ArticleBio-protocol2022
Production and Crystallization of Nanobodies in Complex with the Receptor Binding Domain of the SARS-CoV-2 Spike Protein.
Article in Bio-protocol, 2022. 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 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.
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, 4 citations in OpenAlex.
- Parallelised Cloning, Mammalian Cell Expression, and Purification of Nanobodies Identified by Phage Display.Bio-protocol · 2026Article
- Cattle antibodies identify a cross-serotype broadly neutralising foot-and-mouth disease virus epitope.NPJ vaccines · 2026Article
- Crystal structure of Schistosoma mansoni cathepsin D1 in complex with a nanobody reveals the conformation of the propeptide-bound state.Acta crystallographica. Section D, Structural biology · 2026Article
- Heterohybridomas producing human immunoglobulin light chains using CD138-selected bone marrow cells.Biochemistry and biophysics reports · 2025Article
- Structural and functional characterization of nanobodies that neutralize Omicron variants of SARS-CoV-2.Open biology · 2024Article
- From Llama to Nanobody: A Streamlined Workflow for the Generation of Functionalised VHHs.Bio-protocol · 2024Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
The receptor binding domain (RBD) of the spike protein of SARS-CoV-2 binds angiotensin converting enzyme-2 (ACE-2) on the surface of epithelial cells, leading to fusion, and entry of the virus into the cell. This interaction can be blocked by the binding of llama-derived nanobodies (VHHs) to the RBD, leading to virus neutralisation. Structural analysis of VHH-RBD complexes by X-ray crystallography enables VHH epitopes to be precisely mapped, and the effect of variant mutations to be interpreted and predicted. Key to this is a protocol for the reproducible production and crystallization of the VHH-RBD complexes. Based on our experience, we describe a workflow for expressing and purifying the proteins, and the screening conditions for generating diffraction quality crystals of VHH-RBD complexes. Production and crystallization of protein complexes takes approximately twelve days, from construction of vectors to harvesting and freezing crystals for data collection.
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Registered trials
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