Peer-Reviewed Publication
bioRxiv2025July 5, 2025Journal Article
De novo design of high-affinity miniprotein binders targeting Francisella tularensis virulence factor.
Gizem Gokce-Alpkilic1,2,3, Buwei Huang3,4,5,6, Andi Liu7,8, Lieselotte S M Kreuk7, Yaxi Wang7, Victor Adebomi2,3, Yensi Flores Bueso3,9, Asim K Bera3, Alex Kang3, Stacey R Gerben3, Stephen Rettie2,3,10, Dionne K Vafeados3, Nicole Roullier3, Inna Goreshnik3, Xinting Li3, David Baker3,4,11, Joshua J Woodward7, Joseph D Mougous7,11, Gaurav Bhardwaj1,2,3
1Molecular Engineering and Sciences Institute, University of Washington, Seattle, WA, USA.
2Department of Medicinal Chemistry, University of Washington, Seattle, WA, USA.
3Institute for Protein Design, University of Washington, Seattle, WA, USA.
4Department of Biochemistry, University of Washington, Seattle, WA, USA.
5Department of Bioengineering, University of Washington, Seattle, WA, USA.
6Current address: Xaira Therapeutics, Seattle, WA, USA.
7Department of Microbiology, University of Washington, Seattle, WA, USA.
8Current address: Sound Biologics, Bothell, WA, USA.
9Cancer Research @UCC, University College Cork, Cork, Ireland.
10Molecular and Cellular Biology Program, University of Washington, Seattle, WA, USA.
11Howard Hughes Medical Institute, University of Washington, Seattle, WA, USA.
Abstract
Francisella tularensis poses considerable public health risk due to its high infectivity and potential for bioterrorism. Francisella-like lipoprotein (Flpp3), a key virulence factor unique to Francisella, plays critical roles in infection and immune evasion, making it a promising target for therapeutic development. However, the lack of well-defined binding pockets and structural information on nat…
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