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Regulated, sequential processing by multiple proteases is required for proper maturation and release of Bordetella

Zachary M Nash1, Peggy A Cotter1

  • 1Department of Microbiology and Immunology, School of Medicine, University of North Carolina - Chapel Hill, Chapel Hill, NC, 27599-7290, USA.

Molecular Microbiology
|June 2, 2019
PubMed

Insights

Filamentous hemagglutinin (FHA) maturation involves a novel stepwise proteolysis pathway. Periplasmic protease CtpA and others are crucial for processing FhaB into functional FHA, essential for Bordetella virulence.

Area of Science:

  • Microbiology
  • Molecular Biology
  • Protein Biochemistry

Background:

  • Filamentous hemagglutinin (FHA) is a key virulence factor in Bordetella species, responsible for respiratory infections.
  • FHA is a model protein of the two-partner secretion (TPS) pathway, involving complex translocation and maturation processes.

Purpose of the Study:

  • To elucidate the proteolytic steps involved in the maturation of FHA from its precursor, FhaB.
  • To identify the proteases responsible for processing FhaB and generating mature, functional FHA.

Main Methods:

  • Protease identification and characterization.
  • In vitro and in vivo assays to assess protein processing and function.
  • Analysis of protein domains and their role in proteolytic cleavage.

Main Results:

  • CtpA, a periplasmic protease, was identified as crucial for the regulated degradation of the FhaB prodomain.
  • A three-step proteolytic mechanism involving an unidentified protease (P3), CtpA, and SphB1 is required for FHA maturation.
  • The central prodomain region of FhaB is essential for initiating its own degradation.

Conclusions:

  • A revised model for FHA secretion and maturation via the TPS pathway is proposed, highlighting sequential proteolysis.
  • This stepwise proteolysis is essential for FHA release and virulence in vivo.
  • Understanding this pathway provides insights into the broader family of TPS proteins.

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