ArticleJournal of bacteriology2002
Antigen 43-mediated autotransporter display, a versatile bacterial cell surface presentation system.
Article in Journal of bacteriology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed.
- Engineered Bacterial Membranes as Next-Generation Platforms for Cancer Immunotherapy.Small science · 2026Review
- Antigen 43 associated withMicrobiology spectrum · 2025Article
- Exploring Bacterial Surface Proteome Dynamics During Infection Using Proximity Labeling.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Structural stability for surface display of antigen 43 and application to bacterial outer membrane vesicles production.BMB reports · 2024Article
- Surface Engineering ofCurrent issues in molecular biology · 2024Article
- Engineering Ag43 Signal Peptides with Bacterial Display and Selection.Methods and protocols · 2022Article
- A living material platform for the biomineralization of biosilica.Materials today. Bio · 2022Article
- Killed whole-genome reduced-bacteria surface-expressed coronavirus fusion peptide vaccines protect against disease in a porcine model.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Motility and chemotaxis of bacteria-driven microswimmers fabricated using antigen 43-mediated biotin display.Scientific reports · 2018Article
- Comparing autotransporter β-domain configurations for their capacity to secrete heterologous proteins to the cell surface.PloS one · 2018Article
- Fusion with the cold-active esterase facilitates autotransporter-based surface display of the 10th human fibronectin domain in Escherichia coli.Extremophiles : life under extreme conditions · 2018Article
- Antigen Localization Influences the Magnitude and Kinetics of Endogenous Adaptive Immune Response to Recombinant Salmonella Vaccines.Infection and immunity · 2017Article
- YeeJ is an inverse autotransporter from Escherichia coli that binds to peptidoglycan and promotes biofilm formation.Scientific reports · 2017Article
- BrkAutoDisplay: functional display of multiple exogenous proteins on the surface of Escherichia coli by using BrkA autotransporter.Microbial cell factories · 2015Article
- An autotransporter display platform for the development of multivalent recombinant bacterial vector vaccines.Microbial cell factories · 2014Article
- Antigen 43/Fcε3 chimeric protein expressed by a novel bacterial surface expression system as an effective asthma vaccine.Immunology · 2014Article
- Ag43-mediated display of a thermostable β-glucosidase in Escherichia coli and its use for simultaneous saccharification and fermentation at high temperatures.Microbial cell factories · 2014Article
- Surface display of the HPV L1 capsid protein by the autotransporter Shigella IcsA.Journal of microbiology (Seoul, Korea) · 2014Article
- Characterization and functional analysis of AatB, a novel autotransporter adhesin and virulence factor of avian pathogenic Escherichia coli.Infection and immunity · 2013Article
- Probing the applicability of autotransporter based surface display with the EstA autotransporter of Pseudomonas stutzeri A15.Microbial cell factories · 2012Article
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Antigen 43 (Ag43), a self-recognizing outer membrane protein of Escherichia coli, has been converted into an efficient and versatile tool for surface display of foreign protein segments. Ag43 is an autotransporter protein characterized by the feature that all information required for transport to the outer membrane and secretion through the cell envelope is contained within the protein itself. Ag43 consists of two subunits (alpha and beta), where the beta-subunit forms an integral outer membrane translocator to which the alpha-subunit is noncovalently attached. The simplicity of the Ag43 system makes it ideally suited as a surface display scaffold. Here we demonstrate that the Ag43 alpha-module can accommodate and display correctly folded inserts and has the ability to display entire functional protein domains, exemplified by the FimH lectin domain. The presence of heterologous cysteine bridges does not interfere with surface display, and Ag43 chimeras are correctly processed into alpha- and beta-modules, offering optional and easy release of the chimeric alpha-subunits. Furthermore, Ag43 can be displayed in many gram-negative bacteria. This feature is exploited for display of our chimeras in an attenuated Salmonella strain.
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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.