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    Item type:Publication,
    Unveiling the molecular architecture of Mpox: A new era in viral imaging
    (2026-01-01)
    Jutharee, Kanticha
    ;
    Yongyai, Jiraporn
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    Klankoet, Nawawan
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    Wannigama, Dhammika Leshan
    ;
    Ngamwongsatit, Natharin
    The exceptional size and architectural complexity of the Mpox virus, a giant cytoplasmic DNA virus, has long challenged structural and mechanistic analysis. This gap in structural knowledge has unfortunately stalled the development of effective diagnostic and therapeutic strategies. However, a revolution in structural biology—fueled by the synergy of cryo-EM, cryo-ET, cryo-FIB milling, and AI-based prediction—now allows for the direct interrogation of intact virions and replication factories in near-native states. These techniques reveal that Mpox virus infection is orchestrated by structurally integrated machines rather than isolated components. Consequently, the future of Mpox virus biology depends on leveraging advanced imaging technologies, such as in situ single-particle approaches and visual proteomics. By mapping comprehensive template libraries into cellular reconstructions, these strategies can resolve the near-atomic details of heterogeneous viral assemblies within their cellular environment. This approach elucidates the "molecular sociology" of infection, bridging the gap between atomic structure and cellular context. By revealing regulatory interfaces and assembly logic hidden from purification-based methods, this framework reshapes our understanding of poxvirus biology and lays a precise foundation for architecturally targeted diagnostics and therapeutics.
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    Item type:Publication,
    Development of a Broad-Spectrum Pan-Mpox Vaccine via Immunoinformatic Approaches
    (2025-08-01)
    Puagsopa, Japigorn
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    Jumpalee, Panuwid
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    Dechanun, Sittichoke
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    Choengchalad, Sukanya
    ;
    Lohasupthawee, Pana
    Monkeypox virus (MPXV) has caused 148,892 confirmed cases and 341 deaths from 137 countries worldwide, as reported by the World Health Organization (WHO), highlighting the urgent need for effective vaccines to prevent the spread of MPXV. Traditional vaccine development is low-throughput, expensive, time consuming, and susceptible to reversion to virulence. Alternatively, a reverse vaccinology approach offers a rapid, efficient, and safer alternative for MPXV vaccine design. Here, MPXV proteins associated with viral infection were analyzed for immunogenic epitopes to design multi-epitope vaccines based on B-cell, CD4+, and CD8+ epitopes. Epitopes were selected based on allergenicity, antigenicity, and toxicity parameters. The prioritized epitopes were then combined via peptide linkers and N-terminally fused to various protein adjuvants, including PADRE, beta-defensin 3, 50S ribosomal protein L7/12, RS-09, and the cholera toxin B subunit (CTB). All vaccine constructs were computationally validated for physicochemical properties, antigenicity, allergenicity, safety, solubility, and structural stability. The three-dimensional structure of the selected construct was also predicted. Moreover, molecular docking and molecular dynamics (MD) simulations between the vaccine and the TLR-4 immune receptor demonstrated a strong and stable interaction. The vaccine construct was codon-optimized for high expression in the E. coli and was finally cloned in silico into the pET21a (+) vector. Collectively, these results could represent innovative tools for vaccine formulation against MPXV and be transformative for other infectious diseases.