Announcements

MDPI will be attending the Asia-Pacific Congress of Medical Virology 2024 held in Singapore from 19 to 21 November 2024. The Asia–Pacific Congress of Medical Virology (APCMV) is a triennial international meeting that focuses on diagnostics, public health, research and clinical virology, with emphasis on the Asia–Pacific region. The aim of this congress is to foster the collaboration and information sharing of the latest research in the field of virology pertaining to medically important viruses and treatments against them. Including the most recent COVID-19 pandemic, many emerging virus infections have been centred in the Asia–Pacific region, and the breaking down of boundaries between civilisation and wildlife only serves to accelerate that. Therefore, it is vital for countries in the region to develop a strong public health, diagnostic and research base to address these problems. Hence, the APCMV congress series was established to enable the review, sharing and discussion in each of these areas to form a strong foundation for the management of medically important viruses.

The following MDPI journals will be represented:

• Pathogens;
• Viruses;
• Antibiotics;
• TropicalMed;
• CIMB;
• Life;
• IJMS.

If you are planning to attend the conference, please visit our booth #A07. Our delegates look forward to meeting you in person and answering any questions that you may have. For more information about the conference, please visit the following website: https://apcmv.com/about-apcmv/.

We are pleased to announce that Prof. Mark Douglas has been appointed Associate Editor of the “Human Virology and Viral Diseases” Section in Viruses (ISSN: 1999-4915). With his extensive background in scientific research and publishing, he brings a wealth of knowledge and expertise to this prestigious role.

Name: Prof. Mark Douglas
Affiliation: Storr Liver Centre, The Westmead Institute for Medical Research, The University of Sydney and Westmead Hospital, Sydney, Australia
Website: https://www.sydney.edu.au/medicine-health/about/our-people/academic-staff/mark-douglas

Prof. Mark Douglas is an infectious diseases physician and molecular virologist with a strong research interest in viral hepatitis. He heads the Viral Hepatitis Pathogenesis group at the Storr Liver Centre, Westmead Institute for Medical Research. He is involved in a broad array of projects, ranging from basic molecular pathogenesis to translational and clinical research. He runs liver clinics for patients with hepatitis B and hepatitis C and also treats patients at Westmead Hospital with HIV and a range of infectious diseases.

The following is a short Q&A with Prof. Mark Douglas, who shared his vision for the journal with us as well as his views on the research area and open access publishing:

1. What appealed to you about the journal that made you want to take on the role of Associate Editor?
Viruses is a respected journal that publishes high-quality articles on virology research, with fast review and feedback. As Associate Editor, I look forward to overseeing a thorough and fair peer review process to maintain its high standard.

2. As an expert in the field of viruses, which research topics do you think are popular at present, and what does the future of this field of research look like?
I am particularly passionate about hepatitis B virus research, which has exploded after the recent success of hepatitis C virus direct-acting antivirals. There is excitement in the field about the possibility of now developing a similar cure for hepatitis B.

3. You have been collaborating with Viruses as a Guest Editor, leading multiple Special Issues. Can you share with us more about your experience as Guest Editor over the past few years?
I have had a very positive experience with the editorial team at Viruses during my time as Guest Editor. They are always friendly, responsive, and supportive. They politely remind me about outstanding tasks, while remaining flexible and respecting my other commitments. They work hard to find and follow up with appropriate reviewers to ensure high-quality peer review.

4. What do you think of the development of open access in the publishing field?
Open access publishing has provided equitable access to research findings for people around the world, particularly those who do not have access to libraries with online subscriptions. It has also expanded the number of journals and their capacity to publish articles online rapidly, providing alternatives for authors seeking to publish their research. However, it is essential to provide thorough and timely peer review of articles submitted to open access journals, to ensure they only publish high-quality research, and that the results can be trusted. I see this as a key role of an Associate Editor, and I look forward to working with the editorial team at Viruses to maintain their high standards.

We warmly welcome our new Associate Editor, Prof. Mark Douglas, and wish the journal every success in the future.

As a leader in open access publishing, MDPI is eager to explore new collaboration opportunities, including the launch of new journals and the transfer of existing ones. At present, MDPI publishes over 400 journals, more than 160 of which have established partnerships with academic organizations. Additionally, we publish 19 association journals.

In order to enhance exchange and cooperation with scientific researchers and share the results of open science, MDPI invites experts and scholars from various fields to submit proposals for new journal collaboration opportunities. If your proposal is approved, you could take on the role of Editor-in-Chief, Deputy Editor-in-Chief, or Editorial Board Member of the journal. This position allows you to manage the manuscript review process alongside our editorial department, participate in calls for papers, strengthen your network with scholars in the field, expand scientific research cooperation, enhance your personal and academic influence internationally, and play a leading role in academia.

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MDPI will offer various promotional channels to enhance its visibility and promote it internationally.

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MDPI journals frequently grant travel awards to empower junior researchers to showcase their latest research at academic conferences, thereby amplifying their impact within their research fields.

We extend our heartfelt congratulations to the 103 recipients of MDPI's 2023 Travel Awards from different countries and territories for their exceptional presentations. These outstanding individuals were selected by the journal editors based on the strength of their research proposals and the anticipated impact of their presentations at academic conferences. We commend their exceptional contributions and wish them continued success in their academic endeavors.

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• Biology and Life Sciences;
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About MDPI Awards:

To reward the academic community, especially young researchers, and enhance communication among scientists, MDPI journals regularly offer various awards to researchers in specific fields. These awards, serving as a source of inspiration and recognition, help raise the influence of talented individuals who have been credited with outstanding achievements and are making a significant contribution to the advancement of their fields.

To explore more MDPI awards, please click here.

The “Insect Viruses” Section of our journal has been renamed to “Invertebrate Viruses”, following the suggestion of Section Associate Editor Prof. Dr. A. Lorena Passarelli and with the approval of Editor-in-Chief Dr. Eric O. Freed. The renamed “Invertebrate Viruses” Section will now include research on viruses affecting a broader spectrum of invertebrate species.

The original Section information and the updated version are listed below:

For more detailed information, please visit the following link: https://www.mdpi.com/journal/viruses/sections/invertebrate_viruses.

Viruses Editorial Office

Authors: Haydar Witwit, Carlos Alberto Betancourt, Beatrice Cubitt, Roaa Khafaji, Heinrich Kowalski, Nathaniel Jackson, Chengjin Ye, Luis Martinez-Sobrido and Juan C. de la Torre

The Challenge

Several mammarenaviruses, chiefly Lassa virus (LASV) in Western Africa and Junin (JUNV) in the Argentine Pampas cause hemorrhagic fever (HF) diseases associated with high morbidity and mortality, posing important public health problems in their endemic regions. In addition, mounting evidence indicates that the worldwide-distributed mammarenavirus lymphocytic choriomeningitis virus (LCMV) is a neglected human pathogen of clinical significance in paediatric and transplantation medicine [1–3]. Current anti-mammarenavirus therapy is limited to an off-label use of ribavirin for which efficacy remains controversial [4]. Hence, the importance of developing novel therapeutics to combat human pathogenic mammarenaviruses.

Our Discovery: A New Way to Fight Mammarenavirus Infections

Instead of targeting directly the activity of a viral protein, we focused on targeting N-myristoylation directed by the host cell N-myristoyltransferases (NMT1 and NMT2), a process that the virus relies on to complete both its cell entry and budding exiting processes [5,6]. We found that treatment with specific NMT inhibitors, DDD85646 or IMP-1088, effectively stop propagation of LCMV, as well as the HF causing mammarenaviruses LASV and JUNV [7].

Why This Matters

Our findings support the use of NMT inhibitors as a novel antiviral strategy to combat LASV and other human pathogenic mammarenaviruses. Targeting a host cell process can pose a much higher genetic barrier for the selection of drug-resistant variants, a common problem with direct antiviral drugs. NMT inhibitors can be also incorporated into combination therapy protocols.

A Deep Dive into NMT Inhibition in Mammarenavirus Life Cycle

Mammarenaviruses are enveloped viruses with a bi-segmented negative-stranded (NS) RNA genome [8]. Each genome RNA segment, L (ca 7.3 kb) and S (ca 3.5 kb), uses an ambisense coding strategy to direct the synthesis of two polypeptides in opposite orientation, separated by a non-coding intergenic region (IGR). The L genome segment encodes the viral RNA dependent RNA polymerase (L), and Z matrix protein, whereas the S genome segment encodes the viral glycoprotein precursor (GPC) and the viral nucleoprotein (NP). GPC is co-and post-translationally processed to produce a stable signal peptide (SSP), and the mature GP1 and GP2 subunits that together with the SSP form the spikes that decorate the virus surface and mediate cell entry via receptor-mediated endocytosis [9–11]. GP1 mediates binding to the cellular receptor and GP2 the pH-dependent fusion event in the late endosome required for release of the virus ribonucleoprotein (vRNP) complexes into the cell cytoplasm where they direct the replication and transcription of the viral genome [12,13].

Early studies have shown that N-myristoylation is required for the role of the mammarenavirus matrix Z protein in assembly and budding [5,6], and for the role of the SSP in the GP2-mediate fusion event [12]. These findings were based on the use of 2-hydroxy-myristic acid (2-HMA) and 2-HMA analogs as inhibitors of N-myristoyltransferases (NMT1 and NMT2) responsible for catalyzing N-myristoylation in mammalian cells [5,14]. However, recent studies have demonstrated that 2-HMA acts off-target and does not inhibit N-myristoylation in a concentration range consistent with activity on NMT [15]. Therefore, we have revisited the contribution of N-myristoylation in mammarenavirus infection using the validated on-target specific NMT1/2 inhibitor DDD85646 [16]. We found that DDD85646 exhibits a very potent antiviral activity against LCMV in cultured cells. Cell-based assays probing different steps of the LCMV life cycle revealed that DDD85646 exerted its anti-LCMV activity by interfering  with Z budding activity and GP2 mediated fusion between viral and cellular membranes, a process that requires the participation of myristoylated SSP [7] (Fig. 1).

Figure 1: Proposed model of the effect of the NMT inhibitor DDD85646 on mammarenavirus cell entry and budding

NMT isozymes facilitate the addition of myristic acid to glycine (2) of SSP and Z protein, which protect them from proteasome mediated degradation. Myristoylated SSP interacts with GP2 to facilitate the fusion event in the late endosome required to complete the virus cell entry process, whereas myristoylated Z directs the virus assembly and budding process. Inhibition of SSP and Z myristoylation by DDD85646 results in proteasome mediated degradation of SSP and Z which results in inhibition of virus multiplication. Z myr and SSP myr indicate myristoylated Z and SSP respectively.

During our studies, we observed only a minimal increase in Z protein levels in the presence of an NMT inhibitor, an unexpected finding as inhibition of Z myristoylation would interfere with the Z mediated budding process, thus resulting in accumulation of intracellular Z protein. This unexpected result led us to consider that non-myristoylated Z might be targeted for degradation. We found that treatment with the proteasome inhibitor MG132 rescued Z protein expression in the presence of an NMT inhibitor.

Experimental Validation

The Z proteins have been shown to inhibit in a dose-dependent manner the activity of the mammarenavirus vRNP, responsible for directing replication and transcription of the viral genome, in cell-based minigenome (MG) assays. We therefore predicted that Z inhibitory effect on the MG activity would be diminished in the presence of the pan-NMT inhibitor IMP-1088, and that treatment with MG132 would restore, in the presence of IMP-1088, the Z inhibitory effect on the MG activity (Fig. 2). 

Figure 2: Proposed model of the effect of the NMT (IMP-1088) and proteosome (MG132) inhibitors on the activity of the LCMV MG

NMT isozymes facilitate the addition of myristic acid to glycine (2) of Z protein, which protects the latter from degradation, thus allowing for the Z dose-dependent inhibitory effect on viral RNA synthesis mediated by the vRNP and the consequent inhibition of the activity of the LCMV MG.  Inhibition of Z myristoylation by IMP-1088 results in proteasome mediated degradation of Z, which will relief the Z inhibitory effect on the activity of the LCMV MG (right side of the graph). Treatment with the proteasome inhibitor MG132 prevents IMP-1088 induced Z protein degradation, thus resulting in LCMV MG inhibition. L polymerase (green), NP (red) and RNA (purple) are indicated. Red X indicates cessation activity, black angled arrow indicates RNA synthesis.

Treatment with IMP-1088 resulted in the expected reduced levels of Z expression, which correlated with increased levels of MG activity (Fig. 3). Treatment with MG132 restored expression levels of Z to those observed in the absence of IMP-1088, which resulted in the corresponding inhibitory effect on the activity of the LCMV MG (Fig. 3). 

Figure 3: Effect of treatments with the NMT (IMP-1088) and proteasome (MG132) inhibitors on the activity of the LCMV MG

HEK293T cells were seeded at 2x10⁵ per well in ploy-L-lysine treated M12 plate. Next day, cells were transfected with plasmids expressing LCMV L and NP proteins, required for the formation of a functional vRNP, and a plasmid directing intracellular synthesis of an LCMV MG directing expression of GFP (MG-GFP), together with incremental amounts of LCMV-Z tagged with HA (Z-WT-HA). At 18 h post-transfection, cells were treated with the indicated compounds. At 24 h post-treatment, cells were fixed with 4% PFA, and stained with anti-HA, followed by secondary fluorescence antibody to identify cells expressing the Z protein. The activity of the LCMV MG-GFP was assessed based on expression levels of GFP. Images were acquired at 4X magnification (BZ-X710 Keyence).

Future Directions

Our findings open the door to a new class of broad-spectrum anti-mammarenavirus therapy targeting host-cell lipidation processes. NMT inhibitors could be also incorporated into combination therapy strategies with direct acting antivirals, an approach expected to pose a high genetic barrier to the emergence of drug-resistant viruses, and to facilitate drug formulations with reduced toxicity. Notably, the small molecule NMT inhibitor PCLX-001 has been shown to be safe and well tolerated in humans [17,18], supporting the interest of exploring the repurposing of NMT inhibitors to treat infections by human pathogenic mammarenaviruses. NMT inhibitors have been shown to inhibit other viruses with myristoylated proteins, including picornaviruses [16] and vaccinia virus [19]. The use of specific pan-NMT inhibitors as a broad-spectrum antiviral strategy against viruses with myristoylated proteins warrants further investigation. 

For more details on the experiments and results, please refer to our paper, which can be found at https://doi.org/10.3390/v16091362.

References

1. Yadav, K.; Mathur, G.; Ford, B.; Miller, R.; Group, C.W. A Case Cluster of Lymphocytic Choriomeningitis Virus Transmitted Via Organ Transplantation.: Abstract# D2381. Transplantation 2014, 98, 768.
2. MacNeil, A.; Ströher, U.; Farnon, E.; Campbell, S.; Cannon, D.; Paddock, C.D.; Drew, C.P.; Kuehnert, M.; Knust, B.; Gruenenfelder, R.; et al. Solid Organ Transplant–Associated Lymphocytic Choriomeningitis, United States, 2011. Emerg Infect Dis 2012, 18, 1256–1262. https://doi.org/10.3201/eid1808.120212.
3. Schafer, I.J.; Miller, R.; Ströher, U.; Knust, B.; Nichol, S.T.; Rollin, P.E. A Cluster of Lymphocytic Choriomeningitis Virus Infections Transmitted Through Organ Transplantation — Iowa, 2013. MMWR Morb Mortal Wkly Rep 2014, 63, 249.
4. Carrillo-Bustamante, P.; Nguyen, T.H.T.; Oestereich, L.; Günther, S.; Guedj, J.; Graw, F. Determining Ribavirin’s Mechanism of Action against Lassa Virus Infection. Sci Rep 2017, 7, 11693. https://doi.org/10.1038/s41598-017-10198-0.
5. Perez, M.; Greenwald, D.L.; de La Torre, J.C. Myristoylation of the RING Finger Z Protein Is Essential for Arenavirus Budding. J Virol 2004, 78, 11443–11448. https://doi.org/10.1128/JVI.78.20.11443-11448.2004.
6. Capul, A.A.; Perez, M.; Burke, E.; Kunz, S.; Buchmeier, M.J.; de la Torre, J.C. Arenavirus Z-Glycoprotein Association Requires Z Myristoylation but Not Functional RING or Late Domains. J Virol 2007, 81, 9451–9460. https://doi.org/10.1128/JVI.00499-07.
7. Witwit, H.; Betancourt, C.A.; Cubitt, B.; Khafaji, R.; Kowalski, H.; Jackson, N.; Ye, C.; Martinez-Sobrido, L.; de la Torre, J.C. Cellular N-Myristoyl Transferases Are Required for Mammarenavirus Multiplication. Viruses 2024, 16, 1362. https://doi.org/10.3390/v16091362.
8. Radoshitzky, S.R., Buchmeier, M.J., de la Torre, J.C. 2022 Fields Virology: Emerging Viruses: Arenaviridae. Fields Virology, 7th Ed, Vol I: Emerging Viruses. Knipe, D.M., Howley, P.M., Whelan, S. (Eds). In.
9. Kunz, S.; Edelmann, K.H.; de la Torre, J.-C.; Gorney, R.; Oldstone, M.B.A. Mechanisms for Lymphocytic Choriomeningitis Virus Glycoprotein Cleavage, Transport, and Incorporation into Virions. Virology 2003, 314, 168–178. https://doi.org/10.1016/s0042-6822(03)00421-5.
10. Rojek, J.M.; Lee, A.M.; Nguyen, N.; Spiropoulou, C.F.; Kunz, S. Site 1 Protease Is Required for Proteolytic Processing of the Glycoproteins of the South American Hemorrhagic Fever Viruses Junin, Machupo, and Guanarito. J Virol 2008, 82, 6045–6051. https://doi.org/10.1128/JVI.02392-07.
11. Fedeli, C.; Moreno, H.; Kunz, S. Novel Insights into Cell Entry of Emerging Human Pathogenic Arenaviruses. J Mol Biol 2018, 430, 1839–1852. https://doi.org/10.1016/j.jmb.2018.04.026.
12. York, J.; Nunberg, J.H. Role of the Stable Signal Peptide of Junín Arenavirus Envelope Glycoprotein in pH-Dependent Membrane Fusion. J Virol 2006, 80, 7775–7780. https://doi.org/10.1128/JVI.00642-06.
13. York, J.; Nunberg, J.H. Myristoylation of the Arenavirus Envelope Glycoprotein Stable Signal Peptide Is Critical for Membrane Fusion but Dispensable for Virion Morphogenesis. J Virol 2016, 90, 8341–8350. https://doi.org/10.1128/JVI.01124-16.
14. Cordo, S.M.; Candurra, N.A.; Damonte, E.B. Myristic Acid Analogs Are Inhibitors of Junin Virus Replication. Microbes and Infection 1999, 1, 609–614. https://doi.org/10.1016/S1286-4579(99)80060-4.
15. Kallemeijn, W.W.; Lueg, G.A.; Faronato, M.; Hadavizadeh, K.; Goya Grocin, A.; Song, O.-R.; Howell, M.; Calado, D.P.; Tate, E.W. Validation and Invalidation of Chemical Probes for the Human N-Myristoyltransferases. Cell Chem Biol 2019, 26, 892-900.e4. https://doi.org/10.1016/j.chembiol.2019.03.006.
16. Ramljak, I.C.; Stanger, J.; Real-Hohn, A.; Dreier, D.; Wimmer, L.; Redlberger-Fritz, M.; Fischl, W.; Klingel, K.; Mihovilovic, M.D.; Blaas, D.; et al. Cellular N-Myristoyltransferases Play a Crucial Picornavirus Genus-Specific Role in Viral Assembly, Virion Maturation, and Infectivity. PLOS Pathogens 2018, 14, e1007203. https://doi.org/10.1371/journal.ppat.1007203.
17. Sangha, R.S.; Jamal, R.; Spratlin, J.L.; Kuruvilla, J.; Sehn, L.H.; Weickert, M.; Berthiaume, L.G.; Mackey, J.R. A First-in-Human, Open-Label, Phase I Trial of Daily Oral PCLX-001, an NMT Inhibitor, in Patients with Relapsed/Refractory B-Cell Lymphomas and Advanced Solid Tumors. JCO 2023, 41, e15094–e15094. https://doi.org/10.1200/JCO.2023.41.16_suppl.e15094.
18. Sangha, R.; Davies, N.M.; Namdar, A.; Chu, M.; Spratlin, J.; Beauchamp, E.; Berthiaume, L.G.; Mackey, J.R. Novel, First-in-Human, Oral PCLX-001 Treatment in a Patient with Relapsed Diffuse Large B-Cell Lymphoma. Curr Oncol 2022, 29, 1939–1946. https://doi.org/10.3390/curroncol29030158.
19. Priyamvada, L.; Kallemeijn, W.W.; Faronato, M.; Wilkins, K.; Goldsmith, C.S.; Cotter, C.A.; Ojeda, S.; Solari, R.; Moss, B.; Tate, E.W.; et al. Inhibition of Vaccinia Virus L1 N-Myristoylation by the Host N-Myristoyltransferase Inhibitor IMP-1088 Generates Non-Infectious Virions Defective in Cell Entry. PLoS Pathog 2022, 18, e1010662. https://doi.org/10.1371/journal.ppat.1010662.

We look forward to seeing you at the Asia-Pacific Congress of Medical Virology, taking place in Singapore, from 19 to 21 November 2024.

The Asia-Pacific Congress of Medical Virology (APCMV) is a triennial international meeting that focuses on diagnostic, public health, research and clinical virology, with emphasis on the Asia Pacific region. The aim of this congress is to foster collaboration and information sharing of the latest research in the field of virology pertaining to medically important viruses and treatments against them. Including the most recent COVID-19 pandemic, many emerging virus infections have been centered in the Asia Pacific region, and the breaking down of boundaries between civilization and wildlife only serves to accelerate the spread of such viruses. Therefore, it is vital for the countries in this region to develop a strong public health, diagnostic and research base to address these problems. Hence, the APCMV congress series was started to enable the review, sharing and discussion of information concerning each of these areas in order to form a strong foundation for the management of medically important viruses.

We invite you to participate in this congress. More information can be found at the following link:
https://apcmv.com/.

MDPI’s Best PhD Thesis Awards are granted to promising young scholars whose PhD theses are deemed exceptional within their respective research fields. These awards aim to encourage young scholars to continue their outstanding accomplishments and further contribute to their field.

We extend our heartfelt congratulations to the 54 winners of the 2023 Best PhD Thesis Awards and wish them success with their future research endeavors.

MDPI will continue to provide support and recognition to the academic community. To learn more about all the awardees and their research projects in your field of study, please visit the following pages:

About MDPI Awards:

To reward the academic community, especially young researchers, and enhance communication among scientists, MDPI journals regularly offer various awards to researchers in specific fields. These awards, serving as a source of inspiration and recognition, help raise the influence of talented individuals who have been credited with outstanding achievements and are making a significant contribution to the advancement of their fields.

To explore more MDPI awards, please click here.

“Longitudinal Analysis of Coronavirus-Neutralizing Activity in COVID-19 Patients”
by Florian D. Hastert, Lisa Henss, Christine von Rhein, Julia Gerbeth, Imke Wieters, Frauke Borgans, Yascha Khodamoradi, Kai Zacharowski, Gernot Rohde, Maria J.G.T. Vehreschild et al.
Viruses 2022, 14(5), 882; https://doi.org/10.3390/v14050882
Available online: https://www.mdpi.com/1999-4915/14/5/882

“Evolution of Anti-RBD IgG Avidity following SARS-CoV-2 Infection”
by Alexandra Tauzin, Gabrielle Gendron-Lepage, Manon Nayrac, Sai Priya Anand, Catherine Bourassa, Halima Medjahed, Guillaume Goyette, Mathieu Dubé, Renée Bazin, Daniel E. Kaufmann et al.
Viruses 2022, 14(3), 532; https://doi.org/10.3390/v14030532
Available online: https://www.mdpi.com/1999-4915/14/3/532

“Early Emergence Phase of SARS-CoV-2 Delta Variant in Florida, US”
by Eleonora Cella, Sobur Ali, Sarah E. Schmedes, Brittany Rife Magalis, Simone Marini, Marco Salemi, Jason Blanton and Taj Azarian
Viruses 2022, 14(4), 766; https://doi.org/10.3390/v14040766
Available online: https://www.mdpi.com/1999-4915/14/4/766

“Unique Aggregation of Retroviral Particles Pseudotyped with the Delta Variant SARS-CoV-2 Spike Protein”
by Jennifer D. Petersen, Jianming Lu, Wendy Fitzgerald, Fei Zhou, Paul S. Blank, Doreen Matthies and Joshua Zimmerberg
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Available online: https://www.mdpi.com/1999-4915/14/5/1024

“Duplex One-Step RT-qPCR Assays for Simultaneous Detection of Genomic and Subgenomic RNAs of SARS-CoV-2 Variants”
by Sushma M. Bhosle, Julie P. Tran, Shuiqing Yu, Jillian Geiger, Jennifer D. Jackson, Ian Crozier, Anya Crane, Jiro Wada, Travis K. Warren, Jens H. Kuhn et al.
Viruses 2022, 14(5), 1066; https://doi.org/10.3390/v14051066
Available online: https://www.mdpi.com/1999-4915/14/5/1066