The structure of Yersinia pestis V-antigen, an essential virulence factor and mediator of immunity against plague
Derewenda, U.;Mateja, A.;Devedjiev, Y.;Routzahn, K. M.;Evdokimov, A. G.;Derewenda, Z. S.;Waugh, D. S. (2004). "The structure of Yersinia pestis V-antigen, an essential virulence factor and mediator of immunity against plague." Structure 12 2: 301-6
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 A 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.
ISSN: 0969-2126 (Print);0969-2126 (Linking)
Accession Number: 14962390