ArticleViruses2013
Generation and characterization of a novel recombinant antibody against LMP1-TES1 of Epstein-Barr virus isolated by phage display.
Article in Viruses, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 14 citations in OpenAlex.
- Antibody Phage Display Technology for Sensor-Based Virus Detection: Current Status and Future Prospects.Biosensors · 2023Review
- Developing Recombinant Antibodies by Phage Display Against Infectious Diseases and Toxins for Diagnostics and Therapy.Frontiers in cellular and infection microbiology · 2021Review
- The Epstein-Barr virus LMP1 interactome: biological implications and therapeutic targets.Future virology · 2018Article
- A neutralized human LMP1-IgG inhibits ENKTL growth by suppressing the JAK3/STAT3 signaling pathway.Oncotarget · 2017Article
- Recombinant antibodies for diagnostics and therapy against pathogens and toxins generated by phage display.Proteomics. Clinical applications · 2016Review
- Putative phage-display epitopes of the porcine epidemic diarrhea virus S1 protein and their anti-viral activity.Virus genes · 2015Article
- Probing the sites of interactions of rotaviral proteins involved in replication.Journal of virology · 2014Article
- ROR1 expression correlated with poor clinical outcome in human ovarian cancer.Scientific reports · 2014Article
- Human monoclonal antibody-based therapy in the treatment of invasive candidiasis.Clinical & developmental immunology · 2013Review
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Latent Membrane Protein 1 (LMP1) is a primary target for controlling tumorigenesis in Epstein-Barr virus related malignancies; in this study, we aimed to develop a specific antibody against the TES1 domain of the oncogenic LMP1. We screened a full human naïve Fab phage library against TES1 peptide, which consisted of C terminal-activating regions proximal 44 amino acids. After three rounds of panning, enrichment and testing by phage ELISA and further analyzed by DNA sequencing, we selected a phage clone with the highest affinity to LMP1-TES1 and designated it as htesFab. The positive clone was expressed in Escherichia coli and the purified htesFab was characterized for its binding specificity and affinity to LMP1. ELISA, immunofluorescence and FACS analysis confirmed that htesFab could recognize LMP1 TES1 both in vitro and in LMP1 expressing HNE2-LMP1 cells. Furthermore, MTT assay showed that htesFab inhibited the proliferation of HNE2-LMP1 cells in a dose-dependent manner. In summary, this study reported the isolation and characterization of human Fab, which specifically targets the C terminal region/TES1 of LMP1, and has potential to be developed as novel tool for the diagnosis and therapy of Epstein-Barr virus related carcinoma.
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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.