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Viruses
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Intrinsic Immunity vs. Viral Antagonism: Which One Bites the Dust?
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Intrinsic Immunity vs. Viral Antagonism: Which One Bites the Dust?

A Special Issue of Viruses (ISSN 1999-4915) belonging to the section "Viral Immunology, Vaccines, and Antivirals".

Deadline for manuscript submissions: 31 January 2027 | Viewed by 1432

Editors

Dr. Akatsuki Saito

E-Mail Website
Guest Editor
Department of Veterinary Medicine, Faculty of Agriculture, University of Miyazaki, Miyazaki 889-2192, Japan
Interests: viral–host interplay; evolutionary arms race; species barriers
Dr. Kenzo Tokunaga

E-Mail Website
Guest Editor
Department of Pathology, National Institute of Infectious Diseases, Tokyo 162-8640, Japan
Interests: retrovirology; host–virus interactions; membrane trafficking
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

This Special Issue invites mechanistic studies on intrinsic immunity and viral antagonism during the viral replication cycle. We welcome papers that define the balance between these processes at membranes, in the cytoplasm, and in the nucleus, and their consequences for fusion and entry, intracellular trafficking, genome delivery, gene expression, assembly, release, and cell-to-cell spread. Areas of interest include ubiquitin and trafficking pathways, envelope glycoprotein downregulation, capsid sensing, nucleic acid editing and metabolism, epigenetic silencing, and interferon-inducible pathways.

We particularly invite work on APOBEC3, TRIM family members, BST-2/tetherin, SAMHD1, MX2, SERINC5, MARCH8, IFITMs, GBP5, Smc5/6, and related factors, together with viral antagonists such as Vif, Vpu, Nef, Vpx, HBx, and counterparts in other viruses. Comparative and evolutionary analyses that clarify species barriers and zoonotic potential are encouraged. Suitable approaches range from standard methods (transfection, infection/transduction, reporter assays, protein expression, and mutagenesis) to advanced techniques, including CRISPR screening and genome editing, proteomics, structural analyses, single-cell and spatial analyses, live-cell imaging, and organoid systems.

Original research, reviews, short communications, and methods papers are welcome.

Dr. Akatsuki Saito
Dr. Kenzo Tokunaga
Guest Editors

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 250 words) can be sent to the Editorial Office for assessment.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-anonymized peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Viruses is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2600 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • host restriction factors
  • viral antagonists
  • replication cycle
  • interferon-inducible pathways
  • ubiquitination
  • membrane trafficking

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Published Papers (2 papers)

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Research

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19 pages, 5783 KB  
Article
TRIM21 Neutralizes Hazara Virus Using a Dual Mechanism of Nucleoprotein Caging and Ubiquitination
by Aminu S. Jahun, Boglarka A. Vamos, Anna Albecka, Marina Vaysburd, David Hawman and Leo C. James
Viruses 2026, 18(9), 974; https://doi.org/10.3390/v18090974 - 4 Sep 2026
Viewed by 197
Abstract
Crimean–Congo Hemorrhagic Fever Virus (CCHFV) is a tick-borne bunyavirus with widespread and growing geographic distribution that causes severe hemorrhagic fever and death. Vaccine candidates targeting the viral nucleoprotein (NP) have shown efficacy in both mouse and non-human primate models but the mechanism of [...] Read more.
Crimean–Congo Hemorrhagic Fever Virus (CCHFV) is a tick-borne bunyavirus with widespread and growing geographic distribution that causes severe hemorrhagic fever and death. Vaccine candidates targeting the viral nucleoprotein (NP) have shown efficacy in both mouse and non-human primate models but the mechanism of protection is unclear. Here we employ the closely related Hazara virus (HAZV) to investigate how the intracellular antibody receptor TRIM21 uses anti-NP antibodies to neutralize infection. We show that TRIM21 can detect incoming NP particles within hours of infection and that this results in a potent block to infection. Electroporated-antibody-dependent neutralization assay (EDNA) experiments reveal that TRIM21 inhibits viral transcription, protein expression and genome synthesis and reduces the production of infectious virions. Mutations and domain deletions within TRIM21 reveal that neutralization requires antibody-binding by the PRYSPRY domain but is only partially dependent on the E3 ubiquitin ligase RING domain. The data suggest a dual restriction mechanism in which NP cross-linking by TRIM21 physically interferes with NP function whilst parallel ubiquitination labels the protein for degradation. This dual mechanism is similar to that used by TRIM5 against retroviruses and suggests that antiviral TRIMs may utilize their capacity for self-assembly both for catalytic activation and viral caging. Full article
(This article belongs to the Special Issue Intrinsic Immunity vs. Viral Antagonism: Which One Bites the Dust?)
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Review

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12 pages, 15302 KB  
Review
Structural Basis of Intermolecular Interactions Between APOBEC3 and HIV-1 Vif
by Hirotaka Ode and Yasumasa Iwatani
Viruses 2026, 18(7), 787; https://doi.org/10.3390/v18070787 - 19 Jul 2026
Viewed by 574
Abstract
The human APOBEC3 (A3) family of cytidine deaminases, including A3G, A3F, and A3H, participates in cellular anti-retroviral immunity. In contrast, to antagonize the anti-retroviral activities of these A3 family proteins, HIV-1 produces its gene product called viral infectivity factor (Vif) in infected cells. [...] Read more.
The human APOBEC3 (A3) family of cytidine deaminases, including A3G, A3F, and A3H, participates in cellular anti-retroviral immunity. In contrast, to antagonize the anti-retroviral activities of these A3 family proteins, HIV-1 produces its gene product called viral infectivity factor (Vif) in infected cells. Vif is a pleiotropic hub protein that specifically binds to various A3 proteins with the aid of host core-binding factor subunit β (CBF-β) and mediates their proteasomal degradation. To date, numerous biological and structural studies have been performed to understand the arms race between A3 and Vif. Previous extensive mutagenesis and structural analyses have suggested that there are three distinct types of Vif-binding interfaces among human A3s and three largely nonoverlapping interfaces on Vif for binding with these A3s. Moreover, recent cryo-electron microscopy (cryo-EM) structural analyses have clarified further details of the different intermolecular interactions of Vif with each of three human A3s (A3G, A3F, and A3H) and have proposed a possible mechanism by which one Vif molecule can recognize all three types of A3s. In this review, we summarize the current understanding of the structural basis of the interaction between A3 and Vif. This information may be helpful for developing drugs targeting these interfaces. Full article
(This article belongs to the Special Issue Intrinsic Immunity vs. Viral Antagonism: Which One Bites the Dust?)
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