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Viruses
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Interplay Between Influenza Virus and Host Factors
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Interplay Between Influenza Virus and Host Factors

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

Deadline for manuscript submissions: 31 December 2025 | Viewed by 4316

Special Issue Editor

Dr. Matloob Husain

E-Mail Website
Guest Editor
Department of Microbiology and Immunology, University of Otago, Dunedin 9054, New Zealand
Interests: molecular virology; influenza virus; viral pathogenesis; virus–host interactions; innate antiviral response; post-translational protein modifications; protein trafficking; acetylation; HDACs; HATs
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Influenza virus has posed a challenge to global public health for centuries and will continue to do so for the foreseeable future due to its genetic makeup, diversity, and broad host range. Influenza virus is an obligate intracellular pathogen and interacts with numerous host factors to complete its life cycle in the host. These interactions are both exploitative and antagonistic and contribute to the host adaptation and disease severity of influenza virus. Hence, the host factors involved in the life cycle of influenza virus may be divided into two categories—proviral and antiviral—even if some host factors might play a dual role. Influenza virus utilizes all three main parts—plasma membrane, cytoplasm, and nucleus—of a host cell to complete its life cycle. Influenza virus continues to be the subject of extensive research, and new findings on the interplay between influenza virus and host factors continue to be demonstrated. A detailed understanding of the interplay between influenza virus and host factors is key in elucidating the mechanisms of viral pathogenesis and design-targeted antiviral strategies. This Special Issue of Viruses invites articles reporting the latest research developments in this exciting area of influenza virus research.

Dr. Matloob Husain
Guest Editor

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. 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

  • influenza virus
  • host factors
  • proviral host factors
  • antiviral host factors
  • host adaptation
  • virus entry
  • virus assembly
  • virus release
  • innate antiviral response
  • interferon-stimulated genes
  • post-translational protein modifications

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Published Papers (3 papers)

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Research

25 pages, 3522 KiB  
Article
Repurposing of Some Nucleoside Analogs Targeting Some Key Proteins of the Avian H5N1 Clade 2.3.4.4b to Combat the Circulating HPAI in Birds: An In Silico Approach
by Mohd Yasir Khan, Abid Ullah Shah, Nithyadevi Duraisamy, Mohammed Cherkaoui and Maged Gomaa Hemida
Viruses 2025, 17(7), 972; https://doi.org/10.3390/v17070972 - 10 Jul 2025
Viewed by 557
Abstract
(1) Background: The highly pathogenic avian influenza virus H5N1 clade 2.3.4.4b is an emerging threat that poses a great risk to the poultry industry. A few human cases have been linked to the infection with this clade in many parts of the world, [...] Read more.
(1) Background: The highly pathogenic avian influenza virus H5N1 clade 2.3.4.4b is an emerging threat that poses a great risk to the poultry industry. A few human cases have been linked to the infection with this clade in many parts of the world, including the USA. Unfortunately, there are no specific vaccines or antiviral drugs that could help prevent and treat the infection caused by this virus in birds. Our major objective is to identify/repurpose some (novel/known) antiviral compounds that may inhibit viral replication by targeting some key viral proteins. (2) Methods: We used state-of-the-art machine learning tools such as molecular docking and MD-simulation methods from Biovia Discovery Studio (v24.1.0.321712). The key target proteins such as hemagglutinin (HA), neuraminidase (NA), Matrix-2 protein (M2), and the cap-binding domain of PB2 (PB2/CBD) homology models were validated through structural assessment via DOPE scores, Ramachandran plots, and Verify-3D metrics, ensuring reliable structural representations, confirming their reliability for subsequent in silico approaches. These approaches include molecular docking followed by molecular dynamics simulation for 50 nanoseconds (ns), highlighting the structural stability and compactness of the docked complexes. (3) Results: Molecular docking revealed strong binding affinities for both sofosbuvir and GS441524, particularly with the NA and PB2/CBD protein targets. Among them, GS441524 exhibited superior interaction scores and a greater number of hydrogen bonds with key functional residues of NA and PB2/CBD. The MM-GBSA binding free energy calculations further supported these findings, as GS441524 displayed more favorable binding energies compared to several known standard inhibitors, including F0045S for HA, Zanamivir for NA, Rimantadine and Amantadine for M2, and PB2-39 for PB2/CBD. Additionally, 50 ns molecular dynamics simulations highlighted the structural stability and compactness of the GS441524-PB2/CBD complex, further supporting its potential as a promising antiviral candidate. Furthermore, hydrogen bond monitor analysis over the 50 ns simulation confirmed persistent and specific interactions between the ligand and proteins, suggesting that GS441524 may effectively inhibit the NA, and PB2/CBD might potentially disrupt PB2-mediated RNA synthesis. (4) Conclusions: Our findings are consistent with previous evidence supporting the antiviral activity of certain nucleoside analog inhibitors, including GS441524, against various coronaviruses. These results further support the potential repurposing of GS441524 as a promising therapeutic candidate against H5N1 avian influenza clade 2.3.4.4b. However, further functional studies are required to validate these in silico predictions and support the inhibitory action of GS441524 against the targeted proteins of H5N1, specifically clade 2.3.4.4b. Full article
(This article belongs to the Special Issue Interplay Between Influenza Virus and Host Factors)
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15 pages, 4063 KiB  
Article
HDAC1 and HDAC2 Are Involved in Influenza A Virus-Induced Nuclear Translocation of Ectopically Expressed STAT3-GFP
by Jessica Leong and Matloob Husain
Viruses 2025, 17(1), 33; https://doi.org/10.3390/v17010033 - 29 Dec 2024
Cited by 1 | Viewed by 1349
Abstract
Influenza A virus (IAV) remains a pandemic threat. Particularly, the evolution and increased interspecies and intercontinental transmission of avian IAV H5N1 subtype highlight the importance of continuously studying the IAV and identifying the determinants of its pathogenesis. Host innate antiviral response is the [...] Read more.
Influenza A virus (IAV) remains a pandemic threat. Particularly, the evolution and increased interspecies and intercontinental transmission of avian IAV H5N1 subtype highlight the importance of continuously studying the IAV and identifying the determinants of its pathogenesis. Host innate antiviral response is the first line of defense against IAV infection, and the transcription factor, the signal transducer and activator of transcription 3 (STAT3), has emerged as a critical component of this response. Also, histone deacetylase 1 (HDAC1) and HDAC2 have been identified as important components of IAV-induced host innate antiviral response. Upon IAV infection, STAT3 is activated and translocated to the nucleus to initiate the transcription of innate response genes. Also, the HDAC1 and HDAC2 are localized to the nucleus. In this study, we sought to investigate the role of HDAC1 and HDAC2 in IAV-induced STAT3 nuclear translocation. We employed a quantitative confocal microscopy approach and analyzed the nuclear translocation of plasmid-expressed STAT3-GFP in IAV-infected cells depleted with the expression of HDAC1 or HDAC2. We found that the depletion of both HDAC1 and HDAC2 expression inhibits the IAV-induced nuclear translocation of STAT3-GFP. These findings will help elucidate the significance of the emerging role of acetylation in IAV infection and disease severity. Full article
(This article belongs to the Special Issue Interplay Between Influenza Virus and Host Factors)
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12 pages, 4711 KiB  
Article
Functional Analysis of GRSF1 in the Nuclear Export and Translation of Influenza A Virus mRNAs
by Jordana Schmierer and Toru Takimoto
Viruses 2024, 16(7), 1136; https://doi.org/10.3390/v16071136 - 16 Jul 2024
Viewed by 1734
Abstract
Influenza A viruses (IAV) utilize host proteins throughout their life cycle to infect and replicate in their hosts. We previously showed that host adaptive mutations in avian IAV PA help recruit host protein G-Rich RNA Sequence Binding Factor 1 (GRSF1) to the nucleoprotein [...] Read more.
Influenza A viruses (IAV) utilize host proteins throughout their life cycle to infect and replicate in their hosts. We previously showed that host adaptive mutations in avian IAV PA help recruit host protein G-Rich RNA Sequence Binding Factor 1 (GRSF1) to the nucleoprotein (NP) 5’ untranslated region (UTR), leading to the enhanced nuclear export and translation of NP mRNA. In this study, we evaluated the impact of GRSF1 in the viral life cycle. We rescued and characterized a 2009 pH1N1 virus with a mutated GRSF1 binding site in the 5’ UTR of NP mRNA. Mutant viral growth was attenuated relative to pH1N1 wild-type (WT) in mammalian cells. We observed a specific reduction in the NP protein production and cytosolic accumulation of NP mRNAs, indicating a critical role of GRSF1 in the nuclear export of IAV NP mRNAs. Further, in vitro-transcribed mutated NP mRNA was translated less efficiently than WT NP mRNA in transfected cells. Together, these findings show that GRSF1 binding is important for both mRNA nuclear export and translation and affects overall IAV growth. Enhanced association of GRSF1 to NP mRNA by PA mutations leads to rapid virus growth, which could be a key process of mammalian host adaptation of IAV. Full article
(This article belongs to the Special Issue Interplay Between Influenza Virus and Host Factors)
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