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Article

Herpes Simplex 2 Virus Depletes Cells of DEAD-Box Helicase 3 Protein by Packaging It into Virions

by
Carmen Rita Piazza
1,†,
Giulia Lottini
1,2,†,
Paola Quaranta
1,†,
Paola Perrera
1,
Fabio Filippini
1,
Michele Lai
1,
Cristina Di Primio
3,
Giulia Freer
1,*,† and
Mauro Pistello
1,2,†
1
Retrovirus Center, Department of Translational Medicine and New Technologies in Medicine and Surgery, University of Pisa, 56127 Pisa, Italy
2
Virology Unit, Pisa University Hospital, 56127 Pisa, Italy
3
Institute of Neuroscience, National Research Council of Italy, 56127 Pisa, Italy
*
Author to whom correspondence should be addressed.
†
These authors contributed equally to this work.
Viruses 2025, 17(8), 1124; https://doi.org/10.3390/v17081124
Submission received: 6 June 2025 / Revised: 5 August 2025 / Accepted: 13 August 2025 / Published: 15 August 2025
(This article belongs to the Section Animal Viruses)
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Abstract

Human DEAD-box helicase 3 (DDX3) is a multifunctional RNA helicase implicated in mRNA unwinding and the regulation of gene expression. While DDX3 has been extensively studied in the context of RNA virus replication, its role in DNA virus replication remains less understood. In this study, we explore the involvement of DDX3 in the life cycle of Herpes Simplex Virus type 2 (HSV-2), a double-stranded DNA virus. Silencing of DDX3 expression with siRNA significantly impaired HSV-2 replication, indicating that DDX3 supports viral propagation. Unexpectedly, HSV-2 infection led to a marked reduction in cellular DDX3 protein levels during in vitro replication in human cells, particularly at 24 h post-infection, corresponding to the peak of viral production. Notably, this decrease was not accompanied by a reduction in DDX3 mRNA levels, nor was it prevented by proteasome inhibition, suggesting an alternative mechanism of DDX3 depletion. Further analysis revealed substantial amounts of DDX3 protein within HSV-2 virions, supporting the hypothesis that DDX3 is packaged into viral particles during replication. We propose that HSV-2 exploits host DDX3 by incorporating it into progeny virions to facilitate early stages of infection in newly infected cells. However, no evidence linking DDX3 to the assembly process of HSV-2 particles was found. These findings expand the known functional repertoire of DDX3 and highlight its potential as a host factor co-opted by DNA viruses, suggesting a broader relevance in antiviral strategies.
Keywords: DEAD-box protein-3; herpes simplex virus 2; host factors for viral replication DEAD-box protein-3; herpes simplex virus 2; host factors for viral replication

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MDPI and ACS Style

Piazza, C.R.; Lottini, G.; Quaranta, P.; Perrera, P.; Filippini, F.; Lai, M.; Di Primio, C.; Freer, G.; Pistello, M. Herpes Simplex 2 Virus Depletes Cells of DEAD-Box Helicase 3 Protein by Packaging It into Virions. Viruses 2025, 17, 1124. https://doi.org/10.3390/v17081124

AMA Style

Piazza CR, Lottini G, Quaranta P, Perrera P, Filippini F, Lai M, Di Primio C, Freer G, Pistello M. Herpes Simplex 2 Virus Depletes Cells of DEAD-Box Helicase 3 Protein by Packaging It into Virions. Viruses. 2025; 17(8):1124. https://doi.org/10.3390/v17081124

Chicago/Turabian Style

Piazza, Carmen Rita, Giulia Lottini, Paola Quaranta, Paola Perrera, Fabio Filippini, Michele Lai, Cristina Di Primio, Giulia Freer, and Mauro Pistello. 2025. "Herpes Simplex 2 Virus Depletes Cells of DEAD-Box Helicase 3 Protein by Packaging It into Virions" Viruses 17, no. 8: 1124. https://doi.org/10.3390/v17081124

APA Style

Piazza, C. R., Lottini, G., Quaranta, P., Perrera, P., Filippini, F., Lai, M., Di Primio, C., Freer, G., & Pistello, M. (2025). Herpes Simplex 2 Virus Depletes Cells of DEAD-Box Helicase 3 Protein by Packaging It into Virions. Viruses, 17(8), 1124. https://doi.org/10.3390/v17081124

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