The Peptidoglycan-Binding Protein FimV Promotes Assembly of the <i>Pseudomonas aeruginosa</i> Type IV Pilus Secretin

DOI Web Site 被引用文献6件
  • Hania Wehbi
    Department of Biochemistry and Biomedical Sciences and the Michael G. DeGroote Institute for Infectious Diseases Research, McMaster University, Hamilton, ON, Canada
  • Eder Portillo
    Department of Biochemistry and Biomedical Sciences and the Michael G. DeGroote Institute for Infectious Diseases Research, McMaster University, Hamilton, ON, Canada
  • Hanjeong Harvey
    Department of Biochemistry and Biomedical Sciences and the Michael G. DeGroote Institute for Infectious Diseases Research, McMaster University, Hamilton, ON, Canada
  • Anthony E. Shimkoff
    Department of Biochemistry and Biomedical Sciences and the Michael G. DeGroote Institute for Infectious Diseases Research, McMaster University, Hamilton, ON, Canada
  • Edie M. Scheurwater
    Department of Biochemistry and Biomedical Sciences and the Michael G. DeGroote Institute for Infectious Diseases Research, McMaster University, Hamilton, ON, Canada
  • P. Lynne Howell
    Program in Molecular Structure and Function, The Hospital for Sick Children, and Department of Biochemistry, University of Toronto, Toronto, ON, Canada
  • Lori L. Burrows
    Department of Biochemistry and Biomedical Sciences and the Michael G. DeGroote Institute for Infectious Diseases Research, McMaster University, Hamilton, ON, Canada

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<jats:title>ABSTRACT</jats:title> <jats:p> The <jats:italic>Pseudomonas aeruginosa</jats:italic> inner membrane protein FimV is among several proteins of unknown function required for type IV pilus-mediated twitching motility, arising from extension and retraction of pili from their site of assembly in the inner membrane. The pili transit the periplasm and peptidoglycan (PG) layer, ultimately exiting the cell through the PilQ secretin. Although <jats:italic>fimV</jats:italic> mutants are nonmotile, they are susceptible to killing by pilus-specific bacteriophage, a hallmark of retractable surface pili. Here we show that levels of recoverable surface pili were markedly decreased in <jats:italic>fimV pilT</jats:italic> retraction-deficient mutants compared with levels in the <jats:italic>pilT</jats:italic> control, demonstrating that FimV acts at the level of pilus assembly. Levels of inner membrane assembly subcomplex proteins PilM/N/O/P were decreased in <jats:italic>fimV</jats:italic> mutants, but supplementation of these components in <jats:italic>trans</jats:italic> did not restore pilus assembly or motility. Loss of FimV dramatically reduced the levels of the PilQ secretin multimer through which pili exit the cell, in part due to decreased levels of PilQ monomers, while PilF pilotin levels were unchanged. Expression of <jats:italic>pilQ</jats:italic> in <jats:italic>trans</jats:italic> in the wild type or <jats:italic>fimV</jats:italic> mutants increased total PilQ monomer levels but did not alter secretin multimer levels or motility. PG pulldown assays showed that the N terminus of FimV bound PG in a LysM motif-dependent manner, and a mutant with an in-frame chromosomal deletion of the LysM motif had reduced motility, secretin levels, and surface piliation. Together, our data show that FimV's role in pilus assembly is to promote secretin formation and that this function depends upon its PG-binding domain. </jats:p>

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