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The Neisseria meningitidis outer membrane lipoprotein FrpD binds the RTX protein FrpC

Katerina Prochazkova1, Radim Osicka, Irena Linhartova

  • 1Institute of Microbiology of the Academy of Sciences of the Czech Republic, Videnska 1083, CZ-142 20 Prague 4, Czech Republic.

The Journal of Biological Chemistry
|November 5, 2004
PubMed

Insights

Iron starvation in Neisseria meningitidis induces FrpD production. This outer membrane lipoprotein binds FrpC, potentially anchoring it to the bacterial surface.

Area of Science:

  • Microbiology
  • Bacterial Pathogenesis
  • Protein Biochemistry

Background:

  • Neisseria meningitidis secretes RTX proteins like FrpC under low iron conditions.
  • The function of these RTX proteins in meningococcal lifestyle remains largely unknown.
  • An adjacent gene, frpD, is also upregulated during iron starvation.

Purpose of the Study:

  • To investigate the role and characteristics of the FrpD protein in Neisseria meningitidis.
  • To determine the subcellular localization and potential interactions of FrpD.
  • To elucidate the functional relationship between FrpD and FrpC.

Main Methods:

  • Analysis of gene expression under iron-limiting conditions.
  • Protein localization studies using subcellular fractionation and labeling in E. coli.
  • Biochemical assays to determine FrpD-FrpC binding affinity.

Main Results:

  • Iron starvation induces FrpD production, encoded by the frpDC operon.
  • FrpD is a highly conserved lipoprotein localized to the outer bacterial membrane.
  • FrpD exhibits high-affinity binding to the N-terminal region of FrpC.

Conclusions:

  • FrpD is an RTX loci-encoded accessory lipoprotein.
  • FrpD likely functions in anchoring the secreted RTX protein FrpC to the outer membrane.
  • This interaction may play a role in meningococcal pathogenesis or survival.

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