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Engineering Antiviral Agents via Surface Plasmon Resonance
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Site-Specific Lipidation Enhances IFITM3 Membrane Interactions and Antiviral Activity

Emma H Garst1,2, Hwayoung Lee3, Tandrila Das1,2

  • 1Laboratory of Chemical Biology and Microbial Pathogenesis, The Rockefeller University, New York, New York 10065, United States.

ACS Chemical Biology
|April 22, 2021
PubMed

Insights

Interferon-induced transmembrane proteins (IFITMs) restrict viruses. Site-specific S-palmitoylation of IFITM3 enhances its antiviral activity by altering its structure and membrane interactions.

Area of Science:

  • Biochemistry
  • Virology
  • Cell Biology

Background:

  • Interferon-induced transmembrane proteins (IFITMs) are key antiviral effectors in vertebrates.
  • IFITM3, specifically, inhibits viral entry and promotes lysosomal degradation of viruses.
  • The precise role of S-palmitoylation in modulating IFITM3's structure and function remains largely unknown.

Purpose of the Study:

  • To investigate how site-specific S-palmitoylation influences the antiviral activity of IFITM3.
  • To elucidate the structural and biophysical mechanisms by which S-palmitoylation enhances IFITM3's function.

Main Methods:

  • Computational modeling
  • Chemical biology techniques
  • Biophysical assays

Main Results:

  • Site-specific S-palmitoylation at cysteine 72 significantly enhances IFITM3's antiviral potency.
  • Lipidation at cysteine 72 alters IFITM3's conformation.
  • S-palmitoylation modulates IFITM3's interaction with cellular lipid membranes.

Conclusions:

  • Site-specific S-palmitoylation is a critical regulator of IFITM3 antiviral activity.
  • The modification directly impacts IFITM3's biophysical properties and cellular function to confer resistance against viral infection.

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