ArticleActa crystallographica. Section F, Structural biology communications2015
The structure of a GFP-based antibody (fluorobody) to TLH, a toxin from Vibrio parahaemolyticus.
Article in Acta crystallographica. Section F, Structural biology communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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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
2 citing papers in PubMed, 5 citations in OpenAlex.
- Chagas Disease Diagnosis withVaccines · 2024Article
- Antibody Engineering for Pursuing a Healthier Future.Frontiers in microbiology · 2017Review
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A fluorobody is a manmade hybrid molecule that is composed of green fluorescent protein (GFP) and a fragment of antibody, which combines the affinity and specificity of an antibody with the visibility of a GFP. It is able to provide a real-time indication of binding while avoiding the use of tags and secondary binding reagents. Here, the expression, purification and crystal structure of a recombinant fluorobody for TLH (thermolabile haemolysin), a toxin from the lethal food-borne disease bacterium Vibrio parahaemolyticus, are presented. This is the first structure of a fluorobody to be reported. Crystals belonging to space group P4(3)2(1)2, with unit-cell parameters a = b = 63.35, c = 125.90 Å, were obtained by vapour diffusion in hanging drops and the structure was refined to an Rfree of 16.7% at 1.5 Å resolution. The structure shows a CDR loop of the antibody on the GFP scaffold.
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