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Animal Viruses Molecular Biology
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Animal Viruses Molecular Biology

A special issue of Genes (ISSN 2073-4425). This special issue belongs to the section "Viral Genomics".

Deadline for manuscript submissions: closed (20 June 2024) | Viewed by 2794

Special Issue Editors

Prof. Dr. Xiaofeng Guo

E-Mail Website
Guest Editor
College of Veterinary Medicine, South China Agricultural University, Guangzhou 510642, China
Interests: pathogenicity and immunity of zoonotic virus; development of animal vaccines; high expression of virus protein
Dr. Jun Luo

E-Mail Website
Guest Editor
College of Veterinary Medicine, South China Agricultural University, Guangzhou 510642, China
Interests: animal virus vaccines; new antiviral compounds; epidemiology; diagnosis

Special Issue Information

Dear Colleagues, 

The aim of this Special Issue is to share the latest research on the genetic, immunogenicity, diagnosis and pathogenicity of animal viruses and zoonotic viruses. Studies are welcome that cover topics including animal virus genes and structural protein function, non-coding gene regulation of virus replication, interaction between the virus and host protein, the mechanism of the virus escaping from host immunity, new antiviral compounds, new molecular diagnostic methods of virus and new viral vaccines.

Prof. Dr. Xiaofeng Guo
Dr. Jun Luo
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 100 words) can be sent to the Editorial Office for announcement on this website.

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-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Genes 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

  • animal viruses

  • zoonotic viruses
  • function of genes
  • pathogenicity
  • immunity
  • vaccines

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Published Papers (2 papers)

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Research

14 pages, 4172 KiB  
Article
Network of Interactions between the Mut Domains of the E2 Protein of Atypical Porcine Pestivirus and Host Proteins
by Yuai Yang, Guangfei Jiang, Weiqi He, Xin Tian, Huanli Zheng, Bin Xiang and Yongke Sun
Genes 2024, 15(8), 991; https://doi.org/10.3390/genes15080991 - 27 Jul 2024
Viewed by 462
Abstract
Atypical porcine pestivirus (APPV) can cause congenital tremor type A-II in neonatal piglets, posing a significant threat to swine herd health globally. Our previous study demonstrated that the Mut domains, comprising 112 amino acids at the N-terminus, are the primary functional regions of [...] Read more.
Atypical porcine pestivirus (APPV) can cause congenital tremor type A-II in neonatal piglets, posing a significant threat to swine herd health globally. Our previous study demonstrated that the Mut domains, comprising 112 amino acids at the N-terminus, are the primary functional regions of the E2 protein of APPV. This study identified 14 host cellular proteins that exhibit potential interactions with the Mut domains of the E2 protein using yeast two-hybrid screening. Using bioinformatics analysis, we discovered that the Mut domains of the E2 protein might exert regulatory effects on apoptosis by modulating energy metabolism within the mitochondria. We also conducted co-immunoprecipitation, glutathione S-transferase pull-down, and immunofluorescence assays to confirm the interaction between the Mut domains of the E2 protein and cathepsin H and signal sequence receptor subunit 4 (SSR4). Ultimately, SSR4 enhanced APPV replication in vitro. In summary, our study successfully elucidated the interactions between the Mut domains of the E2 protein and host cell protein, predicted the potential pathways implicated in these interactions, and demonstrated SSR4 involvement in APPV infection. These significant findings contribute valuable knowledge toward a deeper understanding of APPV pathogenesis and the role of the Mut domains of the E2 protein in this intricate process. Full article
(This article belongs to the Special Issue Animal Viruses Molecular Biology)
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14 pages, 4118 KiB  
Article
TRIM25 Suppresses Rabies Virus Fixed HEP-Flury Strain Production by Activating RIG-1-Mediated Type I Interferons
by Boyue Zhang, Ting Cai, Hongling He, Xuezhe Huang, Yongwen Luo, Shile Huang, Jun Luo and Xiaofeng Guo
Genes 2023, 14(8), 1555; https://doi.org/10.3390/genes14081555 - 29 Jul 2023
Cited by 5 | Viewed by 1865
Abstract
Rabies remains a great threat to public health worldwide. So far, the mechanism of rabies virus (RABV) infection is not fully understood, and there is no effective treatment for rabies. Identifying more host restriction factors of RABV will spur the development of novel [...] Read more.
Rabies remains a great threat to public health worldwide. So far, the mechanism of rabies virus (RABV) infection is not fully understood, and there is no effective treatment for rabies. Identifying more host restriction factors of RABV will spur the development of novel therapeutic interventions against rabies. Accumulating studies suggest that tripartite motif-containing (TRIM) proteins have great effects on virus replication. TRIMs control the antiviral responses through either direct interaction with viral proteins or indirect regulation of innate immune signaling molecules in the host. The role of TRIM25 in rabies virus (RABV) infection is poorly understood. Using next-generation sequencing, we found that TRIM25 is upregulated during HEP-Flury infection. Knockdown of TRIM25 enhances HEP-Flury production, while overexpression of TRIM25 suppresses HEP-Flury replication. Knockdown of interferon α and interferon β weakens the anti-RABV response induced by TRIM25 overexpression, and potentiates RABV production. Furthermore, we found that TRIM25 regulates type-I interferon response by targeting retinoic acid-inducible gene I (RIG-I) during HEP-Flury infection. Knockdown of RIG-I weakens the anti-HEP-Flury response induced by TRIM25 overexpression, indicating that TRIM25 regulates RABV production via the RIG-I-IFN axis. In addition, we observed that TRIM25 does not directly interact with HEP-Flury structural proteins, suggesting that TRIM25 regulates HEP-Flury production indirectly. Taken together, our work identifies TRIM25 as a new host factor involved in HEP-Flury infection, which may be a potential target for the development of antiviral drugs against RABV. Full article
(This article belongs to the Special Issue Animal Viruses Molecular Biology)
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