Part:BBa_K4633000

FimHL - Mannose-Binding Domain of FimH

Usage and Biology

FimH is a crucial adhesin employed by Escherichia coli, especially uropathogenic E. coli (UPEC), to establish infections. E. coli is equipped with various types of pili, with type 1 pili being one of the most prevalent, featuring various adhesins at their termini. Among these adhesins, FimH stands out, comprising two distinct domains: the C-terminal pillin domain (FimHP), responsible for pillus anchoring, and the N-terminal lectin domain (FimHL), responsible for mannose binding. UPEC utilizes FimH to bind to mannose-containing glycoproteins located on the surface of epithelial cells within the urinary tract. This binding facilitates not only adhesion but also invasion of these cells, contributing to recurrent infections [1].

This part contains only FimHL domain, consisting of amino acids 1-163, which has been shown to exhibit significantly higher mannose affinity than the full-length FimH protein [2]. This part was intended for expression and testing in Bacillus subtilis 168, selected as a Gram-positive model organism within our project. Further details are available on our wiki.

Sequence and Features

Assembly Compatibility:

• 10
  COMPATIBLE WITH RFC[10]
• 12
  COMPATIBLE WITH RFC[12]
• 21
  INCOMPATIBLE WITH RFC[21]

  Illegal BglII site found at 108
  
• 23
  COMPATIBLE WITH RFC[23]
• 25
  COMPATIBLE WITH RFC[25]
• 1000
  COMPATIBLE WITH RFC[1000]

References

• [1] C. N. Spaulding and S. J. Hultgren, “Adhesive Pili in UTI Pathogenesis and Drug Development,” Pathog. 2016, Vol. 5, Page 30, vol. 5, no. 1, p. 30, Mar. 2016, doi: 10.3390/PATHOGENS5010030.
• [2] M. M. Sauer et al., “Catch-bond mechanism of the bacterial adhesin FimH,” Nat. Commun. 2016 71, vol. 7, no. 1, pp. 1–13, Mar. 2016, doi: 10.1038/ncomms10738.