Abstract 2672 Structural and Dynamical Studies of FimH Reveal Novel Mechanisms of Protein Inhibition
Bacterial adhesins are critical mediators of host-pathogen interactions, enabling bacteria to attach to host tissues and establish colonization. The adhesin FimH, located at the tip of type 1 pili in uropathogenic Escherichia coli (UPEC), is a key virulence factor in urinary tract infections (UTIs) and an important target for therapeutic intervention. With the rise in antimicrobial resistance, anti-adhesive strategies that block FimH-mediated adhesion are promising alternatives to antibiotics. FimH is characterized by substantial conformational flexibility, which is fundamental to its function and regulation.
Authors
- Pearl Magala (ORCID: https://orcid.org/0000-0001-5087-3473)
- Lisa M. Tuttle (ORCID: https://orcid.org/0000-0001-8889-232X)
- Evgeni V. Sokurenko (ORCID: https://orcid.org/0000-0003-2806-4121)
- A.S. Ferreira Ramos
- Rachel E. Klevit (ORCID: https://orcid.org/0000-0002-3476-969X)
Institutions
- University of Washington (US)
- Seattle University (US)
Publication Details
- Journal
- Journal of Biological Chemistry
- Published
- 2025-05-01
- DOI
- https://doi.org/10.1016/j.jbc.2025.110020
- Primary Topic
- RNA modifications and cancer
- Type
- article
- Field-Weighted Citation Impact
- 0.00
Funders
- National Institutes of Health
- National Institute of Allergy and Infectious Diseases