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Profiling Selectivity for the Shigella Virulence Factor OspF.

Nicholas P McCurtin1, Ariana Gazaferi1, Noah D Novick1

  • 1Department of Chemistry, School of Arts and Sciences, Tufts University, 62 Talbot Avenue, Medford, Massachusetts 02155, United States.

Biochemistry
|April 22, 2026
PubMed
Summary
This summary is machine-generated.

Phosphothreonine lyases like OspF from Shigella flexneri modify host proteins, impacting immune response. This study identifies new OspF targets beyond MAPKs, revealing broader roles in infection and potential as protein editing tools.

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Area of Science:

  • Microbiology
  • Biochemistry
  • Molecular Biology

Background:

  • Phosphothreonine lyases are bacterial virulence factors secreted into host cells.
  • They catalyze phosphate β-elimination, converting phosphothreonine to dehydrobutyrine on host proteins.
  • OspF from Shigella flexneri modifies mitogen-activated protein kinases (MAPKs) to suppress host immunity.

Purpose of the Study:

  • To explore the substrate profile of OspF, a phosphothreonine lyase from Shigella flexneri.
  • To identify new cellular targets of OspF beyond the MAPK family.
  • To assess the potential of OspF as a tool for protein editing.

Main Methods:

  • In vitro assays with synthetic phosphopeptides.
  • Bottom-up chemoproteomic profiling.
  • Nucleophilic phosphine chemical probe for target identification.

Main Results:

  • OspF exhibits selectivity within the MAPK family.
  • OspF modifies a wide range of cellular targets in lysates and during Shigella flexneri infection.
  • New OspF targets, including Rab1A and casein kinase 2β, were identified and validated.

Conclusions:

  • OspF targets extend beyond MAPKs, revealing broader roles in Shigella flexneri infection.
  • Further research is needed to fully elucidate OspF's role in pathogenesis.
  • OspF and other phospholyases show potential as tools for site-specific protein editing.