Veterinary Virology: Unraveling Host–Pathogen Interactions for Animal Health

A special issue of Viruses (ISSN 1999-4915). This special issue belongs to the section "Animal Viruses".

Deadline for manuscript submissions: 28 February 2026 | Viewed by 593

Special Issue Editor


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Guest Editor
College of Veterinary Medicine, Murdoch University, Murdoch 6150, Australia
Interests: veterinary virology; host–pathogen interactions; molecular and genomic virology; veterinary infectious diseases; viral Immune evasion; livestock viral disease control
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Special Issue Information

Dear Colleagues,

Veterinary virology plays a critical role in safeguarding animal health by uncovering the complex interactions between viral pathogens and their animal hosts. Understanding these host–pathogen dynamics provides essential insights into viral transmission, replication, immune evasion strategies, and disease progression. Such knowledge is vital for the development of effective diagnostics, vaccines, and therapeutic interventions to control viral diseases in livestock, wildlife, and companion animals. Additionally, with many animal viruses posing zoonotic threats, virus–host interactions contribute significantly to One Health initiatives, bridging animal and human health. This Special Issue will highlight advances in virus–host interactions, showcasing molecular virology, genomics, and immunology, and how this knowledge is enhancing our ability to predict outbreaks, manage emerging and reemerging viral threats, and improve overall animal welfare and productivity.

Dr. Muhammad Jasim Uddin
Guest Editor

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Keywords

  • veterinary virology
  • host–pathogen interactions
  • viral replication and immune evasion
  • zoonotic viruses
  • One Health
  • vaccine and therapeutic development
  • molecular virology and genomics
  • emerging and re-emerging viral pathogens or diseases
  • animal health and welfare
  • high-throughput or deep sequencing
  • outbreak prevention and control
  • food security

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Published Papers (1 paper)

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Research

17 pages, 1606 KB  
Article
Structural Insights into the Nuclear Import of Haliotid Herpesvirus 1 Large Tegument Protein Homologue
by Babu Kanti Nath, Crystall M. D. Swarbrick, Renate H. M. Schwab, Daryl Ariawan, Ole Tietz, Jade K. Forwood and Subir Sarker
Viruses 2025, 17(9), 1279; https://doi.org/10.3390/v17091279 - 20 Sep 2025
Viewed by 403
Abstract
Abalone are highly susceptible to haliotid herpesvirus 1 (HaHV1), the causative agent of abalone viral ganglioneuritis (AVG), a re-emerging disease responsible for significant mortality events in both wild and farmed populations. Currently, there are no effective antiviral treatments or preventive measures available against [...] Read more.
Abalone are highly susceptible to haliotid herpesvirus 1 (HaHV1), the causative agent of abalone viral ganglioneuritis (AVG), a re-emerging disease responsible for significant mortality events in both wild and farmed populations. Currently, there are no effective antiviral treatments or preventive measures available against HaHV1, which is partly due to the limited understanding of the immune responses and viral pathogenesis in this non-model marine invertebrate. This highlights the urgent need for novel intervention strategies, including investigations into the molecular mechanisms underlying HaHV1 infection. In other herpesviruses, the large tegument protein UL36 plays a crucial role in transporting the viral capsid to the host cell’s nuclear pore complex (NPC), mediated by N-terminal nuclear localization signals (NLSs). However, the nuclear import mechanism of UL36 homologue (UL36h) in HaHV1 remains largely uncharacterized. In this study, we identified and functionally characterized the NLS motif within HaHV1 UL36h and elucidated its interactions with the importin alpha (IMPα) nuclear import receptor. Through a combination of high-resolution crystallography and quantitative binding assays, we determined the key residues responsible for binding to IMPα and demonstrated isoform-specific variations in binding affinity. Our biochemical and structural analyses confirmed key interactions within the NLS that are essential for IMPα interactions. These findings advance our molecular understanding of HaHV1 host interactions and pave the way for the development of targeted antiviral strategies against abalone herpesvirus infection. Full article
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