ArticleThe Journal of biological chemistry2010
Generation of a family-specific phage library of llama single chain antibody fragments that neutralize HIV-1.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers, 1 of them a synthesis that pooled it.
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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
24 citing papers in PubMed, 1 synthesis or guideline pooled it, 41 citations in OpenAlex.
- Research Progress and Applications of Multivalent, Multispecific and Modified Nanobodies for Disease Treatment.Frontiers in immunology · 2021Pooled it
- Review
- Nanobodies in the fight against infectious diseases: repurposing nature's tiny weapons.World journal of microbiology & biotechnology · 2024Review
- Structural basis for llama nanobody recognition and neutralization of HIV-1 at the CD4-binding site.Structure (London, England : 1993) · 2022Article
- Nanobodies that Neutralize HIV.Vaccines · 2019Review
- Selection of nanobodies with broad neutralizing potential against primary HIV-1 strains using soluble subtype C gp140 envelope trimers.Scientific reports · 2017Article
- Monoclonal Antibodies and Antibody Like Fragments Derived from Immunised Phage Display Libraries.Advances in experimental medicine and biology · 2017Review
- Inhibition of HIV Virus by Neutralizing Vhh Attached to Dual Functional Liposomes Encapsulating Dapivirine.Nanoscale research letters · 2016Article
- Hypoxia-Targeting Fluorescent Nanobodies for Optical Molecular Imaging of Pre-Invasive Breast Cancer.Molecular imaging and biology · 2016Article
- Nanobody-derived nanobiotechnology tool kits for diverse biomedical and biotechnology applications.International journal of nanomedicine · 2016Review
- Expression Cloning and Production of Human Heavy-Chain-Only Antibodies from Murine Transgenic Plasma Cells.Frontiers in immunology · 2016Article
- Fluorescent labelling of the actin cytoskeleton in plants using a cameloid antibody.Plant methods · 2014Article
- Article
- Preventive and therapeutic applications of neutralizing antibodies to Human Immunodeficiency Virus Type 1 (HIV-1).Therapeutic advances in vaccines · 2013Article
- A gp41 MPER-specific llama VHH requires a hydrophobic CDR3 for neutralization but not for antigen recognition.PLoS pathogens · 2013Article
- Article
- Straightforward selection of broadly neutralizing single-domain antibodies targeting the conserved CD4 and coreceptor binding sites of HIV-1 gp120.Journal of virology · 2013Article
- Potent and broad neutralization of HIV-1 by a llama antibody elicited by immunization.The Journal of experimental medicine · 2012Article
- Candidate antibody-based therapeutics against HIV-1.BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy · 2012Review
- Phages and HIV-1: from display to interplay.International journal of molecular sciences · 2012Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
11 authors at 3 institutions in 3 countries.
Funding
Abstract
Recently, we described llama antibody fragments (VHH) that can neutralize human immunodeficiency virus, type 1 (HIV-1). These VHH were obtained after selective elution of phages carrying an immune library raised against gp120 of HIV-1 subtype B/C CN54 with soluble CD4. We describe here a new, family-specific approach to obtain the largest possible diversity of related VHH that compete with soluble CD4 for binding to the HIV-1 envelope glycoprotein. The creation of this family-specific library of homologous VHH has enabled us to isolate phages carrying similar nucleotide sequences as the parental VHH. These VHH displayed varying binding affinities and neutralization phenotypes to a panel of different strains and subtypes of HIV-1. Sequence analysis of the homologs showed that the C-terminal three amino acids of the CDR3 loop were crucial in determining the specificity of these VHH for different subtype C HIV-1 strains. There was a positive correlation between affinity of VHH binding to gp120 of HIV-1 IIIB and the breadth of neutralization of diverse HIV-1 envelopes. The family-specific approach has therefore allowed us to better understand the interaction of the CD4-binding site antibodies with virus strain specificity and has potential use for the bioengineering of antibodies and HIV-1 vaccine development.
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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.