Publication date: Available online 21 May 2015 Source:Structure
Author(s): James Zook , Gina Mo , Nicholas*J. Sisco , Felicia*M. Craciunescu , Debra*T. Hansen , Bobby Baravati , Brian*R. Cherry , Kathryn Sykes , Rebekka Wachter , Wade*D. Van*Horn , Petra Fromme
Tularemia is a potentially fatal bacterial infection caused by Francisella tularensis, and is endemic to North America and many parts of northern Europe and Asia. The outer membrane lipoprotein, Flpp3, has been identified as a virulence determinant as well as a potential subunit template for vaccine development. Here we present the first structure for the soluble domain of Flpp3 from the highly infectious Type A SCHU S4 strain, derived through high-resolution solution nuclear magnetic resonance (NMR) spectroscopy; the first structure of a lipoprotein from the genus Francisella. The Flpp3 structure demonstrates a globular protein with an electrostatically polarized surface containing an internal cavity—a putative binding site based on the structurally homologous Bet v1 protein family of allergens. NMR-based relaxation studies suggest loop regions that potentially modulate access to the internal cavity. The Flpp3 structure may add to the understanding of F.*tularensis virulence and contribute to the development of effective vaccines. Graphical abstract
Teaser
Flpp3, a virulence determinant for the pathogen F.*tularensis, is a possible target for vaccine and drug development. Zook et*al. report the structure of Flpp3, revealing for the first time the internal binding cavity. Flpp3 is structurally homologous to the Bet v1 family of proteins, responsible for many allergic reactions.
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NMR Structure of Francisella tularensis Virulence Determinant Reveals Structural Homology to Bet v1 Allergen Proteins
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