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Tyrosine-phosphorylated bacterial effector proteins: the enemies within

Steffen Backert1, Matthias Selbach

  • 1Otto-von-Guericke-Universität Magdeburg, Institut für Medizinische Mikrobiologie, Leipziger Str. 44, D-39120 Magdeburg, Germany. steffen.backert@medizin.uni-magdeburg.de

Trends in Microbiology
|August 16, 2005
PubMed

Insights

Bacterial secretion systems deliver effector proteins that hijack host cell functions through tyrosine phosphorylation. This strategy is common in pathogens, impacting diseases like inflammation and proliferation.

Area of Science:

  • Microbiology
  • Cell Biology
  • Biochemistry

Background:

  • Tyrosine phosphorylation is crucial for eukaryotic signal transduction.
  • Bacterial type III and type IV secretion systems translocate effector proteins.
  • These effector proteins are frequently tyrosine phosphorylated.

Purpose of the Study:

  • To highlight the role of tyrosine phosphorylation in bacterial effector proteins.
  • To demonstrate how bacteria subvert host cell functions using these systems.
  • To suggest the emergence of new examples of this phenomenon.

Main Methods:

  • Review of recent scientific literature.
  • Analysis of effector protein functions in various bacterial pathogens.
  • Comparison of secretion system mechanisms.

Main Results:

  • Tyrosine phosphorylation is a shared feature of effector proteins from diverse bacterial secretion systems.
  • Examples include pedestal formation (EPEC, Citrobacter), cell scattering (Helicobacter), invasion (Chlamydia), and inflammation/proliferation (Bartonella).
  • This represents a common bacterial strategy to manipulate host cells.

Conclusions:

  • Bacterial pathogens commonly employ tyrosine-phosphorylated effector proteins via secretion systems.
  • This mechanism is integral to pathogenesis and disease development.
  • Further discoveries of such bacterial strategies are anticipated.

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