-strand RNA viruses replicate within a modified organelle co-opted from intracellular membranes of the endomembrane system, which shields ... ...

Abstract	Many host RNA sensors are positioned in the cytosol to detect viral RNA during infection. However, most positive-strand RNA viruses replicate within a modified organelle co-opted from intracellular membranes of the endomembrane system, which shields viral products from cellular innate immune sensors. Targeting innate RNA sensors to the endomembrane system may enhance their ability to sense RNA generated by viruses that use these compartments for replication. Here, we reveal that an isoform of oligoadenylate synthetase 1, OAS1 p46, is prenylated and targeted to the endomembrane system. Membrane localization of OAS1 p46 confers enhanced access to viral replication sites and results in increased antiviral activity against a subset of RNA viruses including flaviviruses, picornaviruses, and SARS-CoV-2. Finally, our human genetic analysis shows that the
MeSH term(s)	2',5'-Oligoadenylate Synthetase/metabolism ; Animals ; COVID-19/immunology ; COVID-19/virology ; CRISPR-Cas Systems ; Cell Line ; Gene Editing ; Humans ; Polymorphism, Single Nucleotide ; SARS-CoV-2/isolation & purification ; SARS-CoV-2/metabolism
Chemical Substances	OAS1 protein, human (EC 2.7.7.-) ; 2',5'-Oligoadenylate Synthetase (EC 2.7.7.84)
Language	English
Publishing date	2021-08-03
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2687154-3
ISSN	2050-084X ; 2050-084X
ISSN (online)	2050-084X
ISSN	2050-084X
DOI	10.7554/eLife.71047
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Article: Limited Cross-Variant Immunity after Infection with the SARS-CoV-2 Omicron Variant Without Vaccination.

Suryawanshi, Rahul K / Chen, Irene P / Ma, Tongcui / Syed, Abdullah M / Brazer, Noah / Saldhi, Prachi / Simoneau, Camille R / Ciling, Alison / Khalid, Mir M / Sreekumar, Bharath / Chen, Pei-Yi / Kumar, G Renuka / Montano, Mauricio / Garcia-Knight, Miguel A / Sotomayor-Gonzalez, Alicia / Servellita, Venice / Gliwa, Amelia / Nguyen, Jenny / Silva, Ines /

Milbes, Bilal / Kojima, Noah / Hess, Victoria / Shacreaw, Maria / Lopez, Lauren / Brobeck, Matthew / Turner, Fred / Soveg, Frank W / George, Ashley F / Fang, Xiaohui / Maishan, Mazharul / Matthay, Michael / Greene, Warner C / Andino, Raul / Spraggon, Lee / Roan, Nadia R / Chiu, Charles Y / Doudna, Jennifer / Ott, Melanie

medRxiv : the preprint server for health sciences

2022

Abstract: SARS-CoV-2 Delta and Omicron strains are the most globally relevant variants of concern (VOCs). While individuals infected with Delta are at risk to develop severe lung ... ...

Abstract	SARS-CoV-2 Delta and Omicron strains are the most globally relevant variants of concern (VOCs). While individuals infected with Delta are at risk to develop severe lung disease
Language	English
Publishing date	2022-02-09
Publishing country	United States
Document type	Preprint
DOI	10.1101/2022.01.13.22269243
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Article ; Online: Viral E Protein Neutralizes BET Protein-Mediated Post-Entry Antagonism of SARS-CoV-2

bioRxiv

Abstract	Inhibitors of Bromodomain and Extra-terminal domain (BET) proteins are possible anti-SARS-CoV-2 prophylactics as they downregulate angiotensin-converting enzyme 2 (ACE2). Here, we show that BET proteins should not be inactivated therapeutically as they are critical antiviral factors at the post-entry level. Knockouts of BRD3 or BRD4 in cells overexpressing ACE2 exacerbate SARS-CoV-2 infection; the same is observed when cells with endogenous ACE2 expression are treated with BET inhibitors during infection, and not before. Viral replication and mortality are also enhanced in BET inhibitor-treated mice overexpressing ACE2. BET inactivation suppresses interferon production induced by SARS-CoV-2, a process phenocopied by the envelope (E) protein previously identified as a possible "histone mimetic." E protein, in an acetylated form, directly binds the second bromodomain of BRD4. Our data support a model where SARS-CoV-2 E protein evolved to antagonize interferon responses via BET protein inhibition; this neutralization should not be further enhanced with BET inhibitor treatment.
Keywords	covid19
Language	English
Publishing date	2021-11-15
Publisher	Cold Spring Harbor Laboratory
Document type	Article ; Online
DOI	10.1101/2021.11.14.468537
Database	COVID19

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Article ; Online: Limited cross-variant immunity from SARS-CoV-2 Omicron without vaccination.

Suryawanshi, Rahul K / Chen, Irene P / Ma, Tongcui / Syed, Abdullah M / Brazer, Noah / Saldhi, Prachi / Simoneau, Camille R / Ciling, Alison / Khalid, Mir M / Sreekumar, Bharath / Chen, Pei-Yi / Kumar, G Renuka / Montano, Mauricio / Gascon, Ronne / Tsou, Chia-Lin / Garcia-Knight, Miguel A / Sotomayor-Gonzalez, Alicia / Servellita, Venice / Gliwa, Amelia /

Nature

2022 Volume 607, Issue 7918, Page(s) 351–355

Abstract: SARS-CoV-2 Delta and Omicron are globally relevant variants of concern. Although individuals infected with Delta are at risk of developing severe lung disease, infection with Omicron often causes milder symptoms, especially in vaccinated ... ...

Abstract	SARS-CoV-2 Delta and Omicron are globally relevant variants of concern. Although individuals infected with Delta are at risk of developing severe lung disease, infection with Omicron often causes milder symptoms, especially in vaccinated individuals
MeSH term(s)	Animals ; Antibodies, Neutralizing/immunology ; Antibodies, Viral/immunology ; COVID-19/immunology ; COVID-19/prevention & control ; COVID-19/virology ; COVID-19 Vaccines/administration & dosage ; Cross Protection/immunology ; Cytokines ; Humans ; Mice ; SARS-CoV-2/classification ; SARS-CoV-2/immunology ; Vaccination/statistics & numerical data
Chemical Substances	Antibodies, Neutralizing ; Antibodies, Viral ; COVID-19 Vaccines ; Cytokines
Language	English
Publishing date	2022-05-18
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
ZDB-ID	120714-3
ISSN	1476-4687 ; 0028-0836
ISSN (online)	1476-4687
ISSN	0028-0836
DOI	10.1038/s41586-022-04865-0
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