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Structure/function analysis of Neisseria meningitidis PilW, a conserved protein that plays multiple roles in type IV

Tim H Szeto1, Andréa Dessen, Vladimir Pelicic

  • 1Section of Microbiology, Imperial College London, London, United Kingdom.

Infection and Immunity
|June 8, 2011
PubMed

Insights

Type IV pili (Tfp) assembly involves the PilW protein. This study shows PilW has dual roles in Tfp function and secretin channel assembly, suggesting it

Area of Science:

  • Microbiology
  • Molecular Biology
  • Structural Biology

Background:

  • Type IV pili (Tfp) are crucial bacterial organelles involved in pathogenesis.
  • The molecular mechanisms of Tfp biogenesis and function are not fully understood.
  • PilW is a conserved protein essential for Tfp biogenesis in Neisseria meningitidis.

Purpose of the Study:

  • To investigate the structure-function relationship of Neisseria meningitidis PilW.
  • To elucidate the specific roles of PilW in Tfp biogenesis and function.

Main Methods:

  • Site-directed mutagenesis of key PilW residues.
  • Phenotypic assays to analyze Tfp assembly and function.
  • Utilizing a recently reported high-resolution crystal structure of PilW.

Main Results:

  • PilW's role in Tfp functionality can be separated from its role in secretin channel assembly.
  • Specific residues in PilW are critical for distinct functions.
  • Demonstrated PilW's involvement in both Tfp assembly/stabilization and Tfp functionality.

Conclusions:

  • PilW is a multifunctional protein with distinct roles in Type IV pili biogenesis.
  • Understanding PilW's roles provides insights into Tfp assembly and pathogenesis.
  • This study advances the molecular understanding of Tfp biology.

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