NMR Structure of Francisella tularensis Virulence Determinant Reveals Structural Homology to Bet v1 Allergen Proteins.
NMR Structure of Francisella tularensis Virulence Determinant Reveals Structural Homology to Bet v1 Allergen Proteins.
复制标题
土拉弗朗西斯菌毒力决定因子的 NMR 结构揭示了与 Bet v1 过敏原蛋白的结构同源性。
DOI：
10.1016/j.str.2015.03.025
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发表时间：
2015
期刊：
影响因子：
--
通讯作者：
Fromme,Petra
中科院分区：
文献类型：
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作者：
Zook,James;Mo,Gina;Sisco,NicholasJ;Craciunescu,FeliciaM;Hansen,DebraT;Baravati,Bobby;Cherry,BrianR;Sykes,Kathryn;Wachter,Rebekka;VanHorn,WadeD;Fromme,Petra
Tularemia is a potentially fatal bacterial infection caused byFrancisella 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 genusFrancisella. 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 ofF. tularensisvirulence and contribute to the development of effective vaccines.
