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Article ; Online: Binding and entering: COVID finds a new home.

Vu, Michelle N / Menachery, Vineet D

2021 Volume 17, Issue 8, Page(s) e1009857

Abstract: Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2) emerged as a virus with a pathogenicity closer to Severe Acute Respiratory Syndrome Coronavirus (SARS-CoV) and Middle East Respiratory Syndrome Coronavirus (MERS-CoV) and a transmissibility ... ...

Abstract	Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2) emerged as a virus with a pathogenicity closer to Severe Acute Respiratory Syndrome Coronavirus (SARS-CoV) and Middle East Respiratory Syndrome Coronavirus (MERS-CoV) and a transmissibility similar to common cold coronaviruses (CoVs). In this review, we briefly discuss the features of the receptor-binding domain (RBD) and protease cleavage of the SARS-CoV-2 spike protein that enable SARS-CoV-2 to be a pandemic virus.
MeSH term(s)	Angiotensin-Converting Enzyme 2/metabolism ; COVID-19/metabolism ; COVID-19/virology ; Humans ; SARS-CoV-2/pathogenicity ; SARS-CoV-2/physiology ; Spike Glycoprotein, Coronavirus/metabolism ; Virus Internalization
Chemical Substances	Spike Glycoprotein, Coronavirus ; spike protein, SARS-CoV-2 ; Angiotensin-Converting Enzyme 2 (EC 3.4.17.23)
Language	English
Publishing date	2021-08-30
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	2205412-1
ISSN	1553-7374 ; 1553-7374
ISSN (online)	1553-7374
ISSN	1553-7374
DOI	10.1371/journal.ppat.1009857
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Enterovirus-Cardiomyocyte Interactions: Impact of Terminally Deleted Genomic RNAs on Viral and Host Functions.

Bouin, Alexis / Vu, Michelle N / Al-Hakeem, Ali / Tran, Genevieve P / Nguyen, Joseph H C / Semler, Bert L

Journal of virology

2022 Volume 97, Issue 1, Page(s) e0142622

Abstract: Group B enteroviruses, including coxsackievirus B3 (CVB3), can persistently infect cardiac tissue and cause dilated cardiomyopathy. Persistence is linked to 5' terminal deletions of viral genomic RNAs that have been detected together with minor ... ...

Abstract	Group B enteroviruses, including coxsackievirus B3 (CVB3), can persistently infect cardiac tissue and cause dilated cardiomyopathy. Persistence is linked to 5' terminal deletions of viral genomic RNAs that have been detected together with minor populations of full-length genomes in human infections. In this study, we explored the functions and interactions of the different viral RNA forms found in persistently infected patients and their putative role(s) in pathogenesis. Since enterovirus cardiac pathogenesis is linked to the viral proteinase 2A, we investigated the effect of different terminal genomic RNA deletions on 2A activity. We discovered that 5' terminal deletions in CVB3 genomic RNAs decreased the levels of 2A proteinase activity but could not abrogate it. Using newly generated viral reporters encoding nano-luciferase, we found that 5' terminal deletions resulted in decreased levels of viral protein and RNA synthesis in singly transfected cardiomyocyte cultures. Unexpectedly, when full-length and terminally deleted forms were cotransfected into cardiomyocytes, a cooperative interaction was observed, leading to increased viral RNA and protein production. However, when viral infections were carried out in cells harboring 5' terminally deleted CVB3 RNAs, a decrease in infectious particle production was observed. Our results provide a possible explanation for the necessity of full-length viral genomes during persistent infection, as they would stimulate efficient viral replication compared to that of the deleted genomes alone. To avoid high levels of viral particle production that would trigger cellular immune activation and host cell death, the terminally deleted RNA forms act to limit the production of viral particles, possibly as
MeSH term(s)	Humans ; Antigens, Viral ; Cardiomyopathy, Dilated/etiology ; Cardiomyopathy, Dilated/virology ; Coxsackievirus Infections/complications ; Enterovirus B, Human/metabolism ; Genomics ; Myocytes, Cardiac/virology ; Peptide Hydrolases ; Persistent Infection ; RNA, Viral/genetics ; Viral Proteins/metabolism ; Virus Replication
Chemical Substances	Antigens, Viral ; Peptide Hydrolases (EC 3.4.-) ; RNA, Viral ; Viral Proteins
Language	English
Publishing date	2022-12-08
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	80174-4
ISSN	1098-5514 ; 0022-538X
ISSN (online)	1098-5514
ISSN	0022-538X
DOI	10.1128/jvi.01426-22
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Article ; Online: Engineering SARS-CoV-2 using a reverse genetic system.

Xie, Xuping / Lokugamage, Kumari G / Zhang, Xianwen / Vu, Michelle N / Muruato, Antonio E / Menachery, Vineet D / Shi, Pei-Yong

Nature protocols

2021 Volume 16, Issue 3, Page(s) 1761–1784

Abstract: Reverse genetic systems are a critical tool for studying viruses and identifying countermeasures. In response to the ongoing COVID-19 pandemic, we recently developed an infectious complementary DNA (cDNA) clone for severe acute respiratory syndrome ... ...

Abstract	Reverse genetic systems are a critical tool for studying viruses and identifying countermeasures. In response to the ongoing COVID-19 pandemic, we recently developed an infectious complementary DNA (cDNA) clone for severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). The reverse genetic system can be used to rapidly engineer viruses with desired mutations to study the virus in vitro and in vivo. Viruses can also be designed for live-attenuated vaccine development and engineered with reporter genes to facilitate serodiagnosis, vaccine evaluation and antiviral screening. Thus, the reverse genetic system of SARS-CoV-2 will be widely used for both basic and translational research. However, due to the large size of the coronavirus genome (~30,000 nucleotides long) and several toxic genomic elements, manipulation of the reverse genetic system of SARS-COV-2 is not a trivial task and requires sophisticated methods. Here, we describe the technical details of how to engineer recombinant SARS-CoV-2. Overall, the process includes six steps: (i) prepare seven plasmids containing SARS-CoV-2 cDNA fragment(s), (ii) prepare high-quality DNA fragments through restriction enzyme digestion of the seven plasmids, (iii) assemble the seven cDNA fragments into a genome-length cDNA, (iv) in vitro transcribe RNA from the genome-length cDNA, (iv) electroporate the genome-length RNA into cells to recover recombinant viruses and (vi) characterize the rescued viruses. This protocol will enable researchers from different research backgrounds to master the use of the reverse genetic system and, consequently, accelerate COVID-19 research.
MeSH term(s)	DNA, Viral/genetics ; Genetic Engineering/methods ; Genome, Viral/genetics ; Reverse Genetics/methods ; SARS-CoV-2/genetics
Chemical Substances	DNA, Viral
Language	English
Publishing date	2021-01-29
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2244966-8
ISSN	1750-2799 ; 1754-2189
ISSN (online)	1750-2799
ISSN	1754-2189
DOI	10.1038/s41596-021-00491-8
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Article ; Online: Novel ionophores active against La Crosse virus identified through rapid antiviral screening

Sandler, Zachary J. / Vu, Michelle N. / Menachery, Vineet D. / Mounce, Bryan C.

bioRxiv

Abstract: Bunyaviruses are significant human pathogens, causing diseases ranging from hemorrhagic fevers to encephalitis. Among these viruses, La Crosse virus (LACV), a member of the California serogroup, circulates in the eastern and midwestern United States. ... ...

Abstract	Bunyaviruses are significant human pathogens, causing diseases ranging from hemorrhagic fevers to encephalitis. Among these viruses, La Crosse virus (LACV), a member of the California serogroup, circulates in the eastern and midwestern United States. While LACV infection is often asymptomatic, dozens of cases of encephalitis are reported yearly. Unfortunately, no antivirals have been approved to treat LACV infection. Here, we developed a method to rapidly test potential antivirals against LACV infection. From this screen, we identified several potential antiviral molecules, including known antivirals. Additionally, we identified many novel antivirals that exhibited antiviral activity without affecting cellular viability. Valinomycin, a potassium ionophore, was among our top targets. We found that valinomycin exhibited potent anti-LACV activity in multiple cell types in a dose-dependent manner. Valinomycin did not affect particle stability or infectivity, suggesting that it may preclude virus replication by altering cellular potassium ions, a known determinant of LACV entry. We extended these results to other ionophores and found that the antiviral activity of valinomycin extended to other viral families including bunyaviruses (Rift Valley fever virus, Keystone virus), enteroviruses (Coxsackievirus, rhinovirus), flavirivuses (Zika), and coronaviruses (229E and MERS-CoV). In all viral infections, we observed significant reductions in virus titer in valinomycin-treated cells. In sum, we demonstrate the importance of potassium ions to virus infection, suggesting a potential therapeutic target to disrupt virus replication. Importance No antivirals are approved for the treatment of bunyavirus infection. The ability to rapidly screen compounds and identify novel antivirals is one means to accelerate drug discovery for viruses with no approved treatments. We used this approach to screen hundreds of compounds against La Crosse virus, an emerging bunyavirus that causes significant disease, including encephalitis. We identified several known and previously unidentified antivirals. We focused on a potassium ionophore, valinomycin, due to its promising in vitro antiviral activity. We demonstrate that valinomycin, as well as a selection of other ionophores, exhibits activity against La Crosse virus as well as several other distantly related bunyaviruses. We finally observe that valinomycin has activity against a wide array of human viral pathogens, suggesting that disrupting potassium ion homeostasis with valinomycin may be a potent host pathway to target to quell virus infection.
Keywords	covid19
Publisher	BioRxiv; MedRxiv; WHO
Document type	Article ; Online
DOI	10.1101/2020.01.21.914929
Database	COVID19

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Article ; Online: Novel ionophores active against La Crosse virus identified through rapid antiviral screening

Sandler, Zachary J. / Vu, Michelle N. / Menachery, Vineet D. / Mounce, Bryan C.

bioRxiv

Keywords	covid19
Language	English
Publishing date	2020-01-23
Publisher	Cold Spring Harbor Laboratory
Document type	Article ; Online
DOI	10.1101/2020.01.21.914929
Database	COVID19

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Article ; Online: Novel Ionophores Active against La Crosse Virus Identified through Rapid Antiviral Screening.

Sandler, Zachary J / Firpo, Mason R / Omoba, Oreoluwa S / Vu, Michelle N / Menachery, Vineet D / Mounce, Bryan C

Antimicrobial agents and chemotherapy

2020 Volume 64, Issue 6

Abstract	Bunyaviruses are significant human pathogens, causing diseases ranging from hemorrhagic fevers to encephalitis. Among these viruses, La Crosse virus (LACV), a member of the California serogroup, circulates in the eastern and midwestern United States. While LACV infection is often asymptomatic, dozens of cases of encephalitis are reported yearly. Unfortunately, no antivirals have been approved to treat LACV infection. Here, we developed a method to rapidly test potential antivirals against LACV infection. From this screen, we identified several potential antiviral molecules, including known antivirals. Additionally, we identified many novel antivirals that exhibited antiviral activity without affecting cellular viability. Valinomycin, a potassium ionophore, was among our top targets. We found that valinomycin exhibited potent anti-LACV activity in multiple cell types in a dose-dependent manner. Valinomycin did not affect particle stability or infectivity, suggesting that it may preclude virus replication by altering cellular potassium ions, a known determinant of LACV entry. We extended these results to other ionophores and found that the antiviral activity of valinomycin extended to other viral families, including bunyaviruses (Rift Valley fever virus, Keystone virus), enteroviruses (coxsackievirus, rhinovirus), flavirivuses (Zika virus), and coronaviruses (human coronavirus 229E [HCoV-229E] and Middle East respiratory syndrome CoV [MERS-CoV]). In all viral infections, we observed significant reductions in virus titer in valinomycin-treated cells. In sum, we demonstrate the importance of potassium ions to virus infection, suggesting a potential therapeutic target to disrupt virus replication.
MeSH term(s)	Antiviral Agents/pharmacology ; Coronavirus/drug effects ; Dose-Response Relationship, Drug ; Drug Evaluation, Preclinical ; Encephalitis, California/drug therapy ; Encephalitis, California/virology ; Enterovirus/drug effects ; Flavivirus/drug effects ; Humans ; Ionophores/pharmacology ; La Crosse virus/drug effects ; Orthobunyavirus/drug effects ; Potassium/metabolism ; United States ; Valinomycin/pharmacology ; Virus Replication/drug effects
Chemical Substances	Antiviral Agents ; Ionophores ; Valinomycin (2001-95-8) ; Potassium (RWP5GA015D)
Keywords	covid19
Language	English
Publishing date	2020-05-21
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	217602-6
ISSN	1098-6596 ; 0066-4804
ISSN (online)	1098-6596
ISSN	0066-4804
DOI	10.1128/AAC.00086-20
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Zs.A 809: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)
Einzelsignatur: Show issues

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Article ; Online: The NSP3 protein of SARS-CoV-2 binds fragile X mental retardation proteins to disrupt UBAP2L interactions.

Garvanska, Dimitriya H / Alvarado, R Elias / Mundt, Filip Oskar / Lindqvist, Richard / Duel, Josephine Kerzel / Coscia, Fabian / Nilsson, Emma / Lokugamage, Kumari / Johnson, Bryan A / Plante, Jessica A / Morris, Dorothea R / Vu, Michelle N / Estes, Leah K / McLeland, Alyssa M / Walker, Jordyn / Crocquet-Valdes, Patricia A / Mendez, Blanca Lopez / Plante, Kenneth S / Walker, David H /

Weisser, Melanie Bianca / Överby, Anna K / Mann, Matthias / Menachery, Vineet D / Nilsson, Jakob

EMBO reports

2024 Volume 25, Issue 2, Page(s) 902–926

Abstract: Viruses interact with numerous host factors to facilitate viral replication and to dampen antiviral defense mechanisms. We currently have a limited mechanistic understanding of how SARS-CoV-2 binds host factors and the functional role of these ... ...

Abstract	Viruses interact with numerous host factors to facilitate viral replication and to dampen antiviral defense mechanisms. We currently have a limited mechanistic understanding of how SARS-CoV-2 binds host factors and the functional role of these interactions. Here, we uncover a novel interaction between the viral NSP3 protein and the fragile X mental retardation proteins (FMRPs: FMR1, FXR1-2). SARS-CoV-2 NSP3 mutant viruses preventing FMRP binding have attenuated replication in vitro and reduced levels of viral antigen in lungs during the early stages of infection. We show that a unique peptide motif in NSP3 binds directly to the two central KH domains of FMRPs and that this interaction is disrupted by the I304N mutation found in a patient with fragile X syndrome. NSP3 binding to FMRPs disrupts their interaction with the stress granule component UBAP2L through direct competition with a peptide motif in UBAP2L to prevent FMRP incorporation into stress granules. Collectively, our results provide novel insight into how SARS-CoV-2 hijacks host cell proteins and provides molecular insight into the possible underlying molecular defects in fragile X syndrome.
MeSH term(s)	Humans ; COVID-19 ; Fragile X Mental Retardation Protein/genetics ; Fragile X Mental Retardation Protein/metabolism ; Fragile X Syndrome/genetics ; Fragile X Syndrome/metabolism ; Peptides/metabolism ; RNA-Binding Proteins/genetics ; SARS-CoV-2
Chemical Substances	FMR1 protein, human ; Fragile X Mental Retardation Protein (139135-51-6) ; FXR1 protein, human ; Peptides ; RNA-Binding Proteins
Language	English
Publishing date	2024-01-02
Publishing country	England
Document type	Case Reports ; Journal Article
ZDB-ID	2020896-0
ISSN	1469-3178 ; 1469-221X
ISSN (online)	1469-3178
ISSN	1469-221X
DOI	10.1038/s44319-023-00043-z
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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: Loss-of-function mutation in Omicron variants reduces spike protein expression and attenuates SARS-CoV-2 infection.

bioRxiv : the preprint server for biology

2023

Abstract: SARS-CoV-2 Omicron variants emerged in 2022 with >30 novel amino acid mutations in the spike protein alone. While most studies focus on receptor binding domain changes, mutations in the C-terminus of S1 (CTS1), adjacent to the furin cleavage site, have ... ...

Abstract	SARS-CoV-2 Omicron variants emerged in 2022 with >30 novel amino acid mutations in the spike protein alone. While most studies focus on receptor binding domain changes, mutations in the C-terminus of S1 (CTS1), adjacent to the furin cleavage site, have largely been ignored. In this study, we examined three Omicron mutations in CTS1: H655Y, N679K, and P681H. Generating a SARS-CoV-2 triple mutant (YKH), we found that the mutant increased spike processing, consistent with prior reports for H655Y and P681H individually. Next, we generated a single N679K mutant, finding reduced viral replication
Language	English
Publishing date	2023-07-10
Publishing country	United States
Document type	Preprint
DOI	10.1101/2023.04.17.536926
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: SARS-CoV-2 Uses Nonstructural Protein 16 To Evade Restriction by IFIT1 and IFIT3.

Schindewolf, Craig / Lokugamage, Kumari / Vu, Michelle N / Johnson, Bryan A / Scharton, Dionna / Plante, Jessica A / Kalveram, Birte / Crocquet-Valdes, Patricia A / Sotcheff, Stephanea / Jaworski, Elizabeth / Alvarado, Rojelio E / Debbink, Kari / Daugherty, Matthew D / Weaver, Scott C / Routh, Andrew L / Walker, David H / Plante, Kenneth S / Menachery, Vineet D

Journal of virology

2023 Volume 97, Issue 2, Page(s) e0153222

Abstract: Understanding the molecular basis of innate immune evasion by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is an important consideration for designing the next wave of therapeutics. Here, we investigate the role of the nonstructural ... ...

Abstract	Understanding the molecular basis of innate immune evasion by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is an important consideration for designing the next wave of therapeutics. Here, we investigate the role of the nonstructural protein 16 (NSP16) of SARS-CoV-2 in infection and pathogenesis. NSP16, a ribonucleoside 2'-
MeSH term(s)	Adaptor Proteins, Signal Transducing/genetics ; Adaptor Proteins, Signal Transducing/metabolism ; COVID-19/virology ; Interferon Type I/metabolism ; Intracellular Signaling Peptides and Proteins/metabolism ; Methyltransferases/metabolism ; RNA-Binding Proteins/genetics ; SARS-CoV-2/genetics ; SARS-CoV-2/physiology ; Viral Nonstructural Proteins/metabolism ; Animals ; Cricetinae
Chemical Substances	Adaptor Proteins, Signal Transducing ; Interferon Type I ; Intracellular Signaling Peptides and Proteins ; Methyltransferases (EC 2.1.1.-) ; RNA-Binding Proteins ; Viral Nonstructural Proteins ; NSP16 protein, SARS-CoV-2
Language	English
Publishing date	2023-02-01
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	80174-4
ISSN	1098-5514 ; 0022-538X
ISSN (online)	1098-5514
ISSN	0022-538X
DOI	10.1128/jvi.01532-22
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Article: Novel Ionophores Active against La Crosse Virus Identified through Rapid Antiviral Screening

Sandler, Zachary J / Firpo, Mason R / Omoba, Oreoluwa S / Vu, Michelle N / Menachery, Vineet D / Mounce, Bryan C

Abstract	Bunyaviruses are significant human pathogens, causing diseases ranging from hemorrhagic fevers to encephalitis. Among these viruses, La Crosse virus (LACV), a member of the California serogroup, circulates in the eastern and midwestern United States. While LACV infection is often asymptomatic, dozens of cases of encephalitis are reported yearly. Unfortunately, no antivirals have been approved to treat LACV infection. Here, we developed a method to rapidly test potential antivirals against LACV infection. From this screen, we identified several potential antiviral molecules, including known antivirals. Additionally, we identified many novel antivirals that exhibited antiviral activity without affecting cellular viability. Valinomycin, a potassium ionophore, was among our top targets. We found that valinomycin exhibited potent anti-LACV activity in multiple cell types in a dose-dependent manner. Valinomycin did not affect particle stability or infectivity, suggesting that it may preclude virus replication by altering cellular potassium ions, a known determinant of LACV entry. We extended these results to other ionophores and found that the antiviral activity of valinomycin extended to other viral families, including bunyaviruses (Rift Valley fever virus, Keystone virus), enteroviruses (coxsackievirus, rhinovirus), flavirivuses (Zika virus), and coronaviruses (human coronavirus 229E [HCoV-229E] and Middle East respiratory syndrome CoV [MERS-CoV]). In all viral infections, we observed significant reductions in virus titer in valinomycin-treated cells. In sum, we demonstrate the importance of potassium ions to virus infection, suggesting a potential therapeutic target to disrupt virus replication.
Keywords	covid19
Publisher	WHO
Document type	Article
Note	WHO #Covidence: #684617
Database	COVID19

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