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Type 1 Does the Two-Step: Type 1 Secretion Substrates with a Functional Periplasmic Intermediate.

T Jarrod Smith1, Holger Sondermann2, George A O'Toole3

  • 1Department of Microbiology and Immunology, Geisel School of Medicine at Dartmouth, Hanover, New Hampshire, USA.

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|June 6, 2018
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Summary
This summary is machine-generated.

Bacteria use type 1 secretion systems (T1SS) for protein transport. A newly identified subgroup of T1SS, linked with bacterial transglutaminase-like cysteine proteinase (BTLCP), employs a two-step mechanism for secreting RTX adhesins crucial for biofilm formation.

Keywords:
LapAT1SSadhesinbiofilmretention module

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Area of Science:

  • Microbiology
  • Molecular Biology
  • Biochemistry

Background:

  • Bacteria utilize diverse secretion systems, including the well-established type 1 secretion system (T1SS), for protein export.
  • T1SSs were traditionally considered a one-step mechanism, directly translocating substrates from the cytoplasm to the extracellular environment.
  • Recent evidence reveals a distinct T1SS subgroup associated with bacterial transglutaminase-like cysteine proteinase (BTLCP) that operates via a two-step secretion pathway.

Purpose of the Study:

  • To elucidate the mechanism of a distinct subgroup of T1SS linked with BTLCP.
  • To investigate the role of this two-step secretion process in the transport of repeats-in-toxin (RTX) adhesins.
  • To contrast the two-step secretion pathway with the classical one-step T1SS.

Main Methods:

  • Phylogenetic analysis to identify T1SS subgroups.
  • Biochemical assays to characterize protein interactions and cleavage.
  • Genetic studies to investigate the function of secretion machinery components.

Main Results:

  • A subgroup of T1SS machinery linked with BTLCP utilizes a two-step secretion mechanism.
  • This pathway is responsible for secreting RTX adhesins, essential for bacterial biofilm formation.
  • The RTX adhesin LapA from *Pseudomonas fluorescens* uses a cell-surface intermediate and periplasmic cleavage by LapG.

Conclusions:

  • The secretion of LapA and related RTX adhesins is a T1SS-mediated two-step process involving a periplasmic intermediate.
  • This finding expands the known functional repertoire of T1SS machinery.
  • Understanding this novel secretion strategy is crucial for comprehending bacterial adhesion and biofilm development.