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Updated: Dec 26, 2025
Scalable High Throughput Selection From Phage-displayed Synthetic Antibody Libraries
Published on: January 17, 2015
Selection and characterization of a Vibrio parahaemolyticus OmpU antibody by phage display
Junfang Yu1, Zhe Sun1, Xiaoyu Sun2
1School of Life Sciences, Shandong University of Technology, Zibo, 255000, People's Republic of China.
Abstract:
Vibrio parahaemolyticus (V. parahaemolyticus) is a well-known food-borne human pathogen that can cause a variety of clinical manifestations after the consumption of raw or undercooked seafoods. The crucial roles of Vibrio OmpU in bacterial pathogenesis have been found in recent studies. In the present study, we screened for single domain antibody fragment (sdAb) candidates that bind to V. parahaemolyticus OmpU by using a sdAb phage display library and isolated several positive phage clones. The UAb28, which was one of the positive clones, was shown high enrichment and affinity. The CDRs of UAb28 are speculated to perform the OmpU binding function by molecular docking. The capable of recognizing OmpU was verified by binding and inhibition assays. The UAb28 might be useful in future studies to develop the potential sdAb-based immunotherapeutics against V. parahaemolyticus infection.
Insights
Researchers identified a novel single domain antibody fragment (sdAb), UAb28, that effectively binds to Vibrio parahaemolyticus OmpU. This discovery offers potential for developing new immunotherapeutics against this food-borne pathogen.
Area of Science:
- Microbiology
- Immunology
- Biotechnology
Background:
- Vibrio parahaemolyticus is a significant food-borne pathogen.
- The outer membrane protein U (OmpU) plays a critical role in V. parahaemolyticus pathogenesis.
Purpose of the Study:
- To screen for single domain antibody fragments (sdAbs) that specifically bind to V. parahaemolyticus OmpU.
- To characterize the binding affinity and potential therapeutic applications of identified sdAbs.
Main Methods:
- Utilized a single domain antibody fragment (sdAb) phage display library to screen for binders.
- Employed molecular docking to predict binding interactions of the antibody's CDRs with OmpU.
- Verified binding and inhibition capabilities using experimental assays.
Main Results:
- Isolated several positive phage clones, with UAb28 showing high enrichment and affinity for V. par. parahaemolyticus OmpU.
- Confirmed that UAb28 specifically recognizes and binds to OmpU.
- Molecular docking suggested that the CDRs of UAb28 are responsible for OmpU binding.
Conclusions:
- The identified sdAb, UAb28, demonstrates specific binding to V. parahaemolyticus OmpU.
- UAb28 shows promise as a candidate for developing novel sdAb-based immunotherapeutics against V. parahaemolyticus infections.
