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    IpaD Localizes to the Tip of the Type III Secretion System Needle of Shigella flexneri

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    Middaugh_et_al_2006.pdf (550.1Kb)
    Issue Date
    2006-08
    Author
    Espina, Marianela
    Olive, Andrew J.
    Kenjale, Roma
    Moore, David S.
    Ausar, S. Fernando
    Kaminski, Robert W.
    Oaks, Edwin V.
    Middaugh, C. Russell
    Picking, William D.
    Picking, Wendy Lynn
    Publisher
    American Society for Microbiology
    Type
    Article
    Article Version
    Scholarly/refereed, publisher version
    Metadata
    Show full item record
    Abstract
    Shigella flexneri, the causative agent of shigellosis, is a gram-negative bacterial pathogen that initiates infection by invading cells within the colonic epithelium. Contact with host cell surfaces induces a rapid burst of protein secretion via the Shigella type III secretion system (TTSS). The first proteins secreted are IpaD, IpaB, and IpaC, with IpaB and IpaC being inserted into the host cell membrane to form a pore for translocating late effectors into the target cell cytoplasm. The resulting pathogen-host cross talk results in localized actin polymerization, membrane ruffling, and, ultimately, pathogen entry. IpaD is essential for host cell invasion, but its role in this process is just now coming to light. IpaD is a multifunctional protein that controls the secretion and presentation of IpaB and IpaC at the pathogen-host interface. We show here that antibodies recognizing the surface-exposed N terminus of IpaD neutralize Shigella's ability to promote pore formation in erythrocyte membranes. We further show that MxiH and IpaD colocalize on the bacterial surface. When TTSS needles were sheared from the Shigella surface, IpaD was found at only the needle tips. Consistent with this, IpaD localized to the exposed tips of needles that were still attached to the bacterium. Molecular analyses then showed that the IpaD C terminus is required for this surface localization and function. Furthermore, mutations that prevent IpaD surface localization also eliminate all IpaD-related functions. Thus, this study demonstrates that IpaD localizes to the TTSA needle tip, where it functions to control the secretion and proper insertion of translocators into host cell membranes
    Description
    This is the publisher's version, also available electronically from http://iai.asm.org/content/74/8/4391
    URI
    http://hdl.handle.net/1808/14797
    DOI
    https://doi.org/10.1128/IAI.00440-06
    ISSN
    0019-9567
    Collections
    • Pharmaceutical Chemistry Scholarly Works [252]
    Citation
    Espina, Marianela et al. (2006). IpaD Localizes to the Tip of the Type III Secretion System Needle of Shigella flexneri. Infection and Immunity 74(8):4391-4400. http://www.dx.doi.org/10.1128/IAI.00440-06

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    Contact KU ScholarWorks
    785-864-8983
    KU Libraries
    1425 Jayhawk Blvd
    Lawrence, KS 66045
    785-864-8983

    KU Libraries
    1425 Jayhawk Blvd
    Lawrence, KS 66045
    Image Credits
     

     

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