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Related Concept Videos

Leaky Scanning02:28

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During most eukaryotic translation processes, the small 40S ribosome subunit scans an mRNA from its 5' end until it encounters the first start AUG codon. The large 60S ribosomal subunit then joins the smaller one to initiate protein synthesis. The location of the translation initiation is largely determined by the nucleotides near the start codon as there may be multiple translation initiation sites present on the mRNA.  Marilyn Kozak discovered that the sequence RCCAUGG (where R...
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Related Experiment Video

Updated: Jan 12, 2026

Multi-target Parallel Processing Approach for Gene-to-structure Determination of the Influenza Polymerase PB2 Subunit
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Harnessing Multiplexed Proteolysis-Targeting Chimera for Comprehensive Influenza A Virus Targeting.

Yang-Yang Liu1, Cong Yu1, Jing Li2

  • 1State Key Laboratory of Medicinal Chemical Biology, Frontiers Science Centre for New Organic Matter, Tianjin Key Laboratory of Biosensing and Molecular Recognition, Research Center for Analytical Sciences, College of Chemistry, School of Medicine, and Frontiers Science Centre for Cell Responses, Nankai University, Tianjin 300071, P. R. China.

Journal of the American Chemical Society
|November 3, 2025
PubMed
Summary

A novel Proteolysis-Targeting Chimera (PROTAC) strategy simultaneously degrades multiple influenza A virus (IAV) components. This multitarget approach offers potent, broad-spectrum antiviral activity and overcomes drug resistance, advancing influenza therapeutics.

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Area of Science:

  • Virology
  • Molecular Biology
  • Drug Discovery

Background:

  • Influenza A virus (IAV) poses a significant global health risk due to rapid mutation and immune evasion.
  • Existing antiviral therapies are limited by single-target mechanisms and the emergence of drug resistance.

Purpose of the Study:

  • To develop a novel multiplexed Proteolysis-Targeting Chimera (PROTAC) strategy for simultaneous degradation of multiple viral targets.
  • To address limitations of current influenza therapies by creating a resistance-resistant treatment.

Main Methods:

  • Designed a PROTAC molecule integrating an oligonucleotide ligand targeting conserved viral RNA with an E3 ligase recruiter.
  • The PROTAC targets and degrades multiple components of the viral ribonucleoprotein (vRNP) complex, including NP and polymerase subunits (PB1, PB2, PA).
  • Evaluated antiviral efficacy, potency, duration of action, and resistance profiles in vitro and in vivo.

Main Results:

  • The PROTAC strategy effectively degraded multiple vRNP components, disrupting viral replication.
  • PROTAC2 demonstrated potent antiviral activity (0.8 μM) with sustained inhibition (>48 h), outperforming ribavirin.
  • The multitarget approach established a high genetic barrier to resistance and showed broad-spectrum activity against IAV strains.

Conclusions:

  • Multiplexed PROTACs targeting vRNP complexes offer a highly effective and durable therapeutic strategy against influenza A virus.
  • This approach overcomes limitations of current antivirals, providing a resistance-resistant candidate with an extended therapeutic window.
  • This innovative therapy advances influenza treatment by addressing critical challenges of mutation, immune evasion, and drug resistance.