ArticleWorld journal of gastroenterology2005
Screening for PreS specific binding ligands with a phage displayed peptides library.
Article in World journal of gastroenterology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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The trial behind it
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
6 citing papers in PubMed.
- Article
- Applications of human hepatitis B virus preS domain in bio- and nanotechnology.World journal of gastroenterology · 2015Review
- Phage display creates innovative applications to combat hepatitis B virus.World journal of gastroenterology · 2014Review
- Bacteriophages and their applications in the diagnosis and treatment of hepatitis B virus infection.World journal of gastroenterology · 2014Review
- Oligopeptide m13 phage display in pathogen research.Viruses · 2013Review
- Identification of GRP75 as a novel PreS1 binding protein using a proteomics strategy.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2010Article
Corrections and comments
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
aimTo construct a random peptide phage display library and search for peptides that specifically bind to the PreS region of hepatitis B virus (HBV).
methodsA phage display vector, pFuse8, based on the gene 8 product (pVIII) of M13 phage was made and used to construct a random peptide library. E.coli derived thioredoxin-PreS was purified with Thio-bond beads, and exploited as the bait protein for library screening. Five rounds of bio-panning were performed. The PreS-binding specificities of enriched phages were characterized with phage ELISA assay.
resultsA phage display vector was successfully constructed as demonstrated to present a pVIII fused HBV PreS1 epitope on the phage surface with a high efficiency. A cysteine confined random peptide library was constructed containing independent clones exceeding 5+/-10(8) clone forming unit (CFU). A pool of phages showing a PreS-binding specificity was obtained after the screening against thio-PreS with an enrichment of approximately 400 times. Five phages with high PreS-binding specificities were selected and characterized. Sequences of the peptides displayed on these phages were determined.
conclusionA phage library has been constructed, with random peptides displaying as pVIII-fusion proteins. Specific PreS-binding peptides have been obtained, which may be useful for developing antivirals against HBV infection.
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