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The mechanism of bacterial infection by filamentous phages involves molecular interactions between TolA and phage

Fredrik Karlsson1, Carl A K Borrebaeck, Nina Nilsson

  • 1Department of Immunotechnology, Lund University, SE-220 07 Lund, Sweden.

Journal of Bacteriology
|April 3, 2003
PubMed

Insights

Filamentous bacteriophage infection involves interactions between viral gene 3 protein (g3p) and bacterial TolA. Researchers discovered novel interactions between g3p domains and TolA, and self-interaction of TolA, revealing a complex infection mechanism.

Area of Science:

  • Microbiology
  • Virology
  • Molecular Biology

Background:

  • Filamentous bacteriophages infect gram-negative bacteria using their gene 3 protein (g3p).
  • g3p possesses a complex domain structure crucial for viral entry.
  • The bacterial TolA protein acts as a coreceptor during phage infection.

Purpose of the Study:

  • To investigate the molecular interactions between g3p domains and the bacterial TolA protein.
  • To elucidate the role of TolA self-interaction in the phage infection process.
  • To understand the kinetics and specific domain interactions of g3p with TolA.

Main Methods:

  • Biosensor technique to study protein-protein interactions.
  • Analysis of interactions between viral g3p and bacterial TolA.
  • Characterization of TolA self-interaction.

Main Results:

  • A novel interaction was identified between the N2 domain of g3p and the periplasmic domain (TolAII) of TolA.
  • Extensive self-interaction of bacterial TolA molecules was observed.
  • Both N-terminal domains of g3p interact with TolA, with different kinetics than bacteriocins.

Conclusions:

  • The findings reveal a sophisticated interaction network between g3p and TolA during phage infection.
  • TolA self-interaction plays a functional role in the infection mechanism.
  • A model for filamentous bacteriophage infection is proposed based on these interactions.

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