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Antiviral Strategies Targeting Capsid Proteins: Intervention from Assembly to Function
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Antiviral Strategies Targeting Capsid Proteins: Intervention from Assembly to Function

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Macromolecules".

Deadline for manuscript submissions: 20 December 2025 | Viewed by 1569

Special Issue Editor

Prof. Dr. Yuqing Wu

E-Mail Website
Guest Editor
State Key Laboratory of Supramolecular Structure and Materials, Institute of Theoretical Chemistry, College of Chemistry, Jilin University, Changchun 130012, China
Interests: supramolecular assembly; spectroscopic techniques; subtle structural variation
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

The COVID-19 pandemic has significantly impacted the pharmaceutical market globally, leading to a more urgent demand for antiviral strategies to effectively combat virus variants or drug resistance. Virus capsid proteins play crucial roles, including structural stability, gene encapsulation, and immunogenicity in the lifecycle, offering a novel target for vaccine design and therapeutic strategies. The win of the capsid-targeting anti-HIV drug, lenacapavir, at the Breakthrough of the Year of 2024 in Science will powerfully elicit improvements in global research in this field. Understanding the mechanism underlying and revealing active sites in viral capsid are of paramount importance for the development of antiviral therapeutics. The power to disrupt capsid or the formation of the oligomer holds great potential in inhibiting viral replication and/or function, thereby serving as a promising strategy in antiviruses. This comprehensive Special Issue aims to provide valuable insights not only in the form of novel experiments but also computer-aided molecular design on capsid assembly interventions, as well as the reveal of new active sites in versatile capsid proteins, for antiviral approaches.

Prof. Dr. Yuqing Wu
Guest Editor

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Keywords

  • viral capsid protein
  • assembly modulator/intervention
  • virus variants
  • antiviral therapeutics
  • assembly–disassembly

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Published Papers (2 papers)

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26 pages, 14037 KiB  
Article
Nuclear Fraction Proteome Analyses During rAAV Production of AAV2-Plasmid-Transfected HEK-293 Cells
by Susanne K. Golm, Raimund Hoffrogge and Kristian M. Müller
Int. J. Mol. Sci. 2025, 26(13), 6315; https://doi.org/10.3390/ijms26136315 - 30 Jun 2025
Viewed by 598
Abstract
Recombinant adeno-associated virus (rAAV) is the leading vector for gene replacement therapy; however, the roles and regulation of host proteins in rAAV production remain incompletely understood. In this comparative proteomic analysis, we focused on proteins in the nucleus, the epicenter of DNA uptake, [...] Read more.
Recombinant adeno-associated virus (rAAV) is the leading vector for gene replacement therapy; however, the roles and regulation of host proteins in rAAV production remain incompletely understood. In this comparative proteomic analysis, we focused on proteins in the nucleus, the epicenter of DNA uptake, transcription, capsid assembly, and packaging. HEK-293 cells were analyzed under the following three conditions: (i) untransfected, (ii) mock-transfected with the ITR and an unrelated plasmid, and (iii) triple-transfected with rAAV2 production plasmids. Cells were harvested at 24 and 72 h post-transfection, and nuclear fractions were processed using filter-aided sample preparation (FASP) followed by nano-scale liquid chromatography–tandem mass spectrometry (nLC-Orbitrap MS/MS). Across all samples, we identified 3384 proteins, revealing significant regulatory changes associated with transfection and rAAV production. Transfection alone accounted for some of the most substantial proteomic shifts, while rAAV production induced diverse regulatory changes linked to cell cycle control, structure, and metabolism. STRING analysis of significantly regulated proteins also identified an enrichment of those associated with the Gene Ontology (GO) term ‘response to virus’. Additionally, we examined proteins with reported relation to adenoviral components. Our findings help to unravel the complexity of rAAV production, identify interesting targets for further investigation, and may contribute to improving rAAV yield. Full article
(This article belongs to the Special Issue Antiviral Strategies Targeting Capsid Proteins: Intervention from Assembly to Function)
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Review

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16 pages, 2125 KiB  
Review
New Advances in Anti-HIV-1 Strategies Targeting the Assembly and Stability of Capsid Protein
by Chengfeng Zhang, Benteng Li, Jiamei Li, Haihong Zhang and Yuqing Wu
Int. J. Mol. Sci. 2025, 26(12), 5819; https://doi.org/10.3390/ijms26125819 - 17 Jun 2025
Viewed by 756
Abstract
The HIV-1 capsid has emerged as a highly attractive drug target due to its highly conserved sequence and critical role in the viral life cycle. By disrupting interactions between capsid proteins and impairing the proper assembly or disassembly of the capsid, the inhibitors [...] Read more.
The HIV-1 capsid has emerged as a highly attractive drug target due to its highly conserved sequence and critical role in the viral life cycle. By disrupting interactions between capsid proteins and impairing the proper assembly or disassembly of the capsid, the inhibitors can effectively suppress HIV-1 replication and infection. Based on this mechanism, numerous small-molecule agents targeting the HIV-1 capsid protein have been developed to date. In this review, we report the latest advances in such inhibitors and delve into their molecular mechanisms of action. We find a focus on small molecules modulating capsid stability and their assembly/disassembly. Hopefully this study will further enhance the understanding of HIV-1 inhibition mechanisms, facilitating the future exploration of novel capsid inhibitors. Full article
(This article belongs to the Special Issue Antiviral Strategies Targeting Capsid Proteins: Intervention from Assembly to Function)
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