ArticlePloS one2009
Differential bacterial surface display of peptides by the transmembrane domain of OmpA.
Article in PloS one, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 41 citations in OpenAlex.
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- Identification and Expression of Immunogenic Mimotopes ofVaccines · 2026Article
- TheJornal brasileiro de doencas sexualmente transmissiveis : DST · 2026Article
- Diagnosis of gout using monosodium urate (MSU) crystal binding peptides screened from Fv-antibody library.Analytical and bioanalytical chemistry · 2026Article
- Bacterial Systems as a Precision Delivery Platform of Therapeutic Peptides for Cancer Therapy.Polymer science & technology (Washington, D.C.) · 2025Review
- Display of PETase on the Cell Surface of Escherichia coli Using the Anchor Protein PgsA.Applied biochemistry and biotechnology · 2024Article
- Construction of Cupriavidus necator displayed with superoxide dismutases for enhanced growth in bioelectrochemical systems.Bioresources and bioprocessing · 2023Article
- An Engineered OmpG Nanopore with Displayed Peptide Motifs for Single-Molecule Multiplex Protein Detection.Angewandte Chemie (International ed. in English) · 2023Article
- Phase separation in the outer membrane ofProceedings of the National Academy of Sciences of the United States of America · 2021Article
- A nanobody:GFP bacterial platform that enables functional enzyme display and easy quantification of display capacity.Microbial cell factories · 2016Article
- Protecting enzymatic function through directed packaging into bacterial outer membrane vesicles.Scientific reports · 2016Article
- BrkAutoDisplay: functional display of multiple exogenous proteins on the surface of Escherichia coli by using BrkA autotransporter.Microbial cell factories · 2015Article
- Absence of long-range diffusion of OmpA in E. coli is not caused by its peptidoglycan binding domain.BMC microbiology · 2013Article
- Effect of crowding by Ficolls on OmpA and OmpT refolding and membrane insertion.Protein science : a publication of the Protein Society · 2013Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Peptide libraries or antigenic determinants can be displayed on the surface of bacteria through insertion in a suitable outer membrane scaffold protein. Here, we inserted the well-known antibody epitopes 3xFLAG and 2xmyc in exterior loops of the transmembrane (TM) domain of OmpA. Although these highly charged epitopes were successfully displayed on the cell surface, their levels were 10-fold reduced due to degradation. We verified that the degradation was not caused by the absence of the C-terminal domain of OmpA. In contrast, a peptide that was only moderately charged (SA-1) appeared to be stably incorporated in the outer membrane at normal protein levels. Together, these results suggest that the display efficiency is sensitive to the charge of the inserted epitopes. In addition, the high-level expression of OmpA variants with surface-displayed epitopes adversely affected growth in a strain dependent, transient manner. In a MC4100 derived strain growth was affected, whereas in MC1061 derived strains growth was unaffected. Finally, results obtained using a gel-shift assay to monitor beta-barrel folding in vivo show that the insertion of small epitopes can change the heat modifiability of the OmpA TM domain from 'aberrant' to normal, and predict that some beta-barrels will not display any significant heat-modifiability at all.
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