A host-specific factor is necessary for efficient folding of the autotransporter plasmid-encoded toxin

    Authors

    K. N. Nemec; P. Scaglione; F. Navarro-Garcia; J. Huerta; S. A. Tatulian;K. Teter

    Comments

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    Abbreviated Journal Title

    Biochimie

    Keywords

    Autotransporter; Circular dichroism; Plasmid-encoded toxin; Protein; folding; ENTEROAGGREGATIVE ESCHERICHIA-COLI; SHIGELLA-FLEXNERI; PROTEIN; SECRETION; EPITHELIAL-CELLS; COMMON THEMES; BETA-HELIX; PET; PATHWAY; SURFACE; ICSA; Biochemistry & Molecular Biology

    Abstract

    Autotransporters are the most common virulence factors secreted from Gram-negative pathogens. Until recently, autotransporter folding and outer membrane translocation were thought to be self-mediated events that did not require accessory factors. Here, we report that two variants of the autotransporter plasmid-encoded toxin are secreted by a lab strain of Escherichia coli. Biophysical analysis and cell-based toxicity assays demonstrated that only one of the two variants was in a folded, active conformation. The misfolded variant was not produced by a pathogenic strain of enteroaggregative E. coli and did not result from protein overproduction in the lab strain of E coli. Our data suggest a host-specific factor is required for efficient folding of plasmid-encoded toxin. (C) 2009 Elsevier Masson SAS. All rights reserved.

    Journal Title

    Biochimie

    Volume

    92

    Issue/Number

    2

    Publication Date

    1-1-2010

    Document Type

    Article

    Language

    English

    First Page

    171

    Last Page

    177

    WOS Identifier

    WOS:000274610600007

    ISSN

    0300-9084

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