ArticleScientific reports2016
Multivalent pIX phage display selects for distinct and improved antibody properties.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
12 citing papers in PubMed, 20 citations in OpenAlex.
- Nanofilament immunotherapy induces potent antitumor vaccine responses.Journal for immunotherapy of cancer · 2025Article
- Facile Display of Homomultivalent Proteins forACS synthetic biology · 2023Article
- Review
- Affinity maturation of TCR-like antibodies using phage display guided by structural modeling.Protein engineering, design & selection : PEDS · 2022Article
- Rapid-format recombinant antibody-based methods for the diagnosis ofFrontiers in microbiology · 2022Review
- Application of recombinant antibodies for treatment ofFrontiers in immunology · 2022Review
- A high-affinity human TCR-like antibody detects celiac disease gluten peptide-MHC complexes and inhibits T cell activation.Science immunology · 2021Article
- TG2-gluten complexes as antigens for gluten-specific and transglutaminase-2 specific B cells in celiac disease.PloS one · 2021Article
- B cell tolerance and antibody production to the celiac disease autoantigen transglutaminase 2.The Journal of experimental medicine · 2020Article
- Targeting the MHC Ligandome by Use of TCR-Like Antibodies.Antibodies (Basel, Switzerland) · 2019Review
- Plasma Cells Are the Most Abundant Gluten Peptide MHC-expressing Cells in Inflamed Intestinal Tissues From Patients With Celiac Disease.Gastroenterology · 2019Article
- Naïve Human Antibody Libraries for Infectious Diseases.Advances in experimental medicine and biology · 2017Review
Corrections and comments
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Authors and funding
11 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Phage display screening readily allows for the identification of a multitude of antibody specificities, but to identify optimal lead candidates remains a challenge. Here, we direct the antibody-capsid fusion away from the signal sequence-dependent secretory SEC pathway in E. coli by utilizing the intrinsic signal sequence-independent property of pIX to obtain virion integration. This approach was combined with the use of an engineered helper phage known to improve antibody pIX display and retrieval. By direct comparison with pIII display, we demonstrate that antibody display using this pIX system translates into substantially improved retrieval of desired specificities with favorable biophysical properties in de novo selection. We show that the effect was due to less E. coli host toxicity during phage propagation conferred by the lack of a signal sequence. This pIX combinatorial display platform provides a generic alternative route for obtaining good binders with high stability and may thus find broad applicability.
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Registered trials
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