ArticlePloS one2012
Using phage and yeast display to select hundreds of monoclonal antibodies: application to antigen 85, a tuberculosis biomarker.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.
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Who cites it
53 citing papers in PubMed.
- Multiobjective VScience advances · 2026Article
- Integrating fab phage and yeast display through seamless transfer of paired heavy- and light-chain libraries for efficient antibody discovery.Antibody therapeutics · 2026Article
- Nanoyeast-based impedimetric biosensor with mutated single chain antigen-binding fragment anchoring for SARS-CoV-2 detection.Biomedical microdevices · 2026Article
- Discovering Novel Therapeutic VbioRxiv : the preprint server for biology · 2026Article
- Discovering novel therapeutic VFrontiers in immunology · 2026Article
- Article
- Advancements in mammalian display technology for therapeutic antibody development and beyond: current landscape, challenges, and future prospects.Frontiers in immunology · 2024Review
- Insights into next generation sequencing guided antibody selection strategies.Scientific reports · 2023Article
- Rare antibody phage isolation and discrimination (RAPID) biopanning enables identification of high-affinity antibodies against challenging targets.Communications biology · 2023Article
- Genome-Wide Libraries for Protozoan Pathogen Drug Target Screening Using Yeast Surface Display.ACS infectious diseases · 2023Article
- Direct selection of functional fluorescent-protein antibody fusions by yeast display.PloS one · 2023Article
- A pandemic-enabled comparison of discovery platforms demonstrates a naïve antibody library can match the best immune-sourced antibodies.Nature communications · 2022Article
- A single donor is sufficient to produce a highly functional in vitro antibody library.Communications biology · 2021Article
- Construction, characterization and crystal structure of a fluorescent single-chain Fv chimera.Protein engineering, design & selection : PEDS · 2021Article
- Developing Recombinant Antibodies by Phage Display Against Infectious Diseases and Toxins for Diagnostics and Therapy.Frontiers in cellular and infection microbiology · 2021Review
- RNase H-dependent PCR enables highly specific amplification of antibody variable domains from single B-cells.PloS one · 2020Article
- Development of Anti-ImmunoTargets and therapy · 2020Article
- Integration of phage and yeast display platforms: A reliable and cost effective approach for binning of peptides as displayed on-phage.PloS one · 2020Article
- Article
- Recombinant Antibodies against Mycolactone.Toxins · 2019Article
Corrections and comments
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundCurrent diagnostic methods for tuberculosis (TB), a major global health challenge that kills nearly two million people annually, are time-consuming and inadequate. During infection a number of bacterial molecules that play a role in the infective process are released and have been proposed as biomarkers for early TB diagnosis. Antigen 85 (Ag85) is the most abundant secreted TB protein, and a potential target for this diagnostic approach. One of the bottlenecks in the direct detection of such bacterial targets is the availability of robust, sensitive, specific antibodies.
methodsUsing Ag85 as a model, we describe a method to select antibodies against any potential target using a novel combination of phage and yeast display that exploits the advantage of each approach.
resultsThe efficiency of this approach was attested to by the 111 specific antibodies identified in initial screens. These were assessed for binding to the different Ag85 subunits, affinity, and activity in sandwich assays.
conclusionsThe novelty of this approach lies in the possibility of screening the entire output of a phage antibody selection in a single experiment by yeast display. This can be considered analogous to carrying out a million ELISAs. The monoclonal antibodies (mAbs) identified in this way show high binding affinity and selectivity for the antigens and offer an advantage over traditional mAbs produced by relatively expensive and time consuming techniques. This approach has wide applicability, and the affinity of selected antibodies can be significantly improved, if required.
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