ArticleAMB Express2017
Designing novel construction for cell surface display of protein E on Escherichia coli using non-classical pathway based on Lpp-OmpA.
Article in AMB Express, 2017. 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, 22 citations in OpenAlex.
- Engineered bacteria as an orally administered anti-viral treatment and immunization system.Gut microbes · 2025Article
- The Lpp-OmpA-BtaE fusion protein causes a protective immune response against Brucella melitensis in mice.Scientific reports · 2025Article
- Exploring cadmium bioaccumulation and bioremediation mechanisms and related genes in soil microorganisms: a review.Environmental science and pollution research international · 2025Review
- Surface Display of Multiple Metal-Binding Domains inInternational journal of molecular sciences · 2024Article
- Human super antibody to viral RNA-dependent RNA polymerase produced by a modified Sortase self-cleave-bacteria surface display system.Microbial cell factories · 2023Article
- Identification of Subunits for Novel Universal Vaccines against Three Predominant Serogroups and the Emerging O145 among Avian Pathogenic Escherichia coli by Pan-RV Pipeline.Applied and environmental microbiology · 2023Article
- A bacterial outer membrane vesicle-based click vaccine elicits potent immune response againstFrontiers in immunology · 2023Article
- Engineering E. coli cell surface in order to develop a one-step purification method for recombinant proteins.AMB Express · 2018Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Today, transference of recombinant protein on the outer surface of bacteria is deemed as a valuable process for various applications in biotechnology including preparation of vaccines. In this study, Lpp-OmpA structure was used to present outer membrane protein E of Haemophilus influenzae on E. coli outer membrane. Also, a structure was designed according to Lpp-OmpA based on non-classical secretion pathway using bioinformatics software such as MEMSAT-SVM, ScrotumP and SignalP where it lacked any signal peptide at its N-terminal. Potential of this structure in the presentation of protein E on the surface of E. coli through non-classical pathway was indicated by western blotting, SDS page and fluorescent microscopy techniques, similarly its effectiveness was compared with Lpp-OmpA system. The results of the current study showed that the new structure had higher efficiency than Lpp-OmpA, and it could transport protein E on outer membrane well. This study is the first report in the presentation of H. influenzae PE onto the surface of E. coli by Lpp-OmpA, and the structure originated from Lpp-OmpA, according to the non-classical secretion pathway. Our results suggest that non-classical secretion pathway may be exploited as a new secretory pathway on the outer surface of the cell for recombinant proteins.
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