ArticleApplied and environmental microbiology1998
Heterobinary adhesins based on the Escherichia coli FimH fimbrial protein.
Article in Applied and environmental microbiology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 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
9 citing papers in PubMed, 23 citations in OpenAlex.
- FimH as a scaffold for regulated molecular recognition.Journal of biological engineering · 2021Article
- Acinetobacter sp. DW-1 immobilized on polyhedron hollow polypropylene balls and analysis of transcriptome and proteome of the bacterium during phenol biodegradation process.Scientific reports · 2017Article
- Muramidases found in the foregut microbiome of the Tammar wallaby can direct cell aggregation and biofilm formation.The ISME journal · 2011Article
- Transcriptional response of E. coli upon FimH-mediated fimbrial adhesion.Gene regulation and systems biology · 2010Article
- Novel Zn(2+)-chelating peptides selected from a fimbria-displayed random peptide library.Applied and environmental microbiology · 2001Article
- Biofilm formation in a hydrodynamic environment by novel fimh variants and ramifications for virulence.Infection and immunity · 2001Article
- Fimbriae-assisted bacterial surface display of heterologous peptides.International journal of medical microbiology : IJMM · 2000Review
- Genetic characterization of Escherichia coli type 1 pilus adhesin mutants and identification of a novel binding phenotype.Journal of bacteriology · 2000Article
- Functional flexibility of the FimH adhesin: insights from a random mutant library.Infection and immunity · 2000Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The FimH adhesin of Escherichia coli type 1 fimbriae confers the ability to bind to D-mannosides by virtue of a receptor-binding domain located in its N-terminal region. This protein was engineered into a heterobifunctional adhesin by introducing a secondary binding site in the C-terminal region. The insertion of histidine clusters into this site resulted in coordination of various metal ions by recombinant cells expressing chimeric FimH proteins. In addition, libraries consisting of random peptide sequences inserted into the FimH display system and screened by a "panning" technique were used to identify specific sequences conferring the ability to adhere to Ni2+ and Cu2+. Recombinant cells expressing heterobifunctional FimH adhesins could adhere simultaneously to both metals and saccharides. Finally, combining the metal-binding modifications with alterations in the natural receptor-binding region demonstrated the ability to independently modulate the binding of FimH to two ligands simultaneously.
Indexed as
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What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.