ArticleStructure (London, England : 1993)2015
NMR Structure of Francisella tularensis Virulence Determinant Reveals Structural Homology to Bet v1 Allergen Proteins.
Article in Structure (London, England : 1993), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
8 citing papers in PubMed, 13 citations in OpenAlex.
- De Novo Design of High-Affinity Miniprotein Binders Targeting Francisella Tularensis Virulence Factor.Angewandte Chemie (International ed. in English) · 2025Article
- CryoFold: determining protein structures and data-guided ensembles from cryo-EM density maps.Matter · 2021Article
- Data-guided Multi-Map variables for ensemble refinement of molecular movies.The Journal of chemical physics · 2020Article
- XFEL and NMR Structures of Francisella Lipoprotein Reveal Conformational Space of Drug Target against Tularemia.Structure (London, England : 1993) · 2020Article
- Exploring the Diversity Within the GenusFrontiers in microbiology · 2020Article
- The tunable pReX expression vector enables optimizing the T7-based production of membrane and secretory proteins in E. coli.Microbial cell factories · 2017Article
- Article
- From the Outside-In: The Francisella tularensis Envelope and Virulence.Frontiers in cellular and infection microbiology · 2015Review
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Authors and funding
11 authors at 3 institutions in 1 country.
Funding
Abstract
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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