ArticleMethods in molecular biology (Clifton, N.J.)2022
Development of Antibody and Nanobody Tools for P2X7.
Article in Methods in molecular biology (Clifton, N.J.), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 8 citations in OpenAlex.
- The P2X7 receptor: insights from the murine monoclonal antibody clone L4.Purinergic signalling · 2026Review
- Methodological guidelines for P2X receptor assays and data interpretation.Cell death & disease · 2026Review
- Review
- ATP-Gated P2X7-Ion Channel on Kidney-Resident Natural Killer T Cells and Memory T Cells in Intrarenal Inflammation.Journal of the American Society of Nephrology : JASN · 2025Article
- Adeno-associated viral vectors encoding anti-P2X7 nanobodies reduce graft-versus-host disease in a humanised mouse model.Clinical & translational immunology · 2025Article
- Different localization of P2X4 and P2X7 receptors in native mouse lung - lack of evidence for a direct P2X4-P2X7 receptor interaction.Frontiers in immunology · 2024Article
- EU COST Action CA21130 PRESTO 'P2X receptors as therapeutic targets' inaugural meeting report.Purinergic signalling · 2023Article
- Animal Models for the Investigation of P2X7 Receptors.International journal of molecular sciences · 2023Review
- Evaluation of nanobody-based biologics targeting purinergic checkpoints in tumor modelsFrontiers in immunology · 2022Article
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Antibodies that recognize the ATP-gated P2X7 ion channel are etablished research tools. Nanobodies correspond to the antigen-binding variable immunoglobulin domain (VHH) of heavy chain antibodies that naturally occur in camelids. Nanobodies display better solubility than the variable domains (VH) of conventional antibodies. Therefore, it is much easier to construct bivalent and multivalent fusion proteins with nanobodies than with VH domains or with paired VH-VL domains. Moreover, nanobodies can bind functional crevices that are poorly accessbile to conventional VH-VL domains. This makes nanobodies particulary well suited as functional modulators. Here we provide protocols to raise antibodies and nanobodies against mouse and human P2X7 using cDNA-immunization. This approach evokes antibodies and nanobodies that recognize the P2X7 ion channel in native confirmation, some of which inhibit or potentiate gating of P2X7 by extracellular ATP. Furthermore, we developed protocols for producing P2X7-specific nanobodies and antibodies in vivo using rAAV vectors (AAVnano). This approach can be used either to durably inhibit or potentiate P2X7 function in vivo, or to deplete P2X7-expressing cells.
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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.