NMR Structure of Francisella tularensis Virulence Determinant Reveals Structural Homology to Bet v1 Allergen Proteins

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

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4 Citations (Scopus)

Abstract

Summary 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.

Original languageEnglish
Article number3165
Pages (from-to)1116-1122
Number of pages7
JournalStructure
Volume23
Issue number6
DOIs
Publication statusPublished - Jun 3 2015

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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    Zook, J., Mo, G., Sisco, N. J., Craciunescu, F. M., Hansen, D. T., Baravati, B., Cherry, B. R., Sykes, K., Wachter, R., Van Horn, W. D., & Fromme, P. (2015). NMR Structure of Francisella tularensis Virulence Determinant Reveals Structural Homology to Bet v1 Allergen Proteins. Structure, 23(6), 1116-1122. [3165]. https://doi.org/10.1016/j.str.2015.03.025