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Related Concept Videos

Amyloid Fibrils03:03

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Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
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Subviral agents are infectious entities that resemble viruses but lack one or more viral components, such as a capsid or essential replication machinery. These agents include viroids, prions, and satellites, each possessing distinct structural and functional characteristics that influence their mode of infection and replication.Viroids are the simplest subviral agents, consisting of circular, single-stranded RNA molecules without a protein coat. They exclusively infect plants, relying entirely...
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Engineering Antiviral Agents via Surface Plasmon Resonance
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Reverse engineering synthetic antiviral amyloids.

Emiel Michiels1,2, Kenny Roose3,4, Rodrigo Gallardo1,2

  • 1VIB Center for Brain and Disease Research, Leuven, Belgium.

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|June 7, 2020
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Summary
This summary is machine-generated.

Scientists engineered designer amyloids to target specific viral proteins, demonstrating their potential to combat influenza A by accumulating in infected tissues. This approach offers a sequence-specific method for antiviral development against evolving viruses.

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Area of Science:

  • Synthetic biology
  • Virology
  • Biochemistry

Background:

  • Human amyloids can interact with and inhibit viral replication.
  • This interaction suggests a potential therapeutic avenue for viral infections.

Purpose of the Study:

  • To engineer virus-specific amyloids using a synthetic biology approach.
  • To investigate the efficacy of designer amyloids against influenza A and Zika viruses.

Main Methods:

  • Designed amyloids with aggregation-prone fragments homologous to specific viral target proteins.
  • Tested amyloid efficacy against influenza A and influenza B viruses in vivo.
  • Evaluated specificity against viral protein polymorphisms and related viruses.

Main Results:

  • Engineered designer amyloids specifically targeted influenza A virus proteins.
  • Demonstrated in vivo accumulation of an anti-PB2 amyloid in influenza A-infected tissues.
  • Confirmed specificity against influenza A, sparing influenza B due to sequence differences.

Conclusions:

  • Designer amyloids can be engineered for sequence-specific antiviral activity.
  • This approach offers a tunable platform for developing antivirals against evolving viruses like influenza.
  • Amyloid-virus interactions can be modulated by targeting specific protein fragments.