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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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Using Zebrafish Models of Human Influenza A Virus Infections to Screen Antiviral Drugs and Characterize Host Immune Cell Responses
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Exploiting the Affimer platform against influenza A virus.

Oliver Debski-Antoniak1,2, Alex Flynn2,3, David P Klebl2,3

  • 1School of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, United Kingdom.

Mbio
|July 22, 2024
PubMed
Summary

New Affimer proteins offer a promising alternative to traditional therapies for Influenza A virus (IAV) infections. These antibody-like molecules effectively inhibit IAV by blocking viral entry into host cells, showing potential for both treatment and diagnostics.

Keywords:
Affimercryo-electron microscopy sample preparationinfluenza A virusmAb

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Area of Science:

  • Virology
  • Immunology
  • Biotechnology

Background:

  • Influenza A virus (IAV) poses a significant pandemic threat due to its high mutation rate, necessitating continuous development of effective therapeutics.
  • Current treatments for IAV are limited by rapid viral evolution, and while monoclonal antibodies (mAbs) show promise, they have limitations.
  • The Affimer platform offers an alternative, featuring rapid, animal-free production of antibody-like proteins with high expression levels.

Purpose of the Study:

  • To isolate and characterize novel Affimers capable of inhibiting Influenza A virus (IAV) infection.
  • To investigate the mechanism of action and structural basis for Affimer-mediated inhibition of IAV.
  • To evaluate the potential of Affimers as therapeutic agents and diagnostic tools against IAV.

Main Methods:

  • Phage display was used to isolate Affimers targeting a monomeric hemagglutinin (HA) fusion protein of IAV.
  • Affimer binding affinities and specificity were determined using nanomolar-binding assays against H3 HA.
  • Cryo-electron microscopy (cryo-EM) with a novel spray-grid preparation technique was employed to visualize HA-Affimer complexes.
  • Functional assays were conducted to assess Affimer inhibition of IAV infection in vitro and against related viral strains.

Main Results:

  • Twelve Affimers were isolated, with two exhibiting high-affinity nanomolar binding to the HA1 head domain of H3 HA.
  • Cryo-EM revealed the structural basis of Affimer binding, confirming blockade of sialic acid receptor interaction.
  • The characterized Affimers demonstrated potent inhibition of in vitro IAV infection and activity against closely related IAV strains.
  • Affimers were shown to inhibit IAV by preventing HA interaction with host-cell sialic acid receptors.

Conclusions:

  • Affimers represent a viable and promising alternative to existing targeted therapies for Influenza A virus (IAV).
  • The Affimer platform enables rapid development of potent inhibitors against IAV, addressing limitations of current treatments.
  • These Affimers show potential for use as both therapeutic agents and diagnostic reagents for IAV infections.