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Mutagenic Analysis of the HIV Restriction Factor Shiftless.

Niklas Jäger1,2, Shreya Ahana Ayyub3, Natalia Korniy3

  • 1Infection Biology Unit, German Primate Center, 37077 Göttingen, Germany.

Viruses
|July 27, 2022
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Summary

The shiftless (SFL) protein inhibits human immunodeficiency virus (HIV) by blocking ribosomal frameshifting. This action requires a specific RAA region, crucial for SFL binding to HIV RNA and blocking viral replication.

Keywords:
C19orf66HIV-1restriction factorshiftless–1 programmed ribosomal frameshifting

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Area of Science:

  • Virology
  • Molecular Biology
  • Host-Pathogen Interactions

Background:

  • The interferon-induced host cell protein shiftless (SFL) inhibits human immunodeficiency virus (HIV) by blocking -1 programmed ribosomal frameshifting (-1PRF).
  • The precise mechanism by which SFL inhibits -1PRF remains unclear.
  • A 36-amino acid region, termed required for antiviral activity (RAA), is essential for SFL's function but absent in the SFL short (SFLS) splice variant.

Purpose of the Study:

  • To elucidate the mechanism by which SFL inhibits HIV -1PRF.
  • To investigate the role of the RAA region in SFL's antiviral activity.
  • To characterize the function of the SFLS splice variant.

Main Methods:

  • Comparative analysis of SFL and SFLS activity against HIV -1PRF.
  • Mutagenic analysis of the RAA region in SFL.
  • Biochemical assays to assess SFL self-interactions, ribosome association, and binding to HIV RNA.

Main Results:

  • SFL, but not SFLS, inhibits HIV -1PRF in a cell-type-independent manner.
  • The RAA region is essential for SFL self-interactions, ribosome association, and binding to HIV RNA.
  • Deletions within the RAA region impair SFL's ability to bind HIV RNA, inhibit -1PRF, suppress Gag-Pol expression, and confer antiviral activity.

Conclusions:

  • SFL inhibits HIV -1PRF and infection by directly binding to the ribosome and HIV RNA.
  • The RAA region is critical for SFL's mechanism of action.
  • SFL multimerization may play a functional role in its antiviral activity.