Host–Viral Protein Interactions and Post-translational Modifications in Viral Infections

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

Deadline for manuscript submissions: 31 August 2024 | Viewed by 383

Special Issue Editor

1. Department of Bioengineering, College of Engineering, Bourns College of Engineering, University of California at Riverside, Riverside, CA 92521, USA
2. Biomedical Science, School of Medicine, University of California at Riverside, Riverside, CA 92521, USA
3. Institute for Integrative Genome Biology, Department of Biochemistry, University of California at Riverside, Riverside, CA 92521, USA
Interests: post-translational modification; nucleocapsid protein; SUMOylation pathway; protein interaction affinity; influenza B virus; SARS-CoV-2
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Special Issue Information

Dear Colleagues,

Viruses need to engage host factors to infect, replicate and assemble new pathogens. Several genome-wide siRNA or CRISPR screening studies have also identified that host factors are critical for virus infection and growth. In addition, post-translation modifications (PTMs), such as phosphorylation, ubiquitylation and SUMOylation, have been discovered to be critical for many virus life cycles. For example, Ebola, CMV and EMCV utilize SUMOylation to inhibit anti-viral intrinsic and innate immunity via, e.g., reducing interferon production and inhibiting STAT1/3, PML, IRFs and NFkB. SARS-CoV-2 also inhibits the host IFN signaling pathway to repress the host immune response for its replication. Furthermore, many viral infections and replications can manipulate the host factors to ensure their propagation and survival. Herpes simplex virus-1 (HSV-1) infection results in a three-fold decrease in the modification of over 100 cellular proteins, including antiviral promyelocytic leukemia (PML) nuclear bodies. Therapeutics targeting host–virus interactions could potentially present a potential effective and broad-spectrum treatment modality for viruses such as COVID-19 and influenzas, as exemplified in the cases of methylprednisolone and rSIFN-co with even more potential benefits, such as an anti-coinfections effect. A comprehensive understanding of host–virus protein interactions and modifications in viral infection would significantly improve our knowledge and approaches against viral infections and novel therapeutic development.

Dr. Jiayu Liao
Guest Editor

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Keywords

  • host–virus interactions
  • protein post-translational modifications
  • viral manipulation of host immune system
  • therapeutics targeting host–viral interactions

Published Papers (1 paper)

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Research

14 pages, 3734 KiB  
Article
HACD3 Prevents PB1 from Autophagic Degradation to Facilitate the Replication of Influenza A Virus
by Qibing Li, Li Jiang, Yihan Wang, Xuwei Liu, Bo Wang, Zhibo Shan, Yi-Han Wang, Yuqin Wang, Hualan Chen and Chengjun Li
Viruses 2024, 16(5), 702; https://doi.org/10.3390/v16050702 (registering DOI) - 29 Apr 2024
Viewed by 249
Abstract
Influenza A virus (IAV) continues to pose serious threats to the global animal industry and public health security. Identification of critical host factors engaged in the life cycle of IAV and elucidation of the underlying mechanisms of their action are particularly important for [...] Read more.
Influenza A virus (IAV) continues to pose serious threats to the global animal industry and public health security. Identification of critical host factors engaged in the life cycle of IAV and elucidation of the underlying mechanisms of their action are particularly important for the discovery of potential new targets for the development of anti-influenza drugs. Herein, we identified Hydroxyacyl-CoA Dehydratase 3 (HACD3) as a new host factor that supports the replication of IAV. Downregulating the expression of HACD3 reduced the level of viral PB1 protein in IAV-infected cells and in cells that were transiently transfected to express PB1. Silencing HACD3 expression had no effect on the level of PB1 mRNA but could promote the lysosome-mediated autophagic degradation of PB1 protein. Further investigation revealed that HACD3 interacted with PB1 and selective autophagic receptor SQSTM1/p62, and HACD3 competed with SQSTM1/p62 for the interaction with PB1, which prevented PB1 from SQSTM1/p62-mediated autophagic degradation. Collectively, these findings establish that HACD3 plays a positive regulatory role in IAV replication by stabilizing the viral PB1 protein. Full article
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