ArticleMolecular therapy. Oncology2025
A facile chemical strategy to synthesize precise AAV-protein conjugates for targeted gene delivery.
Article in Molecular therapy. Oncology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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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
8 citing papers in PubMed.
- Site-Specific Protein Bioconjugation Through Cellular Incorporation of Noncanonical Amino Acids.Angewandte Chemie (International ed. in English) · 2026Review
- An Expanded Toolbox for Versatile Chemical Editing of Adeno-Associated Virus.Angewandte Chemie (International ed. in English) · 2026Article
- Targeted delivery of genome editors in vivo.Nature biotechnology · 2026Review
- Site-Specific Chemical Conjugation of Recombinant Proteins onto the AAV Capsid.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Reprogramming AAV tropism with tumor-associated targeting ligands.Molecular therapy. Oncology · 2025Article
- Gene regulation technologies for gene and cell therapy.Molecular therapy : the journal of the American Society of Gene Therapy · 2025Review
- Strategies to Expand the Genetic Code of Mammalian Cells.Chemical reviews · 2025Review
- αFAP-specific nanobodies mediate a highly precise retargeting of modified AAV2 capsids thereby enabling specific transduction of tumor tissues.Molecular therapy. Methods & clinical development · 2024Article
Corrections and comments
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Authors and funding
8 authors.
Funding
Abstract
Current adeno-associated virus (AAV) gene therapies are limited by a lack of tissue-specificity, leading to toxic off-target impacts and increased therapeutic costs. More target-specific AAV vectors can offer safer and less expensive therapies. Antibody-like proteins can be used to retarget AAV vectors to unique cell-surface receptors. However, fusing such proteins onto the delicate AAV capsid proteins is complicated; only small and well-folded proteins are tolerated and the architecture of such fusions are highly restricted. Here, we report a versatile chemical strategy to covalently attach recombinant proteins onto the AAV capsid, using a combination of genetic code expansion (GCE) and bioorthogonal conjugation chemistry. This method is efficient, allows excellent control over the site of attachment, and the number of proteins attached on the AAV capsid. Systematic optimization of these parameters allowed us to generate highly active AAV2-anti-HER2 nanobody conjugates that significantly outperform their counterparts generated through genetic fusion. This conjugate exhibited excellent efficiency and selectivity toward HER2+ cancer cells both
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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.