ArticleApplied and environmental microbiology2001
Novel Zn(2+)-chelating peptides selected from a fimbria-displayed random peptide library.
Article in Applied and environmental microbiology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 51 citations in OpenAlex.
- Novel Benzothiazole-Based Highly Selective Ratiometric Fluorescent Turn-On Sensors for ZnACS omega · 2021Article
- Identification of metal binding motifs in protein frameworks to develop novel remediation strategies for HgBiometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2021Article
- Techniques for molecular imaging probe design.Molecular imaging · 2011Review
- Phage display: selecting straws instead of a needle from a haystack.Molecules (Basel, Switzerland) · 2011Review
- Transcriptional response of E. coli upon FimH-mediated fimbrial adhesion.Gene regulation and systems biology · 2010Article
- FimH adhesin of type 1 fimbriae is a potent inducer of innate antimicrobial responses which requires TLR4 and type 1 interferon signalling.PLoS pathogens · 2008Article
- Selection of allosteric beta-lactamase mutants featuring an activity regulation by transition metal ions.Protein science : a publication of the Protein Society · 2006Article
- Co-expression of zinc binding motif and GFP as a cellular indicator of metal ions mobility.International journal of biological sciences · 2005Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The display of peptide sequences on the surface of bacteria is a technology that offers exciting applications in biotechnology and medical research. Type 1 fimbriae are surface organelles of Escherichia coli which mediate D-mannose-sensitive binding to different host surfaces by virtue of the FimH adhesin. FimH is a component of the fimbrial organelle that can accommodate and display a diverse range of peptide sequences on the E. coli cell surface. In this study we have constructed a random peptide library in FimH. The library, consisting of approximately 40 million individual clones, was screened for peptide sequences that conferred on recombinant cells the ability to bind Zn(2+). By serial selection, sequences that exhibited various degrees of binding affinity and specificity toward Zn(2+) were enriched. None of the isolated sequences showed similarity to known Zn(2+)-binding proteins, indicating that completely novel Zn(2+)-binding peptide sequences had been isolated. By changing the protein scaffold system, we demonstrated that the Zn(2+)-binding seems to be uniquely mediated by the peptide insert and to be independent of the sequence of the carrier protein. These findings might be applied in the design of biomatrices for bioremediation purposes or in the development of sensors for detection of heavy metals.
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