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Related Experiment Videos

Surface anchoring of bacterial subtilisin important for maturation function.

Loic Coutte1, Eve Willery, Rudy Antoine

  • 1INSERM U44, Institut de Biologie de Lille, Institut Pasteur de Lille, 1 rue Calmette, 59019 Lille Cedex, France.

Molecular Microbiology
|June 28, 2003
PubMed
Summary

The autotransporter SphB1 protease requires an outer membrane anchor for filamentous hemagglutinin (FHA) maturation in Bordetella pertussis. Surface localization is achieved through lipidation, revealing a novel protease localization mechanism.

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Area of Science:

  • Microbiology
  • Molecular Biology
  • Protein Biochemistry

Background:

  • Extracytoplasmic proteins require proteolytic processing for maturation during secretion.
  • Specific enzymes carry out these post-translational modifications, with subcellular localization being critical for function.
  • The Gram-negative bacterium Bordetella pertussis utilizes autotransporter proteins for secretion.

Purpose of the Study:

  • To investigate the role of the autotransporter SphB1 in protein maturation and secretion in Bordetella pertussis.
  • To determine the importance of SphB1's subcellular localization for its enzymatic activity, specifically FHA maturation.
  • To elucidate the mechanism of SphB1 surface retention and stabilization.

Main Methods:

  • Genetic manipulation of Bordetella pertussis to create strains expressing SphB1 variants.

Related Experiment Videos

  • Analysis of filamentous hemagglutinin (FHA) maturation in different SphB1 mutant strains.
  • Biochemical assays to assess SphB1 auto-maturation and surface localization.
  • Investigation of protein lipidation and N-terminal motifs involved in SphB1 retention.

    • Main Results:

    • The outer membrane anchor of SphB1 is essential for the maturation of filamentous hemagglutinin (FHA).
    • SphB1 variants lacking the outer membrane anchor were released into the milieu, leading to a lack of FHA maturation.
    • Surface association is not required for SphB1 auto-maturation, but lipidation mediates the surface retention of mature SphB1.
    • Unusual Gly- and Pro-rich motifs at the N-terminus stabilize the tethered protease.

    Conclusions:

    • SphB1's outer membrane localization is critical for its function in FHA maturation.
    • Lipidation is the key mechanism for retaining mature SphB1 on the bacterial surface.
    • This study reveals a novel mechanism for protease localization in bacterial secretion systems.