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The structure of Yersinia pestis V-antigen, an essential virulence factor and mediator of immunity against plague

  1. Author:
    Derewenda, U.
    Mateja, A.
    Devedjiev, Y.
    Routzahn, K. M.
    Evdokimov, A. G.
    Derewenda, Z. S.
    Waugh, D. S.

  2. Author Address

    Waugh, DS, Univ Virginia, Dept Mol Physiol & Biol Phys, Charlottesville, VA 22908 USA Univ Virginia, Dept Mol Physiol & Biol Phys, Charlottesville, VA 22908 USA. NCI, Macromol Crystallog Lab, Frederick, MD 21702 USA. Procter & Gamble Pharmaceut, Hlth Care Res Ctr Discovery, Mason, OH 45040 USA.
    1. Year: 2004
  2. Journal: Structure
    1. 12
    2. 2
    3. Pages: 301-306
  4. Type of Article: Article
  1. Abstract:

    The LcrV protein (V-antigen) is a multifunctional virulence factor in Yersinia pestis, the causative agent of plague. LcrV regulates the translocation of cytotoxic effector proteins from the bacterium into the cytosol of mammalian cells via a type III secretion system, possesses antihost activities of its own, and is also an active and passive mediator of resistance to disease. Although a crystal structure of this protein has been actively sought for better understanding of its role in pathogenesis, the wild-type LcrV was found to be recalcitrant to crystallization. We employed a surface entropy reduction mutagenesis strategy to obtain crystals of LcrV that diffract to 2.2 Angstrom and determined its structure. The refined model reveals a dumbbell-like molecule with a novel fold that includes an unexpected coiled-coil motif, and provides a detailed three-dimensional roadmap for exploring structure-function relationships in this essential virulence determinant

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