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 language | English |
|---|---|
| Article number | 3165 |
| Pages (from-to) | 1116-1122 |
| Number of pages | 7 |
| Journal | Structure |
| Volume | 23 |
| Issue number | 6 |
| DOIs | |
| Publication status | Published - Jun 3 2015 |
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ASJC Scopus subject areas
- Molecular Biology
- Structural Biology
Cite this
NMR Structure of Francisella tularensis Virulence Determinant Reveals Structural Homology to Bet v1 Allergen Proteins. / Zook, James; Mo, Gina; Sisco, Nicholas J.; Craciunescu, Felicia M.; Hansen, Debra T.; Baravati, Bobby; Cherry, Brian R.; Sykes, Kathryn; Wachter, Rebekka; Van Horn, Wade D.; Fromme, Petra.
In: Structure, Vol. 23, No. 6, 3165, 03.06.2015, p. 1116-1122.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - NMR Structure of Francisella tularensis Virulence Determinant Reveals Structural Homology to Bet v1 Allergen Proteins
AU - Zook, James
AU - Mo, Gina
AU - Sisco, Nicholas J.
AU - Craciunescu, Felicia M.
AU - Hansen, Debra T.
AU - Baravati, Bobby
AU - Cherry, Brian R.
AU - Sykes, Kathryn
AU - Wachter, Rebekka
AU - Van Horn, Wade D.
AU - Fromme, Petra
PY - 2015/6/3
Y1 - 2015/6/3
N2 - 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.
AB - 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.
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UR - http://www.scopus.com/inward/citedby.url?scp=84930274308&partnerID=8YFLogxK
U2 - 10.1016/j.str.2015.03.025
DO - 10.1016/j.str.2015.03.025
M3 - Article
C2 - 26004443
AN - SCOPUS:84930274308
VL - 23
SP - 1116
EP - 1122
JO - Structure with Folding & design
JF - Structure with Folding & design
SN - 0969-2126
IS - 6
M1 - 3165
ER -