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Interaction between the Yersinia tyrosine phosphatase YopH and its macrophage substrate, Fyn-binding protein, Fyb

Ming Yuan1, Fabienne Deleuil, Maria Fällman

  • 1Department of Molecular Biology, Umeå University, Umeå, Sweden.

Journal of Molecular Microbiology and Biotechnology
|January 18, 2006
PubMed

Insights

Pathogenic Yersinia

Area of Science:

  • Microbiology
  • Immunology
  • Molecular Biology

Background:

  • Pathogenic Yersinia species evade host defenses by injecting virulence proteins like YopH (Yersinia outer protein H).
  • YopH is a protein tyrosine phosphatase that disrupts host cell signaling, impairing phagocytosis.
  • Fyb (Fyn-binding protein), an immune cell adaptor protein, is a known YopH substrate.

Purpose of the Study:

  • To investigate the molecular interactions between Yersinia outer protein H (YopH) and Fyn-binding protein (Fyb).
  • To elucidate the mechanisms by which YopH binds to Fyb and its functional consequences.

Main Methods:

  • Biochemical assays to study protein-protein interactions between YopH and Fyb.
  • Analysis of YopH binding to Fyb in a phosphotyrosine-dependent and -independent manner.
  • Investigation of the role of specific YopH regions in Fyb dephosphorylation and YopH-mediated cellular effects.

Main Results:

  • YopH binds to Fyb through distinct regions, involving both phosphotyrosine-dependent and -independent mechanisms.
  • The N-terminal (1-130) and C-terminal catalytic regions of YopH bind Fyb dependently on phosphotyrosine.
  • A central YopH region (130-260) interacts with the Fyb C-terminus (548-783) independently of phosphotyrosine.

Conclusions:

  • The N-terminal binding region of YopH is crucial for YopH's functional activities in macrophages.
  • These activities include Fyb dephosphorylation, inhibition of phagocytosis, and cytotoxic effects.
  • Understanding YopH-Fyb interaction provides insights into Yersinia pathogenesis and host immune evasion.

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