ArticleJournal of bacteriology2001
Bacterial phage receptors, versatile tools for display of polypeptides on the cell surface.
Article in Journal of bacteriology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 47 citations in OpenAlex.
- Anaerobiosis, a neglected factor in phage-bacteria interactions.Applied and environmental microbiology · 2023Article
- Construction of Cupriavidus necator displayed with superoxide dismutases for enhanced growth in bioelectrochemical systems.Bioresources and bioprocessing · 2023Article
- Streamlined phage display library protocols for identification of insect gut binding peptides highlight peptide specificity.Current research in insect science · 2021Article
- Design and Characterization of a Novel Tool for the Antigenic Enrichment ofPathogens (Basel, Switzerland) · 2020Article
- Phage-delivered sensitisation with subsequent antibiotic treatment reveals sustained effect against antimicrobial resistant bacteria.Theranostics · 2020Article
- Comprehensive antigen screening identifies Moraxella catarrhalis proteins that induce protection in a mouse pulmonary clearance model.PloS one · 2013Article
- Lambda-display: a powerful tool for antigen discovery.Molecules (Basel, Switzerland) · 2011Review
- Novel conserved group A streptococcal proteins identified by the antigenome technology as vaccine candidates for a non-M protein-based vaccine.Infection and immunity · 2010Article
- Development of a cell surface display system in a magnetotactic bacterium, "Magnetospirillum magneticum" AMB-1.Applied and environmental microbiology · 2008Article
- Discovery of a novel class of highly conserved vaccine antigens using genomic scale antigenic fingerprinting of pneumococcus with human antibodies.The Journal of experimental medicine · 2008Article
- Display technologies: application for the discovery of drug and gene delivery agents.Advanced drug delivery reviews · 2006Review
- Surface display of proteins by gram-negative bacterial autotransporters.Microbial cell factories · 2006Article
- Bacterial display using circularly permuted outer membrane protein OmpX yields high affinity peptide ligands.Protein science : a publication of the Protein Society · 2006Article
- Assembly of G protein-coupled receptors onto nanosized bacterial magnetic particles using Mms16 as an anchor molecule.Applied and environmental microbiology · 2004Article
- Functional selection of vaccine candidate peptides from Staphylococcus aureus whole-genome expression libraries in vitro.Infection and immunity · 2003Article
- Selection of peptide entry motifs by bacterial surface display.The Biochemical journal · 2002Article
- Antigen 43-mediated autotransporter display, a versatile bacterial cell surface presentation system.Journal of bacteriology · 2002Article
- Identification of in vivo expressed vaccine candidate antigens from Staphylococcus aureus.Proceedings of the National Academy of Sciences of the United States of America · 2002Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Four outer membrane proteins of Escherichia coli were examined for their capabilities and limitations in displaying heterologous peptide inserts on the bacterial cell surface. The T7 tag or multiple copies of the myc epitope were inserted into loops 4 and 5 of the ferrichrome and phage T5 receptor FhuA. Fluorescence-activated cell sorting analysis showed that peptides of up to 250 amino acids were efficiently displayed on the surface of E. coli as inserts within FhuA. Strains expressing FhuA fusion proteins behaved similarly to those expressing wild-type FhuA, as judged by phage infection and colicin sensitivity. The vitamin B(12) and phage BF23 receptor BtuB could display peptide inserts of at least 86 amino acids containing the T7 tag. In contrast, the receptors of the phages K3 and lambda, OmpA and LamB, accepted only insertions in their respective loop 4 of up to 40 amino acids containing the T7 tag. The insertion of larger fragments resulted in inefficient transport and/or assembly of OmpA and LamB fusion proteins into the outer membrane. Cells displaying a foreign peptide fused to any one of these outer membrane proteins were almost completely recovered by magnetic cell sorting from a large pool of cells expressing the relevant wild-type platform protein only. Thus, this approach offers a fast and simple screening procedure for cells displaying heterologous polypeptides. The combination of FhuA, along with with BtuB and LamB, should provide a comprehensive tool for displaying complex peptide libraries of various insert sizes on the surface of E. coli for diverse applications.
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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.