Plasma membrane association of three classes of bacterial toxins is mediated by a basic-hydrophobic motif

Brett Geissler, Sebastian Ahrens, Karla J. F. Satchell*

*Corresponding author for this work

Research output: Contribution to journalArticle

26 Scopus citations

Abstract

Plasma membrane targeting is essential for the proper function of many bacterial toxins. A conserved fourhelical bundle membrane localization domain (4HBM) was recently identified within three diverse families of toxins: clostridial glucosylating toxins, MARTX toxins and Pasteurella multocida-like toxins. When expressed in tissue culture cells or in yeast, GFP fusions to at least one 4HBM from each toxin family show significant peripheral membrane localization but with differing profiles. Both in vivo expression and in vitro binding studies reveal that the ability of these domains to localize to the plasma membrane and bind negatively charged phospholipids requires a basic-hydrophobic motif formed by the L1 and L3 loops. The different binding capacity of each 4HBM is defined by the hydrophobicity of an exposed residue within the motif. This study establishes that bacterial effectors utilize a normal host cell mechanism to locate the plasma membrane where they can then access their intracellular targets.

Original languageEnglish (US)
Pages (from-to)286-298
Number of pages13
JournalCellular Microbiology
Volume14
Issue number2
DOIs
StatePublished - Feb 1 2012

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ASJC Scopus subject areas

  • Microbiology
  • Immunology
  • Virology

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