ArticleJournal of molecular biology2010
Generation and characterization of a chimeric rabbit/human Fab for co-crystallization of HIV-1 Rev.
Article in Journal of molecular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 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.
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Who cites it
22 citing papers in PubMed, 33 citations in OpenAlex.
- PepINVENT: generative peptide design beyond natural amino acids.Chemical science · 2025Article
- New Anti-RSV Nucleoprotein Monoclonal Antibody Pairs Discovered Using Rabbit Phage Display Technology.Antibodies (Basel, Switzerland) · 2023Article
- Co-crystallization with diabodies: A case study for the introduction of synthetic symmetry.Structure (London, England : 1993) · 2021Article
- Affinity maturation, humanization, and co-crystallization of a rabbit anti-human ROR2 monoclonal antibody for therapeutic applications.The Journal of biological chemistry · 2020Article
- A Sortase A Programmable Phage Display Format for Improved Panning of Fab Antibody Libraries.Journal of molecular biology · 2018Article
- Structure of an RNA Aptamer that Can Inhibit HIV-1 by Blocking Rev-Cognate RNA (RRE) Binding and Rev-Rev Association.Structure (London, England : 1993) · 2018Article
- Chimeric rabbit/human Fab antibodies against the hepatitis Be-antigen and their potential applications in assays, characterization, and therapy.The Journal of biological chemistry · 2017Article
- Mining Naïve Rabbit Antibody Repertoires by Phage Display for Monoclonal Antibodies of Therapeutic Utility.Journal of molecular biology · 2017Article
- Article
- From rabbit antibody repertoires to rabbit monoclonal antibodies.Experimental & molecular medicine · 2017Review
- Cell-Permeable Peptides Containing Cycloalanine Residues.Angewandte Chemie (International ed. in English) · 2016Article
- The Structure of HIV-1 Rev Filaments Suggests a Bilateral Model for Rev-RRE Assembly.Structure (London, England : 1993) · 2016Article
- An overview of the lagomorph immune system and its genetic diversity.Immunogenetics · 2016Review
- Preparation and evaluation of human-murine chimeric antibody against protective antigen of Bacillus anthracis.International journal of molecular sciences · 2014Article
- A cell-penetrating antibody fragment against HIV-1 Rev has high antiviral activity: characterization of the paratope.The Journal of biological chemistry · 2014Article
- Generation and use of antibody fragments for structural studies of proteins refractory to crystallization.Methods in molecular biology (Clifton, N.J.) · 2014Article
- A macrocyclic peptide that serves as a cocrystallization ligand and inhibits the function of a MATE family transporter.Molecules (Basel, Switzerland) · 2013Article
- Cryo-EM study of Hepatitis B virus core antigen capsids decorated with antibodies from a human patient.Journal of structural biology · 2012Article
- Phages and HIV-1: from display to interplay.International journal of molecular sciences · 2012Review
- Therapeutic potential and challenges of targeting receptor tyrosine kinase ROR1 with monoclonal antibodies in B-cell malignancies.PloS one · 2011Article
Corrections and comments
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Authors and funding
11 authors at 5 institutions in 2 countries.
Funding
Abstract
Rev is a key regulatory protein of human immunodeficiency virus type 1. Its function is to bind to viral transcripts and effect export from the nucleus of unspliced mRNA, thereby allowing the synthesis of structural proteins. Despite its evident importance, the structure of Rev has remained unknown, primarily because Rev's proclivity for polymerization and aggregation is an impediment to crystallization. Monoclonal antibody antigen-binding domains (Fabs) have proven useful for the co-crystallization of other refractory proteins. In the present study, a chimeric rabbit/human anti-Rev Fab was selected by phage display, expressed in a bacterial secretion system, and purified from the media. The Fab readily solubilized polymeric Rev. The resulting Fab/Rev complex was purified by metal ion affinity chromatography and characterized by analytical ultracentrifugation, which demonstrated monodispersity and indicated a 1:1 molar stoichiometry. The Fab binds with very high affinity, as determined by surface plasmon resonance, to a conformational epitope in the N-terminal half of Rev. The complex forms crystals suitable for structure determination. The ability to serve as a crystallization aid is a new application of broad utility for chimeric rabbit/human Fab. The corresponding single-chain antibody (scFv) was also prepared, offering the potential of intracellular antibody therapeutics against human immunodeficiency virus type 1.
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Registered trials
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.